|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-220 |
4.24e-103 |
|
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: 297.09 E-value: 4.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDRYR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNV 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 162 DLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
7.37e-93 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 271.53 E-value: 7.37e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---L 77
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 DRYRNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARAL 157
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHR-PSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-221 |
5.06e-68 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 208.37 E-value: 5.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKI---GLDRY 80
Cdd:COG2884 1 MIRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RnQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCN 160
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDK-AKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLElVDRMPKRVLELEDGRLV 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-221 |
1.32e-66 |
|
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: 204.98 E-value: 1.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLD--- 78
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKvqNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARALS 158
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPA-QLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
5.04e-66 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 204.55 E-value: 5.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRy 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 rnqnvSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARALSCN 160
Cdd:COG1116 83 -----GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAY-PHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEvakksdrAVYLS 216
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvDE-------AVFLA 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-221 |
5.84e-63 |
|
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: 195.38 E-value: 5.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnqn 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 vSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03293 76 -GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPH-QLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSqevakkSDRAVYLSKKKLV 221
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD------IDEAVFLADRVVV 204
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-222 |
3.69e-57 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 180.63 E-value: 3.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDRY 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSsneRAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARALSCN 160
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPS-ELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLVV 222
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-221 |
2.88e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.10 E-value: 2.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYesnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDR 79
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 YRnQNVSVIFQSYNLITYMTALQNVLTAM--EITGVKV------QNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRV 151
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNVLAGRlgRTSTWRSllglfpPEDRERALEALERVGLADKAYQR-ADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-221 |
5.06e-56 |
|
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: 178.15 E-value: 5.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKnvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQ- 83
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 -NVSVIFQSYNLITYMTALQNVLTAM--EITGVKV------QNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIA 154
Cdd:cd03256 78 rQIGMIFQQFNLIERLSVLENVLSGRlgRRSTWRSlfglfpKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 155 RALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-221 |
8.59e-56 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 185.11 E-value: 8.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKN-VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRY 80
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKGgVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RN--QNVSVIFQSYN--LITYMTALQNVLTAMEITGV-KVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIAR 155
Cdd:COG1123 338 RElrRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-221 |
1.59e-55 |
|
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: 176.17 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESngknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQN 84
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQ-EVAKKSDRAVYLSKKKLV 221
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQeEALALADRIAVMNEGRIV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-221 |
1.62e-55 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 176.62 E-value: 1.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRN- 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 -QNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNV 161
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLED-KADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 162 DLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-221 |
3.93e-55 |
|
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: 175.60 E-value: 3.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:COG1122 77 VGLVFQNPdDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDlDLVAELADRVIVLDDGRIV 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-221 |
1.46e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.79 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKiGLDRYRnQN 84
Cdd:COG1131 1 IEVRGLTKRY---GDKTA-LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVR-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYlEEAERLCDRVAIIDKGRIV 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-221 |
6.02e-53 |
|
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: 170.56 E-value: 6.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRN- 82
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 -QNVSVIFQSYNLITYMTALQNVLTAM--------EITGVKVQNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAI 153
Cdd:TIGR02315 78 rRRIGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQR-ADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
6.28e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.34 E-value: 6.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI---RKIGLDRY 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RnQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaeaKRNVL--QLSGGQQQRVAIARALS 158
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSD---KADAYpsQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-211 |
1.31e-52 |
|
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: 169.22 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG--LDRYR 81
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NQNVSVIFQ-SYN-LITYMTALQNVLTAMEI--TGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARAL 157
Cdd:cd03257 81 RKEIQMVFQdPMSsLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDR 211
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADR 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-204 |
1.81e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 172.59 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESngknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI-------R 73
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 KIGLdryrnqnvsvIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAI 153
Cdd:COG3842 78 NVGM----------VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGL-ADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 154 ARALSCNVDLLIADEPTGNLD----EQTAMDIIELFQELahkeNKCIIVVTHSQE 204
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQREL----GITFIYVTHDQE 197
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-206 |
5.81e-52 |
|
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: 167.04 E-value: 5.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI-----RKIGLD 78
Cdd:TIGR02673 1 MIEFHNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlrgRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RyrnQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:TIGR02673 78 R---RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEH-KADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQEVA 206
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLV 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-219 |
1.53e-51 |
|
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: 165.72 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYesNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQNV 85
Cdd:cd03225 1 ELKNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR-RKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 86 SVIFQSYNL-ITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKK 219
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
19-215 |
3.23e-51 |
|
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: 164.71 E-value: 3.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 19 KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG----LDRYRNQnVSVIFQSYNL 94
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNskkaSKFRREK-LGYLFQNFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 95 ITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD 174
Cdd:TIGR03608 88 IENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKL-KQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446370010 175 EQTAMDIIELFQELAhKENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:TIGR03608 167 PKNRDEVLDLLLELN-DEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-215 |
4.19e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 165.55 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSlgC--GLDVPKNGYVLYNGKDI--RKIGLDR 79
Cdd:COG1126 1 MIEIENLHKSF---GDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLR--CinLLEEPDSGTITVDGEDLtdSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 YRnQNVSVIFQSYNLITYMTALQNVLTAMeitgVKVQNKT-----ARALQLLERVGLSEaeaKRNVL--QLSGGQQQRVA 152
Cdd:COG1126 75 LR-RKVGMVFQQFNLFPHLTVLENVTLAP----IKVKKMSkaeaeERAMELLERVGLAD---KADAYpaQLSGGQQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTH----SQEVAkksDRAVYL 215
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHemgfAREVA---DRVVFM 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-220 |
3.63e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.29 E-value: 3.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYyyESNGKNvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:COG4619 1 LELEGLSF--RVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITyMTALQNVLTAMEITGVKVQnkTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKL 220
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-221 |
4.98e-50 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 162.50 E-value: 4.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkiGLDRYRNQ 83
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELH--GASKKQLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 ----NVSVIFQSYNLITYMTALQNVLTAMEI-TGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:TIGR02982 79 qlrrRIGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGL-GDHLNYYPHNLSGGQKQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-217 |
1.01e-49 |
|
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: 161.16 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesnGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI--RKIGLDRYRn 82
Cdd:cd03262 1 IEIKNLHKSF---GDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSYNLITYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARALSCNV 161
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPA-QLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 162 DLLIADEPTGNLDEQTAMDIIELFQELAHkENKCIIVVTHSQEVAKK-SDRAVYLSK 217
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREvADRVIFMDD 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-206 |
2.97e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 161.57 E-value: 2.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METiLQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRy 80
Cdd:COG4525 1 MSM-LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 rnqnvSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCN 160
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADF-ARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVA 206
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
7.70e-49 |
|
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: 167.00 E-value: 7.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYEsnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKN----GYVLYNGKDIRKIG 76
Cdd:COG1123 1 MTPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGgrisGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 lDRYRNQNVSVIFQSYnlityMTALqNVLT-------AMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQ 149
Cdd:COG1123 78 -EALRGRRIGMVFQDP-----MTQL-NPVTvgdqiaeALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGRIV 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-224 |
8.56e-49 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 160.02 E-value: 8.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigLDRYRNQN 84
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLVVNE 224
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHImQEVEALCDRVVILHKGKVVAQG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
1.58e-48 |
|
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: 158.99 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---L 77
Cdd:COG1127 2 SEPMIEVRNLTKSF---GDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 DRYRnQNVSVIFQSYNLITYMTALQNVLTAM-EITGVKVQNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARA 156
Cdd:COG1127 78 YELR-RRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPS-ELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-213 |
2.26e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 158.44 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLD---RY 80
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCN 160
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAV 213
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-215 |
1.72e-47 |
|
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: 154.27 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI-RKIGLDRYRNQ 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVltameitgvkvqnktaralqllervglseaeakrnVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENI-----------------------------------ALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYL 215
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVL 174
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-215 |
1.79e-47 |
|
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: 158.68 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTT-LSLgCGLdVPKNGY----VLYNGKDIRKIG-- 76
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAI-LGL-LPPPGItsgeILFDGEDLLKLSek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 -LDRYRNQNVSVIFQSYnlityMTALQNVLT-------AMEI-TGVKVQNKTARALQLLERVGLSEAEAkrnVL-----Q 142
Cdd:COG0444 79 eLRKIRGREIQMIFQDP-----MTSLNPVMTvgdqiaePLRIhGGLSKAEARERAIELLERVGLPDPER---RLdryphE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 143 LSGGQQQRVAIARALSCNVDLLIADEPTgnldeqTAMD------IIELFQELAHKENKCIIVVTHSQEVAKK-SDR-AV- 213
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPT------TALDvtiqaqILNLLKDLQRELGLAILFITHDLGVVAEiADRvAVm 224
|
..
gi 446370010 214 YL 215
Cdd:COG0444 225 YA 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-221 |
4.54e-47 |
|
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: 155.73 E-value: 4.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYnlitY------MTALQNVLTAMEITGVKvqNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:COG1124 81 VQMVFQDP----YaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
23-221 |
4.80e-46 |
|
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: 152.39 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIrkIGLDRYRnQNVSVIFQSYNLITYMTALQ 102
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHK-RPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDII 182
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 183 ELFQELAHKENKCIIVVTHSQEVA-KKSDRAVYLSKKKLV 221
Cdd:cd03300 171 LELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQ 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-220 |
1.25e-45 |
|
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: 151.02 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI-----RKIGLDR 79
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 yrnQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaeaKRNVL--QLSGGQQQRVAIARAL 157
Cdd:cd03292 78 ---RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSH---KHRALpaELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKL 220
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKElVDTTRHRVIALERGKL 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-221 |
4.10e-45 |
|
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: 150.02 E-value: 4.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGL-----DVPKNGYVLYNGKDIRKIGLDR 79
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 Y--RNQnVSVIFQSYNLITyMTALQNVLTAMEITGVKVQNKT-ARALQLLERVGLSEAEAKR-NVLQLSGGQQQRVAIAR 155
Cdd:cd03260 77 LelRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENkcIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT--IVIVTHNmQQAARVADRTAFLLNGRLV 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-221 |
4.76e-45 |
|
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: 149.96 E-value: 4.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK---IGLDRYR 81
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NqNVSVIFQSYNLITYMTALQNV---------LTAMEITgvkvqnktARALQLLERVGLSEAEAKRnVLQLSGGQQQRVA 152
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVafplrehtrLSEEEIR--------EIVLEKLEAVGLRGAEDLY-PAELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
5.73e-45 |
|
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: 150.19 E-value: 5.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLdRYRNQ 83
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR-RELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVL-------TAMEITGVKVQNKTARALqllERVGLsEAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVAlgryphlGLFGRPSAEDREAVEEAL---ERTGL-EHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH--SQeVAKKSDRAVYLSKKKLV 221
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHdlNL-AARYADRLVLLKDGRIV 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-221 |
1.46e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.01 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTT---TLSLgcgLDVPKNG--------YVLYNGKDIR 73
Cdd:PRK11124 3 IQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSllrVLNL---LEMPRSGtlniagnhFDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 KIGLDRyrnQNVSVIFQSYNLITYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVA 152
Cdd:PRK11124 76 AIRELR---RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-222 |
4.12e-44 |
|
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: 147.83 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVailENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAE-AKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLVV 222
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQ 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
8.60e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.16 E-value: 8.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYEsngkNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI----RKIG 76
Cdd:COG1121 3 MMPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPrrarRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 ldrYRNQNVSVifqsyNLITYMTALQNVltAMEITG----VKVQNKT--ARALQLLERVGLSEAeAKRNVLQLSGGQQQR 150
Cdd:COG1121 79 ---YVPQRAEV-----DWDFPITVRDVV--LMGRYGrrglFRRPSRAdrEAVDEALERVGLEDL-ADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 151 VAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKL 220
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-170 |
9.71e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 143.94 E-value: 9.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQNVSVIFQSYNLITYMTALQN 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR-KEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEITGVKVQNKTARALQLLERVGLSEAEAKR---NVLQLSGGQQQRVAIARALSCNVDLLIADEPT 170
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-220 |
1.01e-43 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 146.02 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI------RKIGL 77
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnlsysQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 dryRNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARAL 157
Cdd:NF038007 81 ---RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGI-DNRRNHKPMQLSGGQQQRVAIARAM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:NF038007 157 VSNPALLLADEPTGNLDSKNARAVLQQLKYI-NQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-221 |
1.88e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.31 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNG--------YVLYNGKDIRKIG 76
Cdd:COG4161 3 IQLKNINCFYGSH----QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlniaghqFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 LDRyrnQNVSVIFQSYNLITYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIAR 155
Cdd:COG4161 79 LLR---QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKEnkcI--IVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTG---ItqVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-220 |
6.12e-43 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 143.83 E-value: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYesNGKNvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigldryRNQNV 85
Cdd:cd03235 1 EVEDLTVSY--GGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK------ERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 86 SVIFQSYNLITYM--TALQNVLTAM--EITGVKVQNKT--ARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSC 159
Cdd:cd03235 71 GYVPQRRSIDRDFpiSVRDVVLMGLygHKGLFRRLSKAdkAKVDEALERVGLSEL-ADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKL 220
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDlGLVLEYFDRVLLLNRTVV 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-204 |
2.59e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 146.37 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsngkNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIrkIGL---DRyr 81
Cdd:COG3839 4 LELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLppkDR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 nqNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNV 161
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446370010 162 DLLIADEPTGNLD----EQTAMDIIELFQELahkeNKCIIVVTHSQE 204
Cdd:COG3839 153 KVFLLDEPLSNLDaklrVEMRAEIKRLHRRL----GTTTIYVTHDQV 195
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-221 |
1.03e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.59 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKN-VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI---RKIGLDRY 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RnQNVSVIFQ--SYNL--------ITYmtALQNV-LTAMEITgvkvqnktARALQLLERVGLSEAEAKRNVLQLSGGQQQ 149
Cdd:TIGR04521 81 R-KKVGLVFQfpEHQLfeetvykdIAF--GPKNLgLSEEEAE--------ERVKEALELVGLDEEYLERSPFELSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-221 |
1.28e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 144.17 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKI---GLDRYRn 82
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaeaKRNVL--QLSGGQQQRVAIARALSCN 160
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSD---KADRYpaQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-219 |
1.44e-41 |
|
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: 139.06 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR-KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITyMTALQNVltameitgvkvqnktaralqllervglseaeakrnvlqLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03228 78 IAYVPQDPFLFS-GTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKK 219
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-221 |
2.43e-41 |
|
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: 148.83 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:COG2274 474 IELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSyNLITYMTALQNV-LTAMEITgvkvqnkTARALQLLERVGLSE-------------AEAKRNvlqLSGGQQQR 150
Cdd:COG2274 551 IGVVLQD-VFLFSGTIRENItLGDPDAT-------DEEIIEAARLAGLHDfiealpmgydtvvGEGGSN---LSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 151 VAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHkeNKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-221 |
2.56e-41 |
|
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: 138.72 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLdRYRNQNVSV 87
Cdd:cd03214 3 ENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP-KELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IfqsynlitymtalqnvltameitgvkvqnktaraLQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDLLIAD 167
Cdd:cd03214 78 V----------------------------------PQALELLGLAH-LADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 168 EPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
24-221 |
4.91e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.28 E-value: 4.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI--------RKIGLdryrnqnvsvIFQSYNLI 95
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlppreRRVGF----------VFQHYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 96 TYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDE 175
Cdd:COG1118 88 PHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446370010 176 QTAMDIIELFQELaHKENKCIIV-VTHSQE----VAkksDRAVYLSKKKLV 221
Cdd:COG1118 167 KVRKELRRWLRRL-HDELGGTTVfVTHDQEealeLA---DRVVVMNQGRIE 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-220 |
1.02e-39 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 136.31 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLdryRNQNVSVIFQSYNLITYMTALQN 103
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEITGVKV----QNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAM 179
Cdd:cd03296 95 VAFGLRVKPRSErppeAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446370010 180 DIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKL 220
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-221 |
1.07e-39 |
|
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: 137.39 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 14 YESNGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDRYRNQNVSVIFQ 90
Cdd:cd03294 31 LKKTGQTVGV-NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 91 SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPT 170
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 171 GNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-220 |
1.84e-39 |
|
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: 133.68 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqn 84
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNvltameitgvkvqnktaralqllervglseaeakrnvLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03230 75 IGYLPEEPSLYENLTVREN-------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKL 220
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-216 |
3.09e-39 |
|
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: 134.14 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqnVSVIFQSYNLITYMTALQ 102
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAMEITGVKVQnkTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTamdiI 182
Cdd:COG4133 95 NLRFWAALYGLRAD--REAIDEALEAVGLAGLADLP-VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG----V 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 446370010 183 ELFQEL--AHKENKCIIVVTHSQEVAKKSDRAVYLS 216
Cdd:COG4133 168 ALLAELiaAHLARGGAVLLTTHQPLELAAARVLDLG 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-221 |
3.29e-39 |
|
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: 141.82 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQ-SYnlITYMTALQNV-LTAMEITGVKVQnktaralQLLERVGLSE-------------AEAKRNvlqLSGGQQQ 149
Cdd:COG4988 413 IAWVPQnPY--LFAGTIRENLrLGRPDASDEELE-------AALEAAGLDEfvaalpdgldtplGEGGRG---LSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHkeNKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
23-215 |
3.37e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 135.70 E-value: 3.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSlgC--GLDVPKNGYVLYNGKDIR----KIG---------LDRYRnQNVSV 87
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLR--CinLLETPDSGEIRVGGEEIRlkpdRDGelvpadrrqLQRIR-TRLGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQSYNLITYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEaeaKRNVL--QLSGGQQQRVAIARALSCNVDLL 164
Cdd:COG4598 100 VFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLAD---KRDAYpaHLSGGQQQRAAIARALAMEPEVM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYL 215
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDLA-EEGRTMLVVTHEMGFARDvSSHVVFL 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-223 |
3.41e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 142.56 E-value: 3.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLS-LGCgLDVPKNGYVLYNGKDIRKIGLD- 78
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNiLGC-LDKPTSGTYRVAGQDVATLDADa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 --RYRNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARA 156
Cdd:PRK10535 80 laQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPS-QLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTA---MDIIELFQELAHKenkcIIVVTHSQEVAKKSDRAVYLSKKKLVVN 223
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGeevMAILHQLRDRGHT----VIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-220 |
6.88e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 134.14 E-value: 6.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKI---GLD 78
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-206 |
9.26e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 134.44 E-value: 9.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYEsnGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnq 83
Cdd:PRK11248 1 MLQISHLYADYG--GKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 nvSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:PRK11248 73 --GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVA 206
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-221 |
2.61e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 134.45 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYesNGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI---------RKIG 76
Cdd:COG1125 3 EFENVTKRY--PDGTVAV-DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIrdldpvelrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 ldrYrnqnvsVIfQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAE-AKRNVLQLSGGQQQRVAIAR 155
Cdd:COG1125 80 ---Y------VI-QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDiDEALKLGDRIAVMREGRIV 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-223 |
3.00e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.91 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLD-RYRN 82
Cdd:PRK09493 1 MIEFKNVSKHF---GPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSYNLITYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNV 161
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 162 DLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLVVN 223
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-221 |
3.03e-38 |
|
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: 132.46 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQNVSVIFQSYNLITYMTALQN 103
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIE 183
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 446370010 184 LFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03299 171 ELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-213 |
8.28e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 135.07 E-value: 8.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrn 82
Cdd:PRK09452 13 PLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVD 162
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEF-AQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446370010 163 LLIADEPTGNLDEQ--TAMDiIELFQeLAHKENKCIIVVTHSQEVA-KKSDRAV 213
Cdd:PRK09452 165 VLLLDESLSALDYKlrKQMQ-NELKA-LQRKLGITFVFVTHDQEEAlTMSDRIV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-215 |
9.50e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.03 E-value: 9.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESngknvailENVNFSFQ--KGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrn 82
Cdd:COG3840 2 LRLDDLTYRYGD--------FPLRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSYNLITYMTALQNV---------LTAMEItgvkvqnktARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAI 153
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIglglrpglkLTAEQR---------AQVEQALERVGLAGLL-DRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 154 ARALSCNVDLLIADEPTGNLDeqTAM--DIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYL 215
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALD--PALrqEMLDLVDELCRERGLTVLMVTHDpEDAARIADRVLLV 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-215 |
1.36e-37 |
|
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: 128.52 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQnV 85
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 86 SVIFQsynlitymtalqnvltameitgvkvqnktaralqllervglseaeakrnvlqLSGGQQQRVAIARALSCNVDLLI 165
Cdd:cd00267 76 GYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446370010 166 ADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIV 152
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-213 |
2.11e-37 |
|
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: 133.24 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsngkNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQN 84
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK---RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVlQLSGGQQQRVAIARALSCNVDLL 164
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPG-QLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVA-KKSDRAV 213
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIV 206
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-221 |
3.59e-37 |
|
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: 130.11 E-value: 3.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTL-SLGCGLDVPKN----GYVLYNGKDI--RKIG 76
Cdd:TIGR00972 1 AIEIENLNLFY---GEKEA-LKNINLDIPKNQVTALIGPSGCGKSTLLrSLNRMNDLVPGvrieGKVLFDGQDIydKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 LDRYRnQNVSVIFQSYNLITyMTALQNVLTAMEITGVKVQNK-TARALQLLERVGLSEA---EAKRNVLQLSGGQQQRVA 152
Cdd:TIGR00972 77 VVELR-RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKElDEIVEESLKKAALWDEvkdRLHDSALGLSGGQQQRLC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNmQQAARISDRTAFFYDGELV 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-216 |
6.15e-37 |
|
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: 129.12 E-value: 6.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYrnqnvsVIFQSYNLITYMTALQN 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM------VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEITGVKVQNKTARAL--QLLERVGLSEAEAKRnVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDI 181
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKR-PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 446370010 182 IELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLS 216
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLT 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-201 |
7.85e-37 |
|
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: 134.81 E-value: 7.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKT-TTLSLgCGLdVPKN-----GYVLYNGKDIRK 74
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSI-LRL-LPDPaahpsGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IG---LDRYRNQNVSVIFQSYnlityMTALQNVLTA----MEI----TGVKVQNKTARALQLLERVGLSEAEAKRNVL-- 141
Cdd:COG4172 81 LSereLRRIRGNRIAMIFQEP-----MTSLNPLHTIgkqiAEVlrlhRGLSGAAARARALELLERVGIPDPERRLDAYph 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 142 QLSGGQQQRVAIARALSCNVDLLIADEPTgnldeqTAMD------IIELFQELAHKENKCIIVVTH 201
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPT------TALDvtvqaqILDLLKDLQRELGMALLLITH 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-221 |
2.04e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.99 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLdryRNQNVSVIFQSYNLITY 97
Cdd:PRK11432 17 GSNTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI---QQRDICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 98 MTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFE-DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 178 AMDIIELFQELAHKENKCIIVVTHSQ-EVAKKSDRAVYLSKKKLV 221
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQsEAFAVSDTVIVMNKGKIM 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-221 |
2.33e-36 |
|
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: 134.12 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:COG4987 334 LELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR-RR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLItYMTALQNVLTAmeitgvkvqNKTA---RALQLLERVGLSE-AEAKRNVL---------QLSGGQQQRV 151
Cdd:COG4987 411 IAVVPQRPHLF-DTTLRENLRLA---------RPDAtdeELWAALERVGLGDwLAALPDGLdtwlgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-206 |
4.15e-36 |
|
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: 126.22 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsngkNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG-LDRyrnq 83
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKDR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:cd03301 73 DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446370010 164 LIADEPTGNLD----EQTAMDIIELFQELahkeNKCIIVVTHSQEVA 206
Cdd:cd03301 152 FLMDEPLSNLDaklrVQMRAELKRLQQRL----GTTTIYVTHDQVEA 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-221 |
5.81e-36 |
|
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: 129.15 E-value: 5.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNK 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL---RHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 119 TARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD----EQTAMDIIELFQELAhkenK 194
Cdd:TIGR01187 78 KPRVLEALRLVQLEEF-ADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQLG----I 152
|
170 180
....*....|....*....|....*...
gi 446370010 195 CIIVVTHSQEVA-KKSDRAVYLSKKKLV 221
Cdd:TIGR01187 153 TFVFVTHDQEEAmTMSDRIAIMRKGKIA 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
6.13e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.08 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTL-SL--------GCGLDvpknGYVLYNGKD 71
Cdd:COG1117 8 LEPKIEVRNLNVYY---GDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLrCLnrmndlipGARVE----GEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 72 IRKIGLD----RYRnqnVSVIFQSYNLITyMTALQNVLTAMEITGVKvqNKT---ARALQLLERVGLSEaEAK----RNV 140
Cdd:COG1117 80 IYDPDVDvvelRRR---VGMVFQKPNPFP-KSIYDNVAYGLRLHGIK--SKSeldEIVEESLRKAALWD-EVKdrlkKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 141 LQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHS-QEVAKKSDRAVYLSKKK 219
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNmQQAARVSDYTAFFYLGE 230
|
..
gi 446370010 220 LV 221
Cdd:COG1117 231 LV 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-220 |
6.14e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.39 E-value: 6.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR---------------KIGLDRYRnqnVSV 87
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLLRTR---LTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQSYNLITYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIA 166
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 167 DEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKL 220
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-217 |
4.93e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.12 E-value: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 20 NVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIgldRYRNQNVSVIFQSYNLITYMT 99
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 100 ALQNVltAMEITGVKVQNKTARA------LQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:PRK10851 91 VFDNI--AFGLTVLPRRERPNAAaikakvTQLLEMVQLAHL-ADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446370010 174 DEQTAMDIIELFQELaHKENKCIIV-VTHSQEVAKK-SDRAVYLSK 217
Cdd:PRK10851 168 DAQVRKELRRWLRQL-HEELKFTSVfVTHDQEEAMEvADRVVVMSQ 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-221 |
1.44e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 122.68 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDR--YRNQNVSVIFQSYNLITYMTAL 101
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpFLRRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 102 QNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDI 181
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLD-KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446370010 182 IELFQELaHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK10908 177 LRLFEEF-NRVGVTVLMATHDIGlISRRSYRMLTLSDGHLH 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-221 |
2.02e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI-------RKIGLDRYRNQNVSVIFQSYNLI 95
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 96 TYMTALQNVLTA-MEITGVKVQNKTARALQLLERVGLSEAE---AKRnvlqLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:PRK11264 98 PHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKEtsyPRR----LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446370010 172 NLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-221 |
2.29e-33 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 119.40 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYesnGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqnVSV 87
Cdd:cd03265 4 ENLVKKY---GDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR--IGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIAD 167
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 168 EPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRII 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-221 |
3.59e-33 |
|
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: 118.76 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKiglDRYR-NQ 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA--VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKAaRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-215 |
4.68e-33 |
|
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: 119.08 E-value: 4.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQNVSVIFQSYNLITYMTALQN 103
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAME------ITGVKVQNK----TARALQLLERVGLSEaeaKRNVL--QLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:cd03219 96 VMVAAQartgsgLLLARARREereaRERAEELLERVGLAD---LADRPagELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 172 NLDEQTAMDIIELFQELAHKeNKCIIVVTHSQEVAKK-SDRAVYL 215
Cdd:cd03219 173 GLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSlADRVTVL 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-221 |
5.07e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 119.84 E-value: 5.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNG---------KDIRki 75
Cdd:TIGR04520 1 IEVENVSFSYPESEKPA--LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeenlWEIR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 gldryrnQNVSVIFQS-YNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIA 154
Cdd:TIGR04520 77 -------KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDF-RDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 155 RALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-204 |
5.36e-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: 119.42 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLY-----NGK----DI 72
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerRGGedvwEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 73 RK-IGLdryrnqnVSVIFQSYnLITYMTALQNVLTA--------MEITgvkvQNKTARALQLLERVGLSEaEAKRNVLQL 143
Cdd:COG1119 77 RKrIGL-------VSPALQLR-FPRDETVLDVVLSGffdsiglyREPT----DEQRERARELLELLGLAH-LADRPFGTL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 144 SGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE 204
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE 204
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
24-206 |
6.68e-33 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 121.34 E-value: 6.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQNVSVIFQSYNLITYMTALQN 103
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK---RGIAYVYQNYMLFPHKTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIE 183
Cdd:NF040840 93 IAFGLKLRKVPKEEIERKVKEIMELLGISHL-LHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171
|
170 180
....*....|....*....|...
gi 446370010 184 LFQELAHKENKCIIVVTHSQEVA 206
Cdd:NF040840 172 EMKRWHREFGFTAIHVTHNFEEA 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-221 |
1.34e-32 |
|
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: 116.97 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 14 YESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigLDRYRN-----QNVSvi 88
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--KERRKSigyvmQDVD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 89 fqsYNLITyMTALQNVLTAMEITGvkvqNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADE 168
Cdd:cd03226 82 ---YQLFT-DSVREELLLGLKELD----AGNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 169 PTGNLDEQtAMDII-ELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03226 153 PTSGLDYK-NMERVgELIRELA-AQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-221 |
3.09e-32 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 116.70 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnq 83
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRR-VGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-221 |
3.32e-31 |
|
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: 113.47 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKiglDRYRNQNVSVIFQSYNLITY 97
Cdd:cd03268 12 KKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK---NIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 98 MTALQNVLTAMEITGVkvqnKTARALQLLERVGLSeAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:cd03268 87 LTARENLRLLARLLGI----RKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 178 AMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03268 162 IKELRELILSLR-DQGITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-221 |
6.02e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 20 NVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGL-----DVPKNGYVLYNGKDIRKIGLDRYRnQNVSVIFQSYNL 94
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELR-RRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 95 ITYMTALQNVLTAMEITGVkVQNKT---ARALQLLERVGLSEAEAKR---NVLQLSGGQQQRVAIARALSCNVDLLIADE 168
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRL-VKSKKelqERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446370010 169 PTGNLDEQTAMDIIELFQELahKENKCIIVVTH-SQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK14247 173 PTANLDPENTAKIESLFLEL--KKDMTIVLVTHfPQQAARISDYVAFLYKGQIV 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-222 |
6.71e-31 |
|
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: 113.07 E-value: 6.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGL-DRYRN- 82
Cdd:cd03245 3 IEFRNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPaDLRRNi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 ----QNVSVIFQS-YNLITYMTAL---QNVLTAMEITGV-KVQNKTARALQLleRVGlseaEAKRNvlqLSGGQQQRVAI 153
Cdd:cd03245 81 gyvpQDVTLFYGTlRDNITLGAPLaddERILRAAELAGVtDFVNKHPNGLDL--QIG----ERGRG---LSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKKLVV 222
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-201 |
6.92e-31 |
|
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: 113.98 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkiGLDRY 80
Cdd:COG0411 1 SDPLLEVRGLTKRF---GGLVA-VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT--GLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 R--NQNVSVIFQSYNLITYMTALQNVLTAMEI-TGVKVQNK--------------TARALQLLERVGLsEAEAKRNVLQL 143
Cdd:COG0411 75 RiaRLGIARTFQNPRLFPELTVLENVLVAAHArLGRGLLAAllrlprarreereaRERAEELLERVGL-ADRADEPAGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 144 SGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
7.25e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 115.33 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKN-VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYV----LYNGKDIRKIGLD 78
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENeLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQN-----------VSVIFQ--SYNLITyMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSG 145
Cdd:PRK13631 101 TNPYSKkiknfkelrrrVSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 146 GQQQRVAIARALSCNVDLLIADEPTGNLD---EQTAMDIIelfqELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLI----LDAKANNKTVFVITHTMEhVLEVADEVIVMDKGKIL 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-204 |
7.64e-31 |
|
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: 112.77 E-value: 7.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 26 NVNFSFQ-KGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNG-------KDI------RKIGLdryrnqnvsvIFQS 91
Cdd:cd03297 14 TLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKInlppqqRKIGL----------VFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 92 YNLITYMTALQNVLTAMEITGVKVQnkTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNRED--RISVDELLDLLGLDHLL-NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|...
gi 446370010 172 NLDEQTAMDIIELFQELAHKENKCIIVVTHSQE 204
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLS 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
1.54e-30 |
|
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: 117.77 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:TIGR02857 322 LEFSGVSVAYP--GRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSyNLITYMTALQNVLTAM-EITGVKVQnktaralQLLERVGLSEAEAKR----------NVLQLSGGQQQRVAI 153
Cdd:TIGR02857 398 IAWVPQH-PFLFAGTIAENIRLARpDASDAEIR-------EALERAGLDEFVAALpqgldtpigeGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
2.26e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.16 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqNV 85
Cdd:PRK13632 9 KVENVSFSYPNSENNA--LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK-KI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 86 SVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:PRK13632 86 GIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDY-LDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-201 |
3.13e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.19 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:COG1132 340 IEFENVSFSYP-GDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITyMTALQNV-LTAMEITGVKVQnKTARALQLLERV-----GLsEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:COG1132 416 IGVVPQDTFLFS-GTIRENIrYGRPDATDEEVE-EAAKAAQAHEFIealpdGY-DTVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTH 201
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAH 533
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-221 |
4.09e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.26 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK---------------IGLDRYRN------ 82
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekvleklvIQKTRFKKikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 --QNVSVIFQ--SYNLITyMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:PRK13651 103 irRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDlDNVLEWTKRTIFFKDGKII 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-221 |
7.26e-30 |
|
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: 110.28 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 30 SFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQNVSVIFQSYNLITYMTALQNVLTAMe 109
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENNLFAHLTVEQNVGLGL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 110 ITGVKVQNKTARALQ-LLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQEL 188
Cdd:cd03298 96 SPGLKLTAEDRQAIEvALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....
gi 446370010 189 AHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-216 |
1.26e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQ 83
Cdd:PRK10247 7 LLQLQNVGYLAGDA----KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 nVSVIFQSYNLITyMTALQNVLTAMEITGVKVQNKtaRALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:PRK10247 83 -VSYCAQTPTLFG-DTVYDNLIFPWQIRNQQPDPA--IFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLS 216
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-221 |
1.95e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 110.67 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYESNGKN-----VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKI-- 75
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 -GLDRYRnQNVSVIFQ-SYNLIT-YMTALQNVLTAME-ITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRV 151
Cdd:TIGR02769 81 kQRRAFR-RDVQLVFQdSPSAVNpRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-220 |
2.19e-29 |
|
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: 107.69 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:cd03246 1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 vsvifqsynlITYMtaLQNVltameitgvkvqnktaralQLLErvGlSEAEakrNVlqLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03246 78 ----------VGYL--PQDD-------------------ELFS--G-SIAE---NI--LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-221 |
5.65e-29 |
|
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: 107.66 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesnGKNVAiLENVNFSFQKGhFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK--------IG 76
Cdd:cd03264 1 LQLENLTKRY---GKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpqklrrrIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 ldrYRNQNVSVI--FQSYNLITYMTALQnvltameitGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIA 154
Cdd:cd03264 76 ---YLPQEFGVYpnFTVREFLDYIAWLK---------GIPSKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 155 RALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-206 |
9.28e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.08 E-value: 9.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYEsnGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIglDRYRnQ 83
Cdd:PRK11607 19 LLEIRNLTKSFD--GQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQ-R 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEF-AKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446370010 164 LIADEPTGNLDEQ-------TAMDIIElfqelahKENKCIIVVTHSQEVA 206
Cdd:PRK11607 171 LLLDEPMGALDKKlrdrmqlEVVDILE-------RVGVTCVMVTHDQEEA 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-221 |
1.10e-28 |
|
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: 107.70 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYEsngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQnV 85
Cdd:cd03254 4 EFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 86 SVIFQSynliTYM---TALQNVLTAMEITGVKVQNKTARALQLLERV-----GLsEAEAKRNVLQLSGGQQQRVAIARAL 157
Cdd:cd03254 80 GVVLQD----TFLfsgTIMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGY-DTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-221 |
2.00e-28 |
|
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: 109.81 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIrkigLDRYRNQNVSV-------IFQSYNLITYMTALQNVLTAMeiT 111
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL----QDSARGIFLPPhrrrigyVFQEARLFPHLSVRGNLLYGR--K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 112 GVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHK 191
Cdd:COG4148 104 RAPRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDE 182
|
170 180 190
....*....|....*....|....*....|.
gi 446370010 192 ENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:COG4148 183 LDIPILYVSHSlDEVARLADHVVLLEQGRVV 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-188 |
4.13e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.28 E-value: 4.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYE-------SNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR 73
Cdd:COG4608 4 AEPLLEVRDLKKHFPvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 KIG---LDRYRnQNVSVIFQ----SYNliTYMTALQNVLTAMEITGVK-VQNKTARALQLLERVGLSEAEAKRNVLQLSG 145
Cdd:COG4608 84 GLSgreLRPLR-RRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446370010 146 GQQQRVAIARALSCNVDLLIADEPTGNLD----EQtamdIIELFQEL 188
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ----VLNLLEDL 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-201 |
5.48e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 107.89 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYV----LYNGKDIRKI- 75
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 --GLDRYRNQNVSVIFQ----SYNliTYM---TALQNVLtaMEITGVKVQNKTARALQLLERVGLSEAEAKRNVL--QLS 144
Cdd:PRK09473 88 ekELNKLRAEQISMIFQdpmtSLN--PYMrvgEQLMEVL--MLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYphEFS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 145 GGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-221 |
6.01e-28 |
|
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: 105.78 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLItYMTALQNVLTAM-EITGVKVQN--KTARALQLLERV--GLSEAEAKRNVlQLSGGQQQRVAIARALSC 159
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAYGRpGATREEVEEaaRAANAHEFIMELpeGYDTVIGERGV-KLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-217 |
6.04e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.64 E-value: 6.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGL---DVPKNGYVLYNGKDIRKIGL 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 ----DRYRNQNVSVIFQSYNLITYMTALQNVL------TAMEITGVK--VQNKTARALQLLERVGLSEAEAKRnVLQLSG 145
Cdd:PRK09984 77 lardIRKSRANTGYIFQQFNLVNRLSVLENVLigalgsTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQR-VSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 146 GQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVA-KKSDRAVYLSK 217
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQ 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-221 |
7.52e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 7 FKNLDYYYESNG--KNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYV------LYNGKDIRKigLD 78
Cdd:PRK13634 5 FQKVEHRYQYKTpfERRA-LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNKK--LK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRnQNVSVIFQ--SYNLITyMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK13634 82 PLR-KKVGIVFQfpEHQLFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVF 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-201 |
1.29e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 107.13 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKT-TTLSLGCGLDVPknGYVL-----YNGKDIRKIGl 77
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRIS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 DRYRNQ----NVSVIFQSYnlityMTALQNVLTA----MEitGVKVQN------KTARALQLLERVGLSEAEAKRNVL-- 141
Cdd:PRK11022 80 EKERRNlvgaEVAMIFQDP-----MTSLNPCYTVgfqiME--AIKVHQggnkktRRQRAIDLLNQVGIPDPASRLDVYph 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 142 QLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITH 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-221 |
1.56e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYY------ESNGknvaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR----K 74
Cdd:PRK13641 3 IKFENVDYIYspgtpmEKKG-----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IGLDRYRNQnVSVIFQ-SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAI 153
Cdd:PRK13641 78 KNLKKLRKK-VSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKLI 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5-221 |
2.70e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 108.80 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG-LDRYRN- 82
Cdd:TIGR03375 464 IEFRNVSFAY--PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDpADLRRNi 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 ----QNVSVIFQS-YNLITYMTAL---QNVLTAMEITGVK--VQNKTA-RALQLLERvGLSeaeakrnvlqLSGGQQQRV 151
Cdd:TIGR03375 542 gyvpQDPRLFYGTlRDNIALGAPYaddEEILRAAELAGVTefVRRHPDgLDMQIGER-GRS----------LSGGQRQAV 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKenKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDLVDRIIVMDNGRIV 678
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
3.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.83 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYR 81
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAS--FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 nQNVSVIFQS-YNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCN 160
Cdd:PRK13648 83 -KHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE-RADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSK 217
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNK 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-221 |
3.17e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDRYRNQNVSVIFQSYNLITYMTA 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMD 180
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446370010 181 IIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVV 244
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-221 |
3.28e-27 |
|
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: 103.77 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 7 FKNLDYYYESNgKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQnVS 86
Cdd:cd03249 3 FKNVSFRYPSR-PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 87 VIFQSYNLItYMTALQNVL-------TAMEITGVKVQNKTARALQLLERVglsEAEAKRNVLQLSGGQQQRVAIARALSC 159
Cdd:cd03249 81 LVSQEPVLF-DGTIAENIRygkpdatDEEVEEAAKKANIHDFIMSLPDGY---DTLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-221 |
4.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESN--GKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLD 78
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQNVSVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLqLSGGQQQRVAIARAL 157
Cdd:PRK13633 81 WDIRNKAGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHL-LSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-221 |
4.98e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.44 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGK-NVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNG---------KDIRK 74
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IgldryrNQNVSVIFQ-SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAI 153
Cdd:PRK13649 83 I------RKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTH-SQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHlMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-222 |
6.55e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.36 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI--RKIGLDRYRNQnVSVIFQ--SYNL----- 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK-VGLVFQypEYQLfeeti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 95 ---ITYmtALQNV-LTAMEItgvkvQNKTARALQLlerVGLSEAEAK-RNVLQLSGGQQQRVAIARALSCNVDLLIADEP 169
Cdd:PRK13637 102 ekdIAF--GPINLgLSEEEI-----ENRVKRAMNI---VGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446370010 170 TGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLVV 222
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCEL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-221 |
6.61e-27 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 103.33 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:cd03252 1 ITFEHVRFRYKPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSyNLITYMTALQNVL---TAMEITGVKVQNKTARA----LQLLErvGLSEAEAKRNVlQLSGGQQQRVAIARAL 157
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIAladPGMSMERVIEAAKLAGAhdfiSELPE--GYDTIVGEQGA-GLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-221 |
7.62e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.09 E-value: 7.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNG--KNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRN 82
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAI-HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 ---QNVSVIFQ-SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:PRK13646 82 pvrKRIGMVFQfPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIV 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-221 |
1.14e-26 |
|
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: 101.47 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESN--GKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLS-LGCGLDVPK-NGYVLYNGKDIRKiglDRY 80
Cdd:cd03213 4 LSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGvSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQnVSVIFQSYNLITYMTALQNVLTAMEITGvkvqnktaralqllervglseaeakrnvlqLSGGQQQRVAIARALSCN 160
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG------------------------------LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTH--SQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHqpSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-211 |
1.20e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTL-SLGCGLD----VPKNGYVLYNGKDIRKI 75
Cdd:PRK14239 2 TEPILQVSDLSVYY---NKKKA-LNSVSLDFYPNEITALIGPSGSGKSTLLrSINRMNDlnpeVTITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 GLDRYR-NQNVSVIFQSYNLITyMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAK----RNVLQLSGGQQQR 150
Cdd:PRK14239 78 RTDTVDlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKdrlhDSALGLSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 151 VAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHS-QEVAKKSDR 211
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSmQQASRISDR 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-221 |
1.78e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.04 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 19 KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDV--PKNGYVLYN-----------------------GKDIR 73
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvgepcpvcGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 KIGLD--------RYR-NQNVSVIFQ-SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSE--AEAKRNvl 141
Cdd:TIGR03269 91 PEEVDfwnlsdklRRRiRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHriTHIARD-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 142 qLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEV-AKKSDRAVYLSKKKL 220
Cdd:TIGR03269 169 -LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEViEDLSDKAIWLENGEI 247
|
.
gi 446370010 221 V 221
Cdd:TIGR03269 248 K 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
3.64e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.12 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK--------DI 72
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 73 R-KIGLdryrnqnvsvIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQR 150
Cdd:PRK13650 80 RhKIGM----------VFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDF-KEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 151 VAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-221 |
4.26e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 99.31 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigLDRYRNQN 84
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--LEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLItymtalqnvltameitgvkvqnktarALQLLERVGLseaeakrnvlQLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03247 77 ISVLNQRPYLF--------------------------DTTLRNNLGR----------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVL--KDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-221 |
6.21e-26 |
|
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: 100.42 E-value: 6.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVP---KNGYVLYNGKDiRKIGLDRY 80
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP-RKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RnqnVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARAlQLLERVGLSEAEAKR----NVLQLSGGQQQRVAIARA 156
Cdd:cd03234 82 C---VAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRK-KRVEDVLLRDLALTRiggnLVKGISGGERRRVSIAVQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKeNKCIIVVTHS--QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQprSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-220 |
6.90e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 100.31 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDR-------YRNQNVSvIFQSynli 95
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlgigYLPQEAS-IFRK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 96 tyMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDE 175
Cdd:cd03218 90 --LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHL-RKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446370010 176 QTAMDIIELFQELahKENKCIIVVT--HSQEVAKKSDRAVYLSKKKL 220
Cdd:cd03218 167 IAVQDIQKIIKIL--KDRGIGVLITdhNVRETLSITDRAYIIYEGKV 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-211 |
9.87e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 99.11 E-value: 9.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 25 ENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqnvsvifqsynlITY------- 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD------------LLYlghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 98 ---MTALQNVLTAMEITGvkvQNKTARALQLLERVGLSEAEakrNVL--QLSGGQQQRVAIARALSCNVDLLIADEPTGN 172
Cdd:PRK13538 86 kteLTALENLRFYQRLHG---PGDDEALWEALAQVGLAGFE---DVPvrQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 173 LDEQTAMDIIELFqeLAHKENK-CIIVVTHsQEVAKKSDR 211
Cdd:PRK13538 160 IDKQGVARLEALL--AQHAEQGgMVILTTH-QDLPVASDK 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-222 |
1.00e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 99.28 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK-----DIRKIGL-- 77
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaARNRIGYlp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 -DRYRNQNVSVIFQsynlITYMTALQnvltameitGVKVQNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARA 156
Cdd:cd03269 77 eERGLYPKMKVIDQ----LVYLAQLK---------GLKKEEARRRIDEWLERLELSEYANKR-VEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLVV 222
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELA-RAGKTVILSTHQmELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
1.02e-25 |
|
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: 99.43 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesnGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQN 84
Cdd:cd03224 1 LEVENLNAGY---GKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEI-TGVKVQNKTARALQLLERvgLSEaeaKRNVL--QLSGGQQQRVAIARALSCNV 161
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYArRRAKRKARLERVYELFPR--LKE---RRKQLagTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 162 DLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-221 |
1.49e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGL------DVPKNGYVLYNGKDIRKIGLDRYRNQnVSVIFQSYNLI 95
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKE-VGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 96 TYMTALQNVLTAMEITGVKVQNKTARALQ-LLERVGL-SEAEAKRN--VLQLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLwKEVYDRLNspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446370010 172 NLDEQTAMDIIELFQELahKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK14246 183 MIDIVNSQAIEKLITEL--KNEIAIVIVSHNpQQVARVADYVAFLYNGELV 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-221 |
1.54e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK--------DI 72
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 73 RKigldryrnqNVSVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRV 151
Cdd:PRK13635 80 RR---------QVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-201 |
1.94e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYESNG-----KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigL 77
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 DR-----YRnQNVSVIFQSYnlityMTALQNVLTAMEI--------TGVKVQNKTARALQLLERVGLSEAEAKRNVLQLS 144
Cdd:PRK10419 80 NRaqrkaFR-RDIQMVFQDS-----ISAVNPRKTVREIireplrhlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 145 GGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
2.50e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYEsngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR--KIGLDRYR 81
Cdd:PRK13639 1 ILETRDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 nQNVSVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCN 160
Cdd:PRK13639 78 -KTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 161 VDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDlVPVYADKVYVMSDGKII 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
3.39e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR------- 73
Cdd:COG3845 2 MPPALELRGITKRF---GGVVA-NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 ---KIGLdryrnqnvsvIFQSYNLITYMTALQNVLTAMEITGVKVQN-KTARA--LQLLERVGLS-EAEAKrnVLQLSGG 146
Cdd:COG3845 78 ialGIGM----------VHQHFMLVPNLTVAENIVLGLEPTKGGRLDrKAARAriRELSERYGLDvDPDAK--VEDLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 147 QQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKlREVMAIADRVTVLRRGKVV 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-210 |
4.17e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.96 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGL-----DVPKNGYVLYNGKDI--RKIGL 77
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 DRYRNQnVSVIFQSYNLITyMTALQNVLTAMEITG----VKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAI 153
Cdd:PRK14258 84 NRLRRQ-VSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSD 210
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-201 |
4.36e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.60 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITyMTALQNVLTAmeitgvkvqNKTARALQL---LERVGLSE------------AEAKRnvlQLSGGQQQ 149
Cdd:PRK11160 416 ISVVSQRVHLFS-ATLRDNLLLA---------APNASDEALievLQQVGLEKlleddkglnawlGEGGR---QLSGGEQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQElaHKENKCIIVVTH 201
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITH 532
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-208 |
5.95e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 5.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkiGLDRY 80
Cdd:PRK13537 4 SVAPIDFRNVEKRY---GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGL-SEAEAKrnVLQLSGGQQQRVAIARALSC 159
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLeNKADAK--VGELSGGMKRRLTLARALVN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELAHKeNKCIIVVTHSQEVAKK 208
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAER 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-201 |
8.23e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.78 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCG-LDVPKN--GYVLYNGKDI-------RKIGLdryrnqnvsvIFQSY 92
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFSasGEVLLNGRRLtalpaeqRRIGI----------LFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NLITYMTALQNVLTAMEiTGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGN 172
Cdd:COG4136 86 LLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGF-ADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180
....*....|....*....|....*....
gi 446370010 173 LDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:COG4136 164 LDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-193 |
8.83e-25 |
|
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: 101.30 E-value: 8.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTT-LSLgCGLdVPKNGYVLYNGKDIRkiGLDR-----YRnQNVSVIFQ----SYN 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLgLAL-LRL-IPSEGEIRFDGQDLD--GLSRralrpLR-RRMQVVFQdpfgSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 94 liTYMTALQNVLTAMEI--TGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:COG4172 377 --PRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180
....*....|....*....|..
gi 446370010 172 NLDEQTAMDIIELFQELAHKEN 193
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHG 476
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-213 |
3.67e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 28 NFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRyrnQNVSVIFQSYNLITYMTALQNVLTA 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 108 MEiTGVKVQNKTARALQ-LLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQ 186
Cdd:PRK10771 96 LN-PGLKLNAAQREKLHaIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180
....*....|....*....|....*...
gi 446370010 187 ELAHKENKCIIVVTHSQE-VAKKSDRAV 213
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEdAARIAPRSL 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-213 |
5.59e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRY 80
Cdd:COG1129 1 AEPLLEMRGISKSF---GGVKA-LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNLITYMTALQNVLTAMEIT-GVKVQNKT--ARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARAL 157
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIFLGREPRrGGLIDWRAmrRRARELLARLGLDIDPDTP-VGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 158 SCNVDLLIADEPTGNLDEQtamDIIELFQ---ELAhKENKCIIVVTHS-QEVAKKSDRAV 213
Cdd:COG1129 156 SRDARVLILDEPTASLTER---EVERLFRiirRLK-AQGVAIIYISHRlDEVFEIADRVT 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-221 |
9.69e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.60 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigLDRYR----NQNVSVIFQSYNLITYM 98
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA--MSRSRlytvRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 99 TALQNVLTAM-EITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:PRK11831 100 NVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 178 AMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIV 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
39-220 |
1.32e-23 |
|
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: 96.72 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK---DIRK-IGLDRYRnQNVSVIFQSYNLITYMTALQNVLTAMEITGVK 114
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgIFLPPEK-RRIGYVFQEARLFPHLSVRGNLRYGMKRARPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 115 VQNKT-ARALQLLervGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKEN 193
Cdd:TIGR02142 107 ERRISfERVIELL---GIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFG 182
|
170 180
....*....|....*....|....*...
gi 446370010 194 KCIIVVTHS-QEVAKKSDRAVYLSKKKL 220
Cdd:TIGR02142 183 IPILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-222 |
1.97e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 93.39 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 28 NFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIrkIGLDRYRnQNVSVIFQSYNLITYMTALQNVL-- 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQ-RPVSMLFQENNLFAHLTVRQNIGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 106 --TAMEITGVKVQNKTARALQllerVGLSEAEAkRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIE 183
Cdd:TIGR01277 95 lhPGLKLNAEQQEKVVDAAQQ----VGIADYLD-RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 184 LFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLVV 222
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKIKV 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-221 |
2.07e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYesNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDR 79
Cdd:PRK13548 1 AMLEARNLSVRL--GGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaeLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 YRnqnvSVIFQSYNLITYMTALQNV---LTAMEITGVKVQNKTARALqllERVGLSEAeAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK13548 77 RR----AVLPQHSSLSFPFTVEEVVamgRAPHGLSRAEDDALVAAAL---AQVDLAHL-AGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 157 L---SCNVD---LLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:PRK13548 149 LaqlWEPDGpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-221 |
2.67e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.69 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNG----KDIRKIGLDRYRNQNVSVIFQSYNLITYMT 99
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 100 ALQNVLTAMEIT-GVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTA 178
Cdd:PRK13645 107 TIEKDIAFGPVNlGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446370010 179 MDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVI 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
3.07e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLS-----LGCGLDVPKNGYVLYNGKDIRKI 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 GLDRYR-NQNVSVIFQSYNLITYMTALQNVltameITGVKVQNKTARALQLLERV--GLSEA---EAKRNVL-----QLS 144
Cdd:PRK14267 77 DVDPIEvRREVGMVFQYPNPFPHLTIYDNV-----AIGVKLNGLVKSKKELDERVewALKKAalwDEVKDRLndypsNLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 145 GGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-221 |
6.85e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 6.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVA-ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNgkDIRKIGLDRYRN 82
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 -----QNVSVIFQ-SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK13643 79 ikpvrKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTH-SQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHlMDDVADYADYVYLLEKGHII 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-221 |
1.07e-22 |
|
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: 91.91 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKnvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITyMTALQNV----LTAMEITGVKVqnktARALQLLERVgLSEAEAKRNV-----LQLSGGQQQRVAIAR 155
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIrygrPDATDEEVIEA----AKAAQIHDKI-MRFPDGYDTIvgergLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-218 |
1.28e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYesnGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSL---------GCGLDvpknGYVLYNGKDI 72
Cdd:PRK14243 8 ETVLRTENLNVYY---GSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlipGFRVE----GKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 73 RKIGLD----RYRnqnVSVIFQSYNLITyMTALQNVLTAMEITGVKVQ-----NKTARALQLLERVglsEAEAKRNVLQL 143
Cdd:PRK14243 80 YAPDVDpvevRRR---IGMVFQKPNPFP-KSIYDNIAYGARINGYKGDmdelvERSLRQAALWDEV---KDKLKQSGLSL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 144 SGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHS-QEVAKKSDRAVYLSKK 218
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNmQQAARVSDMTAFFNVE 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-202 |
1.62e-22 |
|
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: 95.12 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITyMTALQNVLTAM-EITGvkvqnktARALQLLERVGLSE-AEAKRNVLQ---------LSGGQQQRVAI 153
Cdd:TIGR02868 411 VSVCAQDAHLFD-TTVRENLRLARpDATD-------EELWAALERVGLADwLRALPDGLDtvlgeggarLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFqeLAHKENKCIIVVTHS 202
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-206 |
2.51e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDryrnqnVSVIFQSYNLITYMTALQ 102
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------TRLMFQDARLLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVltAMEITGvkvqNKTARALQLLERVGLSEaEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDII 182
Cdd:PRK11247 101 NV--GLGLKG----QWRDAALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180
....*....|....*....|....*.
gi 446370010 183 ELFQELAHKENKCIIVVTH--SQEVA 206
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHdvSEAVA 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-221 |
2.72e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTT-LSL-----GCGLDVPKNGYVLYN-GKDIRK 74
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTaLALmrlleQAGGLVQCDKMLLRRrSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IG------LDRYRNQNVSVIFQSYnlityMTALQNVLTAMEI--------TGVKVQNKTARALQLLERVGLSEAEA--KR 138
Cdd:PRK10261 90 LSeqsaaqMRHVRGADMAMIFQEP-----MTSLNPVFTVGEQiaesirlhQGASREEAMVEAKRMLDQVRIPEAQTilSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 139 NVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSK 217
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQ 244
|
....
gi 446370010 218 KKLV 221
Cdd:PRK10261 245 GEAV 248
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-201 |
3.17e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNgKDIRkIGldrYRNQNVS---------VIFQS-- 91
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-IG---YLPQEPPldddltvldTVLDGda 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 92 --YNLITYMTALQNVLTAMEITGVKVQNKT------------ARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARAL 157
Cdd:COG0488 88 elRALEAELEELEAKLAEPDEDLERLAELQeefealggweaeARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDeqtaMDIIELFQELAHKENKCIIVVTH 201
Cdd:COG0488 168 LSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSH 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-201 |
3.37e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK-----DIRKIGL- 77
Cdd:COG4152 1 MLELKGLTKRF---GDKTA-VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpeDRRRIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 --DR--YRNQNVSvifqsyNLITYMTALqnvltameiTGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAI 153
Cdd:COG4152 77 peERglYPKMKVG------EQLVYLARL---------KGLSKAEAKRRADEWLERLGLGDR-ANKKVEELSKGNQQKVQL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTH 201
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSH 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-221 |
3.51e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNgKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGlDRY 80
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNR-PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNL--------ITYmtALQNVLTAmEITGVKVQNKTARALQLLERVGLSEAEAKRNvlQLSGGQQQRVA 152
Cdd:TIGR00958 553 LHRQVALVGQEPVLfsgsvrenIAY--GLTDTPDE-EIMAAAKAANAHDFIMEFPNGYDTEVGEKGS--QLSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQtamdIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
4.96e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESngknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGY---VLYNGKDIRKIGL 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGTYegeIIFEGEELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 DRYRNQNVSVIFQSYNLITYMTALQNVLTAMEIT--GVKVQNK-TARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIA 154
Cdd:PRK13549 77 RDTERAGIAIIHQELALVKELSVLENIFLGNEITpgGIMDYDAmYLRAQKLLAQLKLDINPATP-VGNLGLGQQQLVEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 155 RALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSD 210
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISD 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-221 |
6.01e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 93.24 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQn 84
Cdd:TIGR02203 331 VEFRNVTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERV-----GLsEAEAKRNVLQLSGGQQQRVAIARALSC 159
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVdklplGL-DTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-221 |
7.64e-22 |
|
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: 87.87 E-value: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 20 NVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkigldryrnqnvsvifqsynlitymt 99
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 100 alqnvltameitgvkvqnktaralqllervGLSEAEAKRN----VLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDE 175
Cdd:cd03216 66 ------------------------------FASPRDARRAgiamVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446370010 176 QTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:cd03216 116 AEVERLFKVIRRLR-AQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-201 |
7.93e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.28 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNL--DYYYESNG---KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKi 75
Cdd:COG4167 1 MSALLEVRNLskTFKYRTGLfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 GLDRYRNQNVSVIFQSYNlitymTAL---QNVLTAMEI-----TGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQ 147
Cdd:COG4167 80 GDYKYRCKHIRMIFQDPN-----TSLnprLNIGQILEEplrlnTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446370010 148 QQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQ 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-174 |
8.12e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.17 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesNGKNvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG---LDRYR 81
Cdd:COG4559 2 LEAENLSVRL--GGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpweLARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 ---NQNVSVIFQsynlitymtalqnvLTAMEI-------TGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRV 151
Cdd:COG4559 78 avlPQHSSLAFP--------------FTVEEVvalgrapHGSSAAQDRQIVREALALVGLAHL-AGRSYQTLSGGEQQRV 142
|
170 180 190
....*....|....*....|....*....|
gi 446370010 152 AIARALS---CNVD----LLIADEPTGNLD 174
Cdd:COG4559 143 QLARVLAqlwEPVDggprWLFLDEPTSALD 172
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-210 |
1.05e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGL-DVPKnGYVLYNGKDIRKIGLDRYRNQ 83
Cdd:PRK11176 342 IEFRNVTFTYP--GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFyDIDE-GEILLDGHDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 nVSVIFQSYNL--------ITYmtALQNVLTAMEITGVKvqnKTARALQLLERV--GLSEAEAKRNVLqLSGGQQQRVAI 153
Cdd:PRK11176 419 -VALVSQNVHLfndtiannIAY--ARTEQYSREQIEEAA---RMAYAMDFINKMdnGLDTVIGENGVL-LSGGQRQRIAI 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTHSQEVAKKSD 210
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKAD 546
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-220 |
1.39e-21 |
|
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: 88.68 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYEsNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGlDRY 80
Cdd:cd03248 8 LKGIVKFQNVTFAYP-TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNL--------ITYmtALQNVLTaMEITGVKVQNKTARALQLLERVGLSEAEAKRNvlQLSGGQQQRVA 152
Cdd:cd03248 86 LHSKVSLVGQEPVLfarslqdnIAY--GLQSCSF-ECVKEAAQKAHAHSFISELASGYDTEVGEKGS--QLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQElaHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-221 |
1.58e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.50 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYesnGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqn 84
Cdd:TIGR01193 474 IVINDVSYSY---GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ-- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 vsvifqsynLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVgLSEAEAKRNVLQ---------------LSGGQQQ 149
Cdd:TIGR01193 549 ---------FINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAA-CEIAEIKDDIENmplgyqtelseegssISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHkenKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNGKnvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRY 80
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQnVSVIFQSYN-LITYMTALQNVLTA---MEITGVKVQNKTARALQLlerVGLsEAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK13647 78 RSK-VGLVFQDPDdQVFSSTVWDDVAFGpvnMGLDKDEVERRVEEALKA---VRM-WDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTH---------SQEVAKKSDRAVYLSKKKLVVNE 224
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHdvdlaaewaDQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-207 |
2.77e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAiLENVNFSFQKGHFYTILGPSGSGKTTT----LSLgcgldVPKNGYVLYNGKDIRkiGLDR-----YRNQnVSVI 88
Cdd:PRK15134 297 DHNVV-VKNISFTLRPGETLGLVGESGSGKSTTglalLRL-----INSQGEIWFDGQPLH--NLNRrqllpVRHR-IQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 89 FQSYNlitymTALQNVLTAMEIT--GVKVQNKT-------ARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSC 159
Cdd:PRK15134 368 FQDPN-----SSLNPRLNVLQIIeeGLRVHQPTlsaaqreQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAK 207
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVR 490
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-215 |
4.05e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 20 NVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIgldRYRNQNVSVIFQSYNLITYMT 99
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV---PPAERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 100 ALQNVLTAMEITGVKVQ------NKTARALQL---LERvglseaEAKrnvlQLSGGQQQRVAIARALSCNVDLLIADEPT 170
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEeinqrvNQVAEVLQLahlLDR------KPK----ALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446370010 171 GNLDE----QTAMDIIELfqelaHKENKC-IIVVTHSQ-EVAKKSDRAVYL 215
Cdd:PRK11000 162 SNLDAalrvQMRIEISRL-----HKRLGRtMIYVTHDQvEAMTLADKIVVL 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
4.47e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYeSNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK--DIRKIGLDR 79
Cdd:PRK13636 3 DYILKVEELNYNY-SDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 YRnQNVSVIFQSY-NLITYMTALQNV---LTAMEITGVKVQNKTARALqllERVGLSEAEAKrNVLQLSGGQQQRVAIAR 155
Cdd:PRK13636 80 LR-ESVGMVFQDPdNQLFSASVYQDVsfgAVNLKLPEDEVRKRVDNAL---KRTGIEHLKDK-PTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDiVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-221 |
5.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESNgKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRY 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKE-SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQnVSVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAkRNVLQLSGGQQQRVAIARALSC 159
Cdd:PRK13642 80 RRK-IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKT-REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEII 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-205 |
7.54e-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: 86.26 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNqnvsvifqsynlITYM--- 98
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN------------ILYLghl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 99 TALQNVLTAME-------ITGVKVQNktarALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:TIGR01189 82 PGLKPELSALEnlhfwaaIHGGAQRT----IEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 446370010 172 NLDEQTamdiIELFQEL--AHKENKCIIVVTHSQEV 205
Cdd:TIGR01189 157 ALDKAG----VALLAGLlrAHLARGGIVLLTTHQDL 188
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-221 |
8.62e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.38 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigldryrn 82
Cdd:PRK11231 1 MTLRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 qnvsviFQSYNLITYMTALQNVLTAMEitGVKV-------------------QNKTARALQLLERVGLSEAeAKRNVLQL 143
Cdd:PRK11231 69 ------LSSRQLARRLALLPQHHLTPE--GITVrelvaygrspwlslwgrlsAEDNARVNQAMEQTRINHL-ADRRLTDL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 144 SGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRyCDHLVVLANGHVM 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-200 |
1.00e-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: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdirkiGLDRYRNQnvsvIFQSYNLITYMTAL 101
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-----PLDFQRDS----IARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 102 QNVLTAME-ITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMD 180
Cdd:cd03231 85 KTTLSVLEnLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 446370010 181 IIELFQelAHKENKCIIVVT 200
Cdd:cd03231 164 FAEAMA--GHCARGGMVVLT 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-188 |
1.04e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.48 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYE-SNG-----KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvKRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IG--LDRYRNQNVSVIFQS-YNLITYMTALQNVLTA-MEI-TGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQ 149
Cdd:PRK11308 82 ADpeAQKLLRQKIQIVFQNpYGSLNPRKKVGQILEEpLLInTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQEL 188
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-208 |
1.06e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKT-TTLSLGCGLDVPKngyVLYNGKDIRKIG----- 76
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPP---VVYPSGDIRFHGesllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 -----LDRYRNQNVSVIFQ----SYN-LITYMTALQNVLTAMEitGVKVQNKTARALQLLERVGLSEAEAKRNVL--QLS 144
Cdd:PRK15134 81 aseqtLRGVRGNKIAMIFQepmvSLNpLHTLEKQLYEVLSLHR--GMRREAARGEILNCLDRVGIRQAAKRLTDYphQLS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 145 GGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK 208
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRK 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-210 |
1.18e-20 |
|
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: 89.50 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPK---NGYVLYNGKDIRKIGLDRYRNQNVSVIFQSYNLITY 97
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 98 MTALQNVLTAMEIT--GVKVQNK--TARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:TIGR02633 93 LSVAENIFLGNEITlpGGRMAYNamYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 446370010 174 DEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSD 210
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCD 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-221 |
1.89e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.09 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKNVA-ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNG--YVLYNGK--DIRKIG 76
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEwvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 LD-RYR-NQNVSVIFQSYNLITYMTALQNVLTAMeitGVKVQNKTAR--ALQLLERVGLSEAEAkRNVL-----QLSGGQ 147
Cdd:TIGR03269 357 PDgRGRaKRYIGILHQEYDLYPHRTVLDNLTEAI---GLELPDELARmkAVITLKMVGFDEEKA-EEILdkypdELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 148 QQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKIV 507
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-215 |
2.82e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVlyngkdirkiglDRYRNQNVSVIFQSYNLITYMTALQN 103
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAM----EITGVKVQNKTARAL--QLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:NF040873 76 DLVAMgrwaRRGLWRRLTRDDRAAvdDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 446370010 178 AMDIIELFQElAHKENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:NF040873 155 RERIIALLAE-EHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-220 |
3.07e-20 |
|
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: 88.92 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIrKIGLDRYRnQNVSV 87
Cdd:TIGR01257 932 KNLVKIFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVR-QSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEaeaKRN--VLQLSGGQQQRVAIARALSCNVDLLI 165
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHH---KRNeeAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 166 ADEPTGNLDEQTAMDIIELFqeLAHKENKCIIVVTHSQEVAK-KSDRAVYLSKKKL 220
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-224 |
4.20e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.62 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSL--GCGLDVPKNGYVlyngkDIRKIGLDRyrnqNVSVIFQSYnlitymtA 100
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLlaGALKGTPVAGCV-----DVPDNQFGR----EASLIDAIG-------R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLTAMEItgvkvqnktaralqlLERVGLSEAEA-KRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAM 179
Cdd:COG2401 109 KGDFKDAVEL---------------LNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446370010 180 DIIELFQELAHKENKCIIVVTHSQEVAK--KSDRAVYLSKKKLVVNE 224
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEEK 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-170 |
6.39e-20 |
|
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: 84.65 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYesnGKnVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYR 81
Cdd:COG0410 1 MPMLEVENLHAGY---GG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NQNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKT--ARALQLLERvgLSEaeaKRNVL--QLSGGQQQRVAIARAL 157
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAdlERVYELFPR--LKE---RRRQRagTLSGGEQQMLAIGRAL 151
|
170
....*....|...
gi 446370010 158 SCNVDLLIADEPT 170
Cdd:COG0410 152 MSRPKLLLLDEPS 164
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-222 |
1.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNgknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKD---------IRK 74
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdfsklqgIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IgldryrnqnVSVIFQsyNLITYMTAlqnvLTAMEITGVKVQNKTARALQLLERVGLSEAEAK------RNVLQLSGGQQ 148
Cdd:PRK13644 78 L---------VGIVFQ--NPETQFVG----RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 149 QRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLVV 222
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIVL 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-202 |
1.50e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 20 NVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkigLDRYRNQnvsvifqsynlITYM- 98
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEA-----------CHYLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 99 --TALQNVLTAME-------ITGvkvqNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEP 169
Cdd:PRK13539 80 hrNAMKPALTVAEnlefwaaFLG----GEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 446370010 170 TGNLDEQTamdiIELFQEL--AH-KENKCIIVVTHS 202
Cdd:PRK13539 155 TAALDAAA----VALFAELirAHlAQGGIVIAATHI 186
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-215 |
1.66e-19 |
|
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: 82.90 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNG-KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLS--LGcglDVPK-NGYVLYNGKdirkIGldrY 80
Cdd:cd03250 1 ISVEDASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSalLG---ELEKlSGSVSVPGS----IA---Y 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQnvsvifQSYnlITYMTALQNVLTAMEITGVKVqNKTARALQLL---------------ERvGLSeaeakrnvlqLSG 145
Cdd:cd03250 71 VSQ------EPW--IQNGTIRENILFGKPFDEERY-EKVIKACALEpdleilpdgdlteigEK-GIN----------LSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 146 GQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIE--LFQELahKENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-211 |
1.66e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 26 NVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkiGLDRYRNQNVSVI--FQSYNLITYMTALQN 103
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGHQIARMGVVrtFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEI---TGV------------KVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADE 168
Cdd:PRK11300 101 LLVAQHQqlkTGLfsgllktpafrrAESEALDRAATWLERVGLLEH-ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446370010 169 PTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDR 211
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKlVMGISDR 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-224 |
1.88e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKnVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRY 80
Cdd:PRK11614 2 EKVMLSFDKVSAHY---GK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNLITYMTALQN-VLTAMEITGVKVQNKTARALQLLERvgLSEAEAKRnVLQLSGGQQQRVAIARALSC 159
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENlAMGGFFAERDQFQERIKWVYELFPR--LHERRIQR-AGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLVVNE 224
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-221 |
3.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.70 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVP---KNGYVLYNGKDIRKIGLD 78
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQnVSVIFQSY-NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARAL 157
Cdd:PRK13640 81 DIREK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDY-IDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 158 SCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-201 |
3.34e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.82 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYrNQNVSV 87
Cdd:COG4604 5 KNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL-AKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQSYNLITYMTALQNV-----------LTAMEitgvkvQNKTARALQLLERVGLSEaeakRNVLQLSGGQQQRVAIARA 156
Cdd:COG4604 80 LRQENHINSRLTVRELVafgrfpyskgrLTAED------REIIDEAIAYLDLEDLAD----RYLDELSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-191 |
4.32e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYesNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDR-- 79
Cdd:COG1137 1 MMTLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 80 -----YRNQNVSvIFQsynlitYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIA 154
Cdd:COG1137 77 rlgigYLPQEAS-IFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHL-RKSKAYSLSGGERRRVEIA 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 446370010 155 RALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHK 191
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER 185
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-206 |
5.55e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGlDRYRNQNVSVIFQSYNLITYMTA 100
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVltAMEIT------GVKVQNKTARALQLLERVGLSeAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD 174
Cdd:PRK09536 95 RQVV--EMGRTphrsrfDTWTETDRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190
....*....|....*....|....*....|..
gi 446370010 175 EQTAMDIIELFQELAhKENKCIIVVTHSQEVA 206
Cdd:PRK09536 172 INHQVRTLELVRRLV-DDGKTAVAAIHDLDLA 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-221 |
6.79e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVP----KNGYVLYNGKDIRKIGLdryRNQNVSVIFQ----SY 92
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAL---RGRKIATIMQnprsAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NLITYMTA-LQNVLTAMEITGVKvqnktARALQLLERVGLSEAE--AKRNVLQLSGGQQQRVAIARALSCNVDLLIADEP 169
Cdd:PRK10418 93 NPLHTMHThARETCLALGKPADD-----ATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 170 TGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
7.43e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNgknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQ 83
Cdd:PRK13652 3 LIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQ-SYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVD 162
Cdd:PRK13652 79 FVGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 163 LLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLVVNE 224
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-221 |
1.02e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.13 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 17 NGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYVLYNGKDIRKIGLDRYRnQNVSVIFQSYNLIt 96
Cdd:PRK11174 361 DGK--TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWR-KHLSWVGQNPQLP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 97 YMTALQNVLTAmeitgvKVQNKTARALQLLERVGLSE----------AEAKRNVLQLSGGQQQRVAIARALSCNVDLLIA 166
Cdd:PRK11174 436 HGTLRDNVLLG------NPDASDEQLQQALENAWVSEflpllpqgldTPIGDQAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 167 DEPTGNLDEQTAMDIIELFQELAHkeNKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-211 |
1.20e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGY---VLYNG-----KDIR---KIGldryrnqnVSVIF 89
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGSYegeILFDGevcrfKDIRdseALG--------IVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 90 QSYNLITYMTALQNVLTAMEIT--GVKVQNKT-ARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARALSCNVDLLIA 166
Cdd:NF040905 85 QELALIPYLSIAENIFLGNERAkrGVIDWNETnRRARELLAKVGLDESPDTL-VTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 167 DEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDR 211
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADS 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-205 |
1.33e-18 |
|
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: 80.94 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLD---YYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKD------ 71
Cdd:COG4778 1 MTTLLEVENLSktfTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 72 ---------IRK--IGldrYrnqnVSvifQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeakrnv 140
Cdd:COG4778 81 qaspreilaLRRrtIG---Y----VS---QFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPER------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 141 L-QL-----SGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKC-IIVVTHSQEV 205
Cdd:COG4778 145 LwDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA--KARGTaIIGIFHDEEV 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-221 |
1.38e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGY-----VLYNGKDIRKigldrYRN-----QNVSVIFQSY 92
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFN-----YRDvlefrRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NLITyMTALQNVLTameitGVKVQNKTAR------ALQLLERVGLSEAEAKR---NVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:PRK14271 111 NPFP-MSIMDNVLA-----GVRAHKLVPRkefrgvAQARLTEVGLWDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENkcIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNlAQAARISDRAALFFDGRLV 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-221 |
1.65e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesngKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKN-GYVLYNGKDIRKIGLDRYRN 82
Cdd:PRK10895 3 TLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI-VPRDaGNIIIDDEDISLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSYNLITYMTALQNVLTAMEI-TGVKVQNKTARALQLLERVGLSEAeakRNVL--QLSGGQQQRVAIARALSC 159
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHL---RDSMgqSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 160 NVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-221 |
1.83e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.47 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 6 QFKNLDYYYESNGKNVailENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQNV 85
Cdd:PRK13657 336 EFDDVSFSYDNSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR-RNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 86 SVIFQSYNLITYMTA-----------LQNVLTAMEItgvkvqnktARALQLLER--VGLSEAEAKRNvLQLSGGQQQRVA 152
Cdd:PRK13657 412 AVVFQDAGLFNRSIEdnirvgrpdatDEEMRAAAER---------AQAHDFIERkpDGYDTVVGERG-RQLSGGERQRLA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHkeNKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-212 |
2.15e-18 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 80.40 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQ 83
Cdd:TIGR04406 1 TLVAENLIKSY--KKRKV--VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAMEITG-VKVQNKTARALQLLERVGLSEAEAKRNvLQLSGGQQQRVAIARALSCNVD 162
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKA-MSLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446370010 163 LLIADEPTGNLDEQTAMDIIELFQELAHKeNKCIIVVTHS-QEVAKKSDRA 212
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNvRETLDICDRA 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-200 |
2.82e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLD--YYYES---NGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIrKI 75
Cdd:PRK15112 1 VETLLEVRNLSktFRYRTgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 GLDRYRNQNVSVIFQSYNliTYMTALQNVLTAMEI-----TGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQR 150
Cdd:PRK15112 80 GDYSYRSQRIRMIFQDPS--TSLNPRQRISQILDFplrlnTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446370010 151 VAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVT 200
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-208 |
5.16e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNG-------KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK 74
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IGLDRYR--NQNVSVIFQS--YNLITYMTALQNVLTAMEITGVkVQNKTA--RALQLLERVGLSEAEAKRNVLQLSGGQQ 148
Cdd:PRK10261 391 LSPGKLQalRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGL-LPGKAAaaRVAWLLERVGLLPEHAWRYPHEFSGGQR 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 149 QRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK 208
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVER 529
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-204 |
1.45e-17 |
|
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: 75.95 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGyvlyngkdirkigldryrnqn 84
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG--------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 vSVIFQSYNLITYMTalqnvltameitgvkvqnktaralqllervglseaeakrnvlQLSGGQQQRVAIARALSCNVDLL 164
Cdd:cd03221 56 -IVTWGSTVKIGYFE------------------------------------------QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 165 IADEPTGNLDEQTAMDIIELFQELahkeNKCIIVVTHSQE 204
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEY----PGTVILVSHDRY 128
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-201 |
1.61e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.87 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkigldRYRNQNVSvifQSYNLITymtalQ 102
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-----HYASKEVA---RRIGLLA-----Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAMEITgvkVQNKTARA-------------------LQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:PRK10253 89 NATTPGDIT---VQELVARGryphqplftrwrkedeeavTKAMQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLH 202
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-221 |
2.18e-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: 77.57 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYY-ESNgknvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQ 83
Cdd:TIGR03410 1 LEVSNLNVYYgQSH-----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQLLERvgLSEAEAKRNVLqLSGGQQQRVAIARALSCNVDL 163
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGD-LSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 164 LIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-221 |
2.63e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLdyyyeSNGKNVailENVNFSFQKGHfytILGPSG---SGKTTTLSLGCGLDVPKNGYVLYNGKDIR----- 73
Cdd:COG1129 254 EVVLEVEGL-----SVGGVV---RDVSFSVRAGE---ILGIAGlvgAGRTELARALFGADPADSGEIRLDGKPVRirspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 -----KIGL---DRyrnqnvsvifQSYNLITYMTALQNV-LTAME--ITGVKVQNKTARAL--QLLERVGLSEAEAKRNV 140
Cdd:COG1129 323 dairaGIAYvpeDR----------KGEGLVLDLSIRENItLASLDrlSRGGLLDRRRERALaeEYIKRLRIKTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 141 LQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVThS--QEVAKKSDRAVYLSKK 218
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVIS-SelPELLGLSDRILVMREG 470
|
...
gi 446370010 219 KLV 221
Cdd:COG1129 471 RIV 473
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-222 |
2.90e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 19 KNVAI---LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYVLYNGKDIRKI---GLDRYR---NQNVSVIF 89
Cdd:COG4138 4 NDVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWsaaELARHRaylSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 90 QsynlityMTALQnvLTAMEITGVKVQNKTARAL-QLLERVGLSEaeaK--RNVLQLSGGQQQRVAIARAL-----SCNV 161
Cdd:COG4138 83 A-------MPVFQ--YLALHQPAGASSEAVEQLLaQLAEALGLED---KlsRPLTQLSGGEWQRVRLAAVLlqvwpTINP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 162 D--LLIADEPTGNLD--EQTAMDiiELFQELAHKENkCIIV----VTHSqevAKKSDRAVYLSKKKLVV 222
Cdd:COG4138 151 EgqLLLLDEPMNSLDvaQQAALD--RLLRELCQQGI-TVVMsshdLNHT---LRHADRVWLLKQGKLVA 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-211 |
3.54e-17 |
|
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: 75.93 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLdyyyeSNGKNVailENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR-------- 73
Cdd:cd03215 2 EPVLEVRGL-----SVKGAV---RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 --KIGL---DRyrnqnvsvifQSYNLITYMTALQNVLTAmeitgvkvqnktaralqllervglseaeakrnvLQLSGGQQ 148
Cdd:cd03215 74 raGIAYvpeDR----------KREGLVLDLSVAENIALS---------------------------------SLLSGGNQ 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 149 QRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVThS--QEVAKKSDR 211
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLIS-SelDELLGLCDR 173
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-211 |
4.35e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.33 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDI-RKIGLDRYRnqnVSVIFQSYNLITYMTA 100
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARAR---IGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMD 180
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFARL-ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190
....*....|....*....|....*....|..
gi 446370010 181 IIELFQELAHKeNKCIIVVTHSQEVAKK-SDR 211
Cdd:PRK13536 211 IWERLRSLLAR-GKTILLTTHFMEEAERlCDR 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-221 |
5.08e-17 |
|
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: 76.38 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLR-SR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQS---------YNLITYmtalqNVLTAMEItgvkvqnktaraLQLLERVGLSE----------AEAKRNVLQLSG 145
Cdd:cd03244 80 ISIIPQDpvlfsgtirSNLDPF-----GEYSDEEL------------WQALERVGLKEfveslpggldTVVEEGGENLSV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 146 GQQQRVAIARALSCNVDLLIADEPTGNLDEQTAmdiiELFQELAHKE--NKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETD----ALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-223 |
1.02e-16 |
|
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: 75.83 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 19 KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGyvlyngkDIRKIGLDRYRNQN-----VSVIF-QSY 92
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG-------EVRVAGLVPWKRRKkflrrIGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NLITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGN 172
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 173 LDEQTAMDIIELFQELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLVVN 223
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-221 |
3.35e-16 |
|
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: 73.72 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLdyYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPK--NGYVLYNGKDIRKIGLDRYRN 82
Cdd:cd03217 1 LEIKDL--HVSVGGK--EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSVIFQSynlitymtalqnvltAMEITGVKVQNktaralqLLervglseaeakRNV-LQLSGGQQQRVAIARALSCNV 161
Cdd:cd03217 77 LGIFLAFQY---------------PPEIPGVKNAD-------FL-----------RYVnEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 162 DLLIADEPTGNLDeQTAMDII-ELFQELaHKENKCIIVVTHSQEVAK--KSDRAVYLSKKKLV 221
Cdd:cd03217 124 DLAILDEPDSGLD-IDALRLVaEVINKL-REEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-201 |
3.59e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVlyngkdirKIGldryrn 82
Cdd:COG0488 314 KVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLG------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 QNVSvifqsynlITYMTALQNVL----TAME-ITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARAL 157
Cdd:COG0488 376 ETVK--------IGYFDQHQEELdpdkTVLDeLRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 158 SCNVDLLIADEPTGNLDeqtaMDIIELFQE-LAHKENkCIIVVTH 201
Cdd:COG0488 448 LSPPNVLLLDEPTNHLD----IETLEALEEaLDDFPG-TVLLVSH 487
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-219 |
4.05e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNgKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVL----YNGKDIR------K 74
Cdd:PTZ00265 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindsHNLKDINlkwwrsK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IG-----------------------------LDRYRNQNVSVIFQSYNLITYMTA-----LQNVLTAMEITGVKVQNKTA 120
Cdd:PTZ00265 462 IGvvsqdpllfsnsiknnikyslyslkdleaLSNYYNEDGNDSQENKNKRNSCRAkcagdLNDMSNTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 121 RALQLLERVGLS----------------EAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIEL 184
Cdd:PTZ00265 542 QTIKDSEVVDVSkkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|....*
gi 446370010 185 FQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKK 219
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-211 |
4.61e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQNVSVIFQSYNLITYMTA 100
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNV----LTAMEITGVKV---QNKTARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:PRK09700 98 LENLyigrHLTKKVCGVNIidwREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 446370010 174 DEQTAMDIIELFQELaHKENKCIIVVTHS-QEVAKKSDR 211
Cdd:PRK09700 177 TNKEVDYLFLIMNQL-RKEGTAIVYISHKlAEIRRICDR 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-221 |
5.85e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLS-LGCGL--DVPKNGYVLYNGkdiRKIGLDRYRnQNVSVIFQSYNLITYMT 99
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSpkGVKGSGSVLLNG---MPIDAKEMR-AISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 100 ALQNVL-TAMeitgVKVQN------KTARALQLLERVGLSEAEAKR-----NVLQLSGGQQQRVAIARALSCNVDLLIAD 167
Cdd:TIGR00955 116 VREHLMfQAH----LRMPRrvtkkeKRERVDEVLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 168 EPTGNLDEQTAMDIIELFQELAHKeNKCIIVVTH--SQEVAKKSDRAVYLSKKKLV 221
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHqpSSELFELFDKIILMAEGRVA 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-203 |
5.92e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.26 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsnGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIgldRYRNQN 84
Cdd:PRK11650 4 LKLQAVRKSYD--GKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMTALQNVLTAMEITGV-------KVQnKTARALQLlervglsEAEAKRNVLQLSGGQQQRVAIARAL 157
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMpkaeieeRVA-EAARILEL-------EPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446370010 158 SCNVDLLIADEPTGNLDE----QTAMDIIELFQELahkeNKCIIVVTHSQ 203
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL----KTTSLYVTHDQ 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-198 |
1.28e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYESngknVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRY 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQNVSVIFQSYNLITYMTALQNVLTAMEIT----GVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK10762 77 QEAGIGIIHQELNLIPQLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFS-SDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446370010 157 LSCNVDLLIADEPTGNL-DEQTAmdiiELF---QELahKENKCIIV 198
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETE----SLFrviREL--KSQGRGIV 195
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-211 |
1.39e-15 |
|
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: 74.78 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK---------IGldrYRNQNVSV- 87
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdreelgrhIG---YLPQDVELf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 ---IFQsyNlITYMTalqnvltamEITGVKVQnKTARA-------LQLLE----RVGLSEAeakrnvlQLSGGQQQRVAI 153
Cdd:COG4618 419 dgtIAE--N-IARFG---------DADPEKVV-AAAKLagvhemiLRLPDgydtRIGEGGA-------RLSGGQRQRIGL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKKSDR 211
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAVDK 535
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-215 |
2.35e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYE---------SNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK 74
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IGLDRYRN--QNVSVIFQ----SYN------------LITYmtalQNVLTAMEITGvKVQNktaralqLLERVGLSEAEA 136
Cdd:PRK15079 88 MKDDEWRAvrSDIQMIFQdplaSLNprmtigeiiaepLRTY----HPKLSRQEVKD-RVKA-------MMLKVGLLPNLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 137 KRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAV-- 213
Cdd:PRK15079 156 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLvm 235
|
..
gi 446370010 214 YL 215
Cdd:PRK15079 236 YL 237
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-203 |
7.10e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLdyYYESNGKNvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDV--PKNGYVLYNGKDI-------R-K 74
Cdd:COG0396 1 LEIKNL--HVSVEGKE--ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDIlelspdeRaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 75 IGLdryrnqnvSVIFQsYNL----ITYMTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEAKRNV-LQLSGGQQQ 149
Cdd:COG0396 77 AGI--------FLAFQ-YPVeipgVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQ 203
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQ 200
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-221 |
7.88e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.21 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYVLYNG-------KDI------RKIGldrYrnqnvsvIFQSYNLITYMTALQNVL 105
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIclppekRRIG---Y-------VFQDARLFPHYKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 106 TameitGVKVQNKtARALQLLERVGLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELF 185
Cdd:PRK11144 99 Y-----GMAKSMV-AQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 446370010 186 QELAHKENKCIIVVTHS-QEVAKKSDRAVYLSKKKLV 221
Cdd:PRK11144 172 ERLAREINIPILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-221 |
8.23e-15 |
|
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: 71.02 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYeSNGKNVailENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGL---- 77
Cdd:TIGR02323 1 KPLLQVSGLSKSY-GGGKGC---RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELyqls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 --DRYRNQNVSVIFQSYN----LITYMTALQNVLTAMEITGVK-VQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQR 150
Cdd:TIGR02323 77 eaERRRLMRTEWGFVHQNprdgLRMRVSAGANIGERLMAIGARhYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 151 VAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAK-KSDRAVYLSKKKLV 221
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-201 |
9.28e-15 |
|
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: 70.90 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 30 SFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkigldrYRNQNVSVIFQsynliTYMTALQNVLTAME 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKPQYIKADYE-----GTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 110 ITGVKVQNKTARALQLlervglsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD-EQTAM--DIIELFQ 186
Cdd:cd03237 90 YTHPYFKTEIAKPLQI-------EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDvEQRLMasKVIRRFA 162
|
170
....*....|....*
gi 446370010 187 ElahKENKCIIVVTH 201
Cdd:cd03237 163 E---NNEKTAFVVEH 174
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-201 |
1.14e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 72.38 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRK---------IGldrYRNQNVSvIFQSyn 93
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdretfgkhIG---YLPQDVE-LFPG-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 94 litymTALQNV------LTAMEITGVKvqnKTARALQLLERV------GLSEAEAKrnvlqLSGGQQQRVAIARALSCNV 161
Cdd:TIGR01842 407 -----TVAENIarfgenADPEKIIEAA---KLAGVHELILRLpdgydtVIGPGGAT-----LSGGQRQRIALARALYGDP 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446370010 162 DLLIADEPTGNLDEQTAMDIIELFQELahKENKCI-IVVTH 201
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKAL--KARGITvVVITH 512
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-224 |
1.39e-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: 69.87 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 17 NGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLdryrnqnvSVIFQSynlit 96
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL--------GGGFNP----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 97 YMTALQNVLTAMEITGVkvqnKTARALQLLERV-GLSEAEAKRN--VLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:cd03220 98 ELTGRENIYLNGRLLGL----SRKEIDEKIDEIiEFSELGDFIDlpVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 174 DEQTAMDIIELFQELaHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLVVNE 224
Cdd:cd03220 174 DAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-222 |
1.67e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGK--DIRKIGLDRYRNQnVSVIFQSYNLITYMTA 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQ-VATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 L-QNVLTAMEITGVkVQNKTARALQllERVGLSEAEAKRN--VLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:PRK13638 95 IdSDIAFSLRNLGV-PEAEITRRVD--EALTLVDAQHFRHqpIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446370010 178 AMDIIELFQELAHKENKcIIVVTHSQEVAKKSDRAVYLSKKKLVV 222
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-201 |
1.91e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYV-----LYNGKDIRKIGLD 78
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYR---NQNVSVIFQ--SYNL---ITYMTALQNVLTAMEITGV---KVQNKTARALQLLERVGLSEAEAKRNVL--QLSG 145
Cdd:COG4170 82 ERRkiiGREIAMIFQepSSCLdpsAKIGDQLIEAIPSWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYphELTE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 146 GQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-201 |
2.76e-14 |
|
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: 71.00 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKnvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRN-- 82
Cdd:COG5265 358 VRFENVSFGYDPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAai 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 83 ----QNVsVIFQS---YNlITY--MTAlqnvlTAMEItgvkvqNKTARALQLLE-----------RVGlseaeaKRNvLQ 142
Cdd:COG5265 435 givpQDT-VLFNDtiaYN-IAYgrPDA-----SEEEV------EAAARAAQIHDfieslpdgydtRVG------ERG-LK 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 143 LSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTH 201
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA--RGRTTLVIAH 551
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-211 |
3.13e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.22 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDvpkngyvlyngKDIRKIGLDRYR-- 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVT-----------KDNWRVTADRMRfd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 ----------------NQNVSVIFQSynlitymtaLQNVLTAMEITGVK-VQN----------------KTARALQLLER 128
Cdd:PRK15093 72 didllrlsprerrklvGHNVSMIFQE---------PQSCLDPSERVGRQlMQNipgwtykgrwwqrfgwRKRRAIELLHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 129 VGLSE-AEAKRNV-LQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHS-QEV 205
Cdd:PRK15093 143 VGIKDhKDAMRSFpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQML 222
|
....*.
gi 446370010 206 AKKSDR 211
Cdd:PRK15093 223 SQWADK 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-211 |
4.82e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.22 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYyESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLslgcgldvpkngyvlyngkdiRKI-GLDRY--- 80
Cdd:COG4178 363 LALEDLTLR-TPDGR--PLLEDLSLSLKPGERLLITGPSGSGKSTLL---------------------RAIaGLWPYgsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 ---RNQNVSVIF---QSY-NLITymtaLQNVL----TAMEITgvkvqnkTARALQLLERVGLSEAEAKRNVLQ-----LS 144
Cdd:COG4178 419 riaRPAGARVLFlpqRPYlPLGT----LREALlypaTAEAFS-------DAELREALEAVGLGHLAERLDEEAdwdqvLS 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 145 GGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQElaHKENKCIIVVTHSQEVAKKSDR 211
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDR 552
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-204 |
5.60e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLdyyyesnGKN---VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRkigl 77
Cdd:PRK11288 1 SSPYLSFDGI-------GKTfpgVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 drYRN------QNVSVIFQSYNLITYMTALQNV-LTAMEITGVKVQNKT--ARALQLLERVGLS-EAEAKrnVLQLSGGQ 147
Cdd:PRK11288 70 --FASttaalaAGVAIIYQELHLVPEMTVAENLyLGQLPHKGGIVNRRLlnYEAREQLEHLGVDiDPDTP--LKYLSIGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 148 QQRVAIARALSCNVDLLIADEPTGNLdeqTAMDIIELFQ---ELaHKENKCIIVVTHSQE 204
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSL---SAREIEQLFRvirEL-RAEGRVILYVSHRME 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-200 |
6.32e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLdyyyesNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR-KIGLDRY 80
Cdd:PRK09700 263 ETVFEVRNV------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 R--------NQNVSVIFQSYNLITYMTALQNVLT-----AMEITGVKVQNKTARALQllERVGLSEAEAKRNVLQLSGGQ 147
Cdd:PRK09700 337 KkgmayiteSRRDNGFFPNFSIAQNMAISRSLKDggykgAMGLFHEVDEQRTAENQR--ELLALKCHSVNQNITELSGGN 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 148 QQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVT 200
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVS 466
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-215 |
1.15e-13 |
|
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: 69.55 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdirkigldryrnqnVSVIFQsYNLITYMTALQ 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ-TSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAMEITGVKVQNkTARALQLLERVGLSeAEAKRNVL-----QLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:TIGR01271 506 NIIFGLSYDEYRYTS-VIKACQLEEDIALF-PEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 178 AMDIIE--LFQELAhkeNKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:TIGR01271 584 EKEIFEscLCKLMS---NKTRILVTSKLEHLKKADKILLL 620
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-201 |
1.40e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.04 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGyvLYNGK-DIRKIgLDRYRNqnvSVIFqsynliTYMTALQN--VLTAMEITGV-- 113
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLG--DYDEEpSWDEV-LKRFRG---TELQ------DYFKKLANgeIKVAHKPQYVdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 114 --KVQNKTARAL-----------QLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMD 180
Cdd:COG1245 172 ipKVFKGTVRELlekvdergkldELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN 250
|
170 180
....*....|....*....|.
gi 446370010 181 IIELFQELAhKENKCIIVVTH 201
Cdd:COG1245 251 VARLIRELA-EEGKYVLVVEH 270
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-201 |
1.85e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSL-GCGLDVpKNGYVLYNGKDIRKIGLDRYRNQnVSVIFQSYNLIT 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLiQRHFDV-SEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 97 YMTALQNVL-----TAMEITGV-KVQNKTARALQLLErvGLSEAEAKRNVLqLSGGQQQRVAIARALSCNVDLLIADEPT 170
Cdd:PRK10789 403 DTVANNIALgrpdaTQQEIEHVaRLASVHDDILRLPQ--GYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190
....*....|....*....|....*....|..
gi 446370010 171 GNLDEQTAMDIIelfQELAH-KENKCIIVVTH 201
Cdd:PRK10789 480 SAVDGRTEHQIL---HNLRQwGEGRTVIISAH 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-220 |
1.93e-13 |
|
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: 68.70 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKnVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPK-NGYVLYNGK--DIR----- 73
Cdd:TIGR02633 255 DVILEARNLTCWDVINPH-RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRnpaqa 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 ---KIGL---DRYRNQNVSVIFQSYNlITyMTALQNVLTAMEITGVKVQNKTARALQlleRVGLSEAEAKRNVLQLSGGQ 147
Cdd:TIGR02633 334 iraGIAMvpeDRKRHGIVPILGVGKN-IT-LSVLKSFCFKMRIDAAAELQIIGSAIQ---RLKVKTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 148 QQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-219 |
2.17e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.75 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKN--GYVLYNGKDIRKIGLDRyrnqnVSVIFQSYNLITYMTA 100
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKR-----TGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLTAMEI---TGVKVQNKTARALQLLERVGLSEAE----AKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:PLN03211 158 RETLVFCSLLrlpKSLTKQEKILVAESVISELGLTKCEntiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446370010 174 DEQTAMDIIELFQELAHKeNKCIIVVTH--SQEVAKKSDRAVYLSKKK 219
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQK-GKTIVTSMHqpSSRVYQMFDSVLVLSEGR 284
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-198 |
3.34e-13 |
|
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: 65.75 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPK---NGYVLYNGKDIRKIGlDRY 80
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RNQnvsVIF--QSYNLITYMTalqnvltameitgVKvqnktaralQLLERVGlsEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:cd03233 82 PGE---IIYvsEEDVHFPTLT-------------VR---------ETLDFAL--RCKGNEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIV 198
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-201 |
3.61e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYvlYNGKDIRKIGLDRYR------------NQNVSVIFQsynlITYMTALQNVL- 105
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSWDEVLKRFRgtelqnyfkklyNGEIKVVHK----PQYVDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 106 -TAMEItgVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIEL 184
Cdd:PRK13409 178 gKVREL--LKKVDERGKLDEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARL 254
|
170
....*....|....*..
gi 446370010 185 FQELAhkENKCIIVVTH 201
Cdd:PRK13409 255 IRELA--EGKYVLVVEH 269
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-201 |
4.58e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdiRKIGLdryrnqnvsvIFQSYNLITYMTal 101
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--LRIGY----------VPQKLYLDTTLP-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 102 qnvLTAMEITGVKVQNKTARALQLLERVG---LSEAEAKRnvlqLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTA 178
Cdd:PRK09544 84 ---LTVNRFLRLRPGTKKEDILPALKRVQaghLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|...
gi 446370010 179 MDIIELFQELAHKENKCIIVVTH 201
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSH 179
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-223 |
6.00e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 19 KNVAI---LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYVLYNGKDIRKI---GLDRYR---NQNVSV-- 87
Cdd:PRK03695 4 NDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWsaaELARHRaylSQQQTPpf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 ---IFQsynlitYMTALQNVLTAMEiTGVKVQNKTARALQLLERVGlseaeakRNVLQLSGGQQQRVAIA-------RAL 157
Cdd:PRK03695 83 ampVFQ------YLTLHQPDKTRTE-AVASALNEVAEALGLDDKLG-------RSVNQLSGGEWQRVRLAavvlqvwPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 158 SCNVDLLIADEPTGNLD--EQTAMD-IIELFQELAhkenkcIIVVTHSQE---VAKKSDRAVYLSKKKLVVN 223
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLDvaQQAALDrLLSELCQQG------IAVVMSSHDlnhTLRHADRVWLLKQGKLLAS 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-207 |
7.14e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 1 METILQFKNLDYYYesnGKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGL--- 77
Cdd:PRK11701 3 DQPLLSVRGLTKLY---GPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 78 ---DRYRNQNVSVIFQSYN----LITYMTALQNVLTAMEITGVK-VQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQ 149
Cdd:PRK11701 79 seaERRRLLRTEWGFVHQHprdgLRMQVSAGGNIGERLMAVGARhYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 150 RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAK 207
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVAR 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-201 |
9.28e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVP-----------KNGYV-----LYNGKDIRKI----------G 76
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDfngearpqpgiKVGYLpqepqLDPTKTVRENveegvaeikdA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 LDRYrNQnvsvIFQSYN--------LITYMTALQNVLTAMEitGVKVQNKTARALQLLErvgLSEAEAKrnVLQLSGGQQ 148
Cdd:TIGR03719 100 LDRF-NE----ISAKYAepdadfdkLAAEQAELQEIIDAAD--AWDLDSQLEIAMDALR---CPPWDAD--VTKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 149 QRVAIARALSCNVDLLIADEPTGNLDEQTamdiIELFQELAHKENKCIIVVTH 201
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTH 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-214 |
2.15e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKiGLDRYRNQ 83
Cdd:PRK13540 1 MLDVIELDFDYHDQ----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSyNLITYMTALQNVL-------TAMEITGVKVQNKTARALQLleRVGLseaeakrnvlqLSGGQQQRVAIARA 156
Cdd:PRK13540 76 LCFVGHRS-GINPYLTLRENCLydihfspGAVGITELCRLFSLEHLIDY--PCGL-----------LSSGQKRQVALLRL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 157 LSCNVDLLIADEPTGNLDEQTAMDIIELFQElAHKENKCIIVVTHSQEVAKKSDRAVY 214
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQDLPLNKADYEEY 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-215 |
4.44e-12 |
|
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: 63.72 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdirkigldryrnqnVSVIFQsYNLITYMTALQ 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQ-FSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAMEITGVKVQNkTARALQLLERVgLSEAEAKRNVL-----QLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:cd03291 117 NIIFGVSYDEYRYKS-VVKACQLEEDI-TKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 178 AMDIIE--LFQELAhkeNKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:cd03291 195 EKEIFEscVCKLMA---NKTRILVTSKMEHLKKADKILIL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-213 |
5.01e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYyyeSNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYR 81
Cdd:COG3845 255 EVVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NQNVSVI---FQSYNLITYMTALQNVL-----TAMEITGVKVQNKTAR--ALQLLE----RVGLSEAEAKrnvlQLSGGQ 147
Cdd:COG3845 332 RLGVAYIpedRLGRGLVPDMSVAENLIlgryrRPPFSRGGFLDRKAIRafAEELIEefdvRTPGPDTPAR----SLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 148 QQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVthSQ---EVAKKSDR-AV 213
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAGAAVLLI--SEdldEILALSDRiAV 474
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-221 |
7.79e-12 |
|
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: 62.04 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTT-TLSLGCGLDvPKNGYVLYNGKDIRKIGLDRYRNQ 83
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTlILALFRFLE-AEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 nVSVIFQSYNLitYMTALQNVLTAM-EITGVKVqnktaralqlleRVGLSEAEAKRNvlqLSGGQQQRVAIARALSCNVD 162
Cdd:cd03369 84 -LTIIPQDPTL--FSGTIRSNLDPFdEYSDEEI------------YGALRVSEGGLN---LSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370010 163 LLIADEPTGNLDEQTAMDIielfQELAHKE--NKCIIVVTHSQEVAKKSDRAVYLSKKKLV 221
Cdd:cd03369 146 VLVLDEATASIDYATDALI----QKTIREEftNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-201 |
8.65e-12 |
|
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: 62.77 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYvlYNGKDIRKIGLDRYRNqnvsvifqsynlitymTALQNVLTAMEITGVKVQNK 118
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFRG----------------SELQNYFTKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 119 -----------TARALQLLERVglSEAEAK--------------RNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:cd03236 93 pqyvdlipkavKGKVGELLKKK--DERGKLdelvdqlelrhvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*...
gi 446370010 174 DEQTAMDIIELFQELAhKENKCIIVVTH 201
Cdd:cd03236 171 DIKQRLNAARLIRELA-EDDNYVLVVEH 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-211 |
9.90e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 26 NVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIG-LDRYR--------NQNVSVIFQ----SY 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLArglvylpeDRQSSGLYLdaplAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NLITYMTALQNVLTameitgvkvqnKTARALQLLER----VGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADE 168
Cdd:PRK15439 361 NVCALTHNRRGFWI-----------KPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446370010 169 PTGNLDEQTAMDIIELFQELAhKENKCIIVVTHS-QEVAKKSDR 211
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDlEEIEQMADR 472
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-217 |
1.16e-11 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 61.47 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTT---LSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnqnVSVIFQS-----YNLITYMTALQNVltamei 110
Cdd:cd03240 27 IVGQNGAGKTTIieaLKYALTGELPPNSKGGAHDPKLIREGEVRAQ---VKLAFENangkkYTITRSLAILENV------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 111 tgVKVQNKTARALQLLERVglseaeakrnvlQLSGGQQQ------RVAIARALSCNVDLLIADEPTGNLD-EQTAMDIIE 183
Cdd:cd03240 98 --IFCHQGESNWPLLDMRG------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeENIEESLAE 163
|
170 180 190
....*....|....*....|....*....|....
gi 446370010 184 LFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSK 217
Cdd:cd03240 164 IIEERKSQKNFQLIVITHDEELVDAADHIYRVEK 197
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-221 |
1.21e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdirkigldryrnqnVSVifqsynLITYMTALQ 102
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--------------VSA------LLELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAMEitgvkvqNKTARALQLlervGLSEAEAKRN-----------------VLQLSGGQQQRVAIARALSCNVDLLI 165
Cdd:COG1134 101 PELTGRE-------NIYLNGRLL----GLSRKEIDEKfdeivefaelgdfidqpVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 166 ADEPTGnldeqtAMDI------IELFQELAhKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:COG1134 170 VDEVLA------VGDAafqkkcLARIRELR-ESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLV 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-174 |
1.30e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGlDVPK---NGYVLYnGK---------DI-RKIG-------LDrYR- 81
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysNDLTLF-GRrrgsgetiwDIkKHIGyvssslhLD-YRv 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NQNV-SVI----FQSYNLITYMTALQNVLtameitgvkvqnktarALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK10938 352 STSVrNVIlsgfFDSIGIYQAVSDRQQKL----------------AQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRA 415
|
170
....*....|....*...
gi 446370010 157 LSCNVDLLIADEPTGNLD 174
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLD 433
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-220 |
2.03e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNgKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLS--LGCgldVP--KNGYVLYNGK--DIR-- 73
Cdd:PRK13549 257 EVILEVRNLTAWDPVN-PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQclFGA---YPgrWEGEIFIDGKpvKIRnp 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 ----KIGL-----DRYRNQNVSVIFQSYNlITyMTALQNVLTAMEITGVKVQNKTARALQLLeRVGLSEAEAKrnVLQLS 144
Cdd:PRK13549 333 qqaiAQGIamvpeDRKRDGIVPVMGVGKN-IT-LAALDRFTGGSRIDDAAELKTILESIQRL-KVKTASPELA--IARLS 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 145 GGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVThSQ--EVAKKSDRAVYLSKKKL 220
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVIS-SElpEVLGLSDRVLVMHEGKL 483
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-203 |
3.40e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLdyyyESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdvPK----NGYVLYNGKDIRKIGLD 78
Cdd:CHL00131 6 PILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQNVSVIFQsYNLitymtalqnvltamEITGV--------------KVQNKT-ARALQLLE-------RVGLSEAEA 136
Cdd:CHL00131 80 ERAHLGIFLAFQ-YPI--------------EIPGVsnadflrlaynskrKFQGLPeLDPLEFLEiineklkLVGMDPSFL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 137 KRNVLQ-LSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENkCIIVVTHSQ 203
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQ 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-201 |
4.47e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.74 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDY-YYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQ 83
Cdd:COG4615 328 LELRGVTYrYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR-Q 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITymtalqnvltamEITGVKVQNKTARALQLLERVGLSEAEAKRN----VLQLSGGQQQRVAiaralsc 159
Cdd:COG4615 407 LFSAVFSDFHLFD------------RLLGLDGEADPARARELLERLELDHKVSVEDgrfsTTDLSQGQRKRLA------- 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 160 nvdLLIA---DEPTGNLDEQTA-MDII-------ELFQELaHKENKCIIVVTH 201
Cdd:COG4615 468 ---LLVAlleDRPILVFDEWAAdQDPEfrrvfytELLPEL-KARGKTVIAISH 516
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-174 |
1.89e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIglDRYRnqnvsviFQSYnlITYMTAL 101
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSR-------FMAY--LGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 102 QNVLTAME-------ITGVKVQNKTARALQLlerVGLSEAEAKRnVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD 174
Cdd:PRK13543 94 KADLSTLEnlhflcgLHGRRAKQMPGSALAI---VGLAGYEDTL-VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-204 |
2.09e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQNVSVIFQSYNLITYMTA 100
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNV------LTAMEITGVKVQNKTARALQLLErvglSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD 174
Cdd:PRK10982 91 MDNMwlgrypTKGMFVDQDKMYRDTKAIFDELD----IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190
....*....|....*....|....*....|.
gi 446370010 175 EQTAMDIIELFQELahKENKC-IIVVTHSQE 204
Cdd:PRK10982 167 EKEVNHLFTIIRKL--KERGCgIVYISHKME 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-213 |
2.36e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 14 YESNGKNVAILENVN-FSFQKghfytilgPSGSGKTTTLslgcgldVPKNGYVLYNGKDIRKIGLDRYRNQnVSVIFQSY 92
Cdd:PTZ00265 1242 YQGDEEQNVGMKNVNeFSLTK--------EGGSGEDSTV-------FKNSGKILLDGVDICDYNLKDLRNL-FSIVSQEP 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NLITyMTALQNVLTAME---ITGVKVQNKTARALQLLERVglsEAEAKRNV----LQLSGGQQQRVAIARALSCNVDLLI 165
Cdd:PTZ00265 1306 MLFN-MSIYENIKFGKEdatREDVKRACKFAAIDEFIESL---PNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILL 1381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446370010 166 ADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAV 213
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-218 |
2.40e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 57.33 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 14 YESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGcgldvpkngyvLYNGKDIRKI-GLDRYRNQNVSVIFQsy 92
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------LYASGKARLIsFLPKFSRNKLIFIDQ-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 nlitymtalqnvltameitgvkvqnktaraLQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD--LLIADEPT 170
Cdd:cd03238 68 ------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446370010 171 GNLDEQTAMDIIELFQELAHKENKcIIVVTHSQEVAKKSDRAVYLSKK 218
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNT-VILIEHNLDVLSSADWIIDFGPG 164
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-217 |
2.86e-10 |
|
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: 57.64 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSlgcgldvpkngyVLYNGKDIRKIGLDryrnq 83
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLD------------VLAGRKTAGVITGE----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 nvsvifqsynlitymtalqnvltaMEITGVKVQNKTARALQLLERVGLSEAEAK-RNVLQ-------LSGGQQQRVAIAR 155
Cdd:cd03232 66 ------------------------ILINGRPLDKNFQRSTGYVEQQDVHSPNLTvREALRfsallrgLSVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 156 ALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTH--SQEVAKKSDRAVYLSK 217
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHqpSASIFEKFDRLLLLKR 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-168 |
2.86e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVAileNVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVG---PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYR-KL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSYNLITYMtalqnvltameITGVKVQNKTARALQLLERVGLSE----AEAKRNVLQLSGGQQQRVAIARALSCN 160
Cdd:PRK10522 399 FSAVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHklelEDGRISNLKLSKGQKKRLALLLALAEE 467
|
....*...
gi 446370010 161 VDLLIADE 168
Cdd:PRK10522 468 RDILLLDE 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-201 |
3.51e-10 |
|
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: 59.03 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 39 ILGPSGSGKTTTLSLGCGLDVPKNGYVlynGKDIrKIGldrYRNQNVSVIFQsynlITYMTALQNVLTAmEITGVKVQNK 118
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-KIS---YKPQYISPDYD----GTVEEFLRSANTD-DFGSSYYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 119 TARALQL---LERvglseaeakrNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKC 195
Cdd:COG1245 439 IIKPLGLeklLDK----------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
....*.
gi 446370010 196 IIVVTH 201
Cdd:COG1245 509 AMVVDH 514
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-191 |
4.20e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCG-LDVPKNGYVLyngkdIRkiGLDRYRNQnVSVIFQSynlitymTALQ 102
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVV-----IR--GTVAYVPQ-VSWIFNA-------TVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVL-----------TAMEITGVKvqnktaRALQLLERVGLSEAeAKRNVlQLSGGQQQRVAIARALSCNVDLLIADEPTG 171
Cdd:PLN03130 698 NILfgspfdperyeRAIDVTALQ------HDLDLLPGGDLTEI-GERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180
....*....|....*....|..
gi 446370010 172 NLDEQTAMDIIE--LFQELAHK 191
Cdd:PLN03130 770 ALDAHVGRQVFDkcIKDELRGK 791
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-218 |
6.71e-10 |
|
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: 56.01 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdvpkngYVLYNGKdirkigLDRYRNQNVSVIFQSynliTYMTALq 102
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL------WPWGSGR------IGMPEGEDLLFLPQR----PYLPLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 nvltameitgvkvqnkTARAlQLL---ERVglseaeakrnvlqLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAM 179
Cdd:cd03223 79 ----------------TLRE-QLIypwDDV-------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446370010 180 DIIELFQELahkenKCIIV-VTHSQEVAKKSDRAVYLSKK 218
Cdd:cd03223 129 RLYQLLKEL-----GITVIsVGHRPSLWKFHDRVLDLDGE 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-202 |
7.24e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKI---GLDRYRNQNVSVIFqSYNLITYMTA 100
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqkNLVAYVPQSEEVDW-SFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLTAMEITGVKVQNKTARALQLLERVGLSEAEaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMD 180
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFR-HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|..
gi 446370010 181 IIELFQELaHKENKCIIVVTHS 202
Cdd:PRK15056 181 IISLLREL-RDEGKTMLVSTHN 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-221 |
1.33e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 19 KNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKiglDRYRN-QNVSVIF-QSYNLIT 96
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK---RRKEFaRRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 97 YMTALQNvltameitgvkvqnktaraLQLLERV-GLSEAEAKRN-----------------VLQLSGGQQQRVAIARALS 158
Cdd:COG4586 110 DLPAIDS-------------------FRLLKAIyRIPDAEYKKRldelvelldlgelldtpVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH-SQEVAKKSDRAVYLSKKKLV 221
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHdMDDIEALCDRVIVIDHGRII 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-201 |
1.48e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYV----------------LYNGKDIR----------KIG 76
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgikvgylpqepqLDPEKTVRenveegvaevKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 LDRYrNQnvsvIFQSYN--------LITYMTALQNVLTAMEitGVKVQNKTARALQLLervGLSEAEAKrnVLQLSGGQQ 148
Cdd:PRK11819 102 LDRF-NE----IYAAYAepdadfdaLAAEQGELQEIIDAAD--AWDLDSQLEIAMDAL---RCPPWDAK--VTKLSGGER 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446370010 149 QRVAIARALSCNVDLLIADEPTGNLDeqtAMDIIELFQELaHKENKCIIVVTH 201
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFL-HDYPGTVVAVTH 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
120-221 |
1.70e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 120 ARALQLLERVGLSeAEAKRNvlQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDeqtaMDIIELFQELAHKENKCIIVV 199
Cdd:PRK11147 137 NRINEVLAQLGLD-PDAALS--SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFI 209
|
90 100
....*....|....*....|...
gi 446370010 200 THSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK11147 210 SHDRSfIRNMATRIVDLDRGKLV 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-215 |
1.88e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQnVSVIFQSYNLITYMTALQ 102
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLT-------AMEITGVKVQNKTARALQLlerVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDE 175
Cdd:PRK10575 105 LVAIgrypwhgALGRFGAADREKVEEAISL---VGLKPL-AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446370010 176 QTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYL 215
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVAL 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-201 |
2.02e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRnQN 84
Cdd:PRK10790 341 IDIDNVSFAYR-DDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-QG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIfQSYNLITYMTALQNVLTAMEITGVKVqnktaraLQLLERVGLSE-------------AEAKRNvlqLSGGQQQRV 151
Cdd:PRK10790 417 VAMV-QQDPVVLADTFLANVTLGRDISEEQV-------WQALETVQLAElarslpdglytplGEQGNN---LSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELahKENKCIIVVTH 201
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-201 |
2.08e-09 |
|
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: 56.87 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesnGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYnGKDIRKIGLDRYR-- 81
Cdd:TIGR03719 322 VIEAENLTKAF---GDKLLI-DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRda 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 ---NQNVsvifqsYNLITymtalqNVLTAMEITGVKVQnktARALqlLERVGLSEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:TIGR03719 397 ldpNKTV------WEEIS------GGLDIIKLGKREIP---SRAY--VGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446370010 159 CNVDLLIADEPTGNLDEQTAMDIIELFQELAhkenKCIIVVTH 201
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFA----GCAVVISH 498
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-216 |
2.44e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLdyyyesNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIR-KIGLDRY 80
Cdd:PRK10982 248 EVILEVRNL------TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 81 RN-------QNVSVIFQSYNLITYMTALQNVLTAMEITGVKVQNKTARALQ-LLERVGLSEAEAKRNVLQLSGGQQQRVA 152
Cdd:PRK10982 322 NHgfalvteERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQwVIDSMRVKTPGHRTQIGSLSGGNQQKVI 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370010 153 IARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLS 216
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-201 |
1.03e-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: 52.38 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 33 KGHFYTILGPSGSGKTTTL-SLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQNVsvifqsynlitymtalqnvltameit 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLArALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 112 gvkvqnktaralqllervglseaeaKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIEL-----FQ 186
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170
....*....|....*
gi 446370010 187 ELAHKENKCIIVVTH 201
Cdd:smart00382 110 LLKSEKNLTVILTTN 124
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
123-213 |
1.42e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.03 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 123 LQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD--LLIADEPTGNLDEQTAMDIIELFQELAHKENKcIIVVT 200
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVE 196
|
90
....*....|...
gi 446370010 201 HSQEVAKKSDRAV 213
Cdd:cd03270 197 HDEDTIRAADHVI 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-210 |
1.47e-08 |
|
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: 53.10 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 14 YESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQN-VSVIFQSY 92
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 NlitymTALQNVLTAMEITGVKVQNK-----TARALQLLERVGL----SEAEAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:cd03290 87 K-----PWLLNATVEENITFGSPFNKqrykaVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 164 LIADEPTGNLDEQTA-----MDIIELFQElahkENKCIIVVTHSQEVAKKSD 210
Cdd:cd03290 162 VFLDDPFSALDIHLSdhlmqEGILKFLQD----DKRTLVLVTHKLQYLPHAD 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-216 |
1.77e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAILENVNFSFQKGHFYTILGPSGSGKTTTL-SLGC---GLDVPKNGYVLYNG---KDIRKigldRYRNQnvsVIFQ 90
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASntdGFHIGVEGVITYDGitpEEIKK----HYRGD---VVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 91 SYNLI--TYMTALQNVLTAMEITGVKVQNKTARALQLLERV--------GLSEAeakRN-------VLQLSGGQQQRVAI 153
Cdd:TIGR00956 144 AETDVhfPHLTVGETLDFAARCKTPQNRPDGVSREEYAKHIadvymatyGLSHT---RNtkvgndfVRGVSGGERKRVSI 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH--SQEVAKKSDRAVYLS 216
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYqcSQDAYELFDKVIVLY 285
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
5-204 |
2.25e-08 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 52.66 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYEsngknvaileNVNFSFQKGH---FYTILGPSGSGKTT-----TLSL-GCGLDVPKNG---YVLYNGKDI 72
Cdd:cd03279 6 LELKNFGPFRE----------EQVIDFTGLDnngLFLICGPTGAGKSTildaiTYALyGKTPRYGRQEnlrSVFAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 73 RKIGLDRYRNQNVSVIFQSYNLiTYMTALQNVLTAmeitgvkvQNKTARALqllervglseaeaKRNVLQLSGGQQQRVA 152
Cdd:cd03279 76 AEVSFTFQLGGKKYRVERSRGL-DYDQFTRIVLLP--------QGEFDRFL-------------ARPVSTLSGGETFLAS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 153 IARALS----------CNVDLLIADEPTGNLDEQT---AMDIIELFQElahkENKCIIVVTHSQE 204
Cdd:cd03279 134 LSLALAlsevlqnrggARLEALFIDEGFGTLDPEAleaVATALELIRT----ENRMVGVISHVEE 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-215 |
2.61e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 11 DYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTL-SLGCGLDVPKnGYVLYNgkdiRKIGldrYRNQnvsvif 89
Cdd:PTZ00243 665 DDFFELEPK--VLLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEISE-GRVWAE----RSIA---YVPQ------ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 90 QSYnlITYMTALQNVLTAMEITGVKVQnKTARALQLLERV-----GLsEAEAKRNVLQLSGGQQQRVAIARALSCNVDLL 164
Cdd:PTZ00243 729 QAW--IMNATVRGNILFFDEEDAARLA-DAVRVSQLEADLaqlggGL-ETEIGEKGVNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446370010 165 IADEPTGNLDEQTAMDII-ELFqeLAHKENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVeECF--LGALAGKTRVLATHQVHVVPRADYVVAL 854
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-220 |
2.87e-08 |
|
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: 53.80 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGkdirkigldryrnqNVSVIFQSyNLITYMTALQN 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 104 VLTAMEITGVKVQnKTARALQLLERV----GLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAM 179
Cdd:TIGR00957 719 ILFGKALNEKYYQ-QVLEACALLPDLeilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446370010 180 DIIE-LFQELAHKENKCIIVVTHSQEVAKKSDRAVYLSKKKL 220
Cdd:TIGR00957 798 HIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-210 |
2.89e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.48 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 118 KTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD---LLIADEPTGNLDEQTAMDIIELFQELAHKENK 194
Cdd:TIGR00630 805 SISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNT 884
|
90
....*....|....*.
gi 446370010 195 cIIVVTHSQEVAKKSD 210
Cdd:TIGR00630 885 -VVVIEHNLDVIKTAD 899
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-188 |
4.12e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 21 VAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIGLDRYRNQNVSVIFQSYNLITYMTA 100
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLTAMEitgvKVQNKTARALQLLERVGLS-EAEAKRNVLQLSggQQQRVAIARALSCNVDLLIADEPTGNLdeqTAM 179
Cdd:PRK15439 104 KENILFGLP----KRQASMQKMKQLLAALGCQlDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASL---TPA 174
|
....*....
gi 446370010 180 DIIELFQEL 188
Cdd:PRK15439 175 ETERLFSRI 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-204 |
5.82e-08 |
|
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: 52.71 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYesNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKigldryrnq 83
Cdd:TIGR01257 1937 ILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--------- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 NVSVIFQSYNLITYMTALQNVLTAME-------ITGVKVQNKTARALQLLERVGLSeAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 157 LSCNVDLLIADEPTGNLDEQ-------TAMDIIelfqelahKENKCIIVVTHSQE 204
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQarrmlwnTIVSII--------REGRAVVLTSHSME 2131
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-217 |
6.83e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLyngkDIRkiGLDRYRNQn 84
Cdd:PLN03232 615 ISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV----VIR--GSVAYVPQ- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 85 VSVIFQSynlitymTALQNVL-----------TAMEITGVKvqnktaRALQLLERVGLSEAeAKRNVlQLSGGQQQRVAI 153
Cdd:PLN03232 687 VSWIFNA-------TVRENILfgsdfeserywRAIDVTALQ------HDLDLLPGRDLTEI-GERGV-NISGGQKQRVSM 751
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 154 ARALSCNVDLLIADEPTGNLDEQTAMDIIE--LFQELahkENKCIIVVTHSQEVAKKSDRAVYLSK 217
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDEL---KGKTRVLVTNQLHFLPLMDRIILVSE 814
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-201 |
7.20e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 138 RNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD-EQ--TAMDIIelfQELAHKENKCIIVVTH 201
Cdd:PRK13409 449 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQrlAVAKAI---RRIAEEREATALVVDH 512
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
120-174 |
9.90e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 9.90e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 120 ARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLD 174
Cdd:PRK10636 127 SRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
120-204 |
1.97e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 120 ARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMdiieLFQELAHKENKCIIVV 199
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVL----WLETYLLKWPKTFIVV 397
|
....*
gi 446370010 200 THSQE 204
Cdd:PLN03073 398 SHARE 402
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
143-213 |
2.39e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 2.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 143 LSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhkENKCIIVVTHSQ--EVAKKSDRAV 213
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA--AQGVAVLFVSSDlpEVLGVADRIV 467
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
103-217 |
2.81e-07 |
|
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: 48.51 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NVLTAME-ITGVKvQNKTARALQLLER--VGLSEAEAKRNVLQLSGGQQQRVAIARALS----CNVDLLIADEPTGNLDE 175
Cdd:cd03227 36 TILDAIGlALGGA-QSATRRRSGVKAGciVAAVSAELIFTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446370010 176 QTAMDIIELFQELAHKENKcIIVVTHSQEVAKKSDRAVYLSK 217
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQ-VIVITHLPELAELADKLIHIKK 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
143-211 |
3.99e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 3.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 143 LSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELaHKENKCIIVVTHSQ-EVAKKSDR 211
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMpEVLGMSDR 464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-201 |
5.11e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYEsnGKNvaILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVlYNGKDIRKIGLDRYRnqnvsv 87
Cdd:PRK11147 323 ENVNYQID--GKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLEVAYFDQHR------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 ifqsynlitymTALQNVLTAMEITG-----VKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD 162
Cdd:PRK11147 392 -----------AELDPEKTVMDNLAegkqeVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSN 460
|
170 180 190
....*....|....*....|....*....|....*....
gi 446370010 163 LLIADEPTGNLDEQTamdiIELFQELAHKENKCIIVVTH 201
Cdd:PRK11147 461 LLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSH 495
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
118-210 |
1.14e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 118 KTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD---LLIADEPTGNLDEQTAMDIIELFQELAHKENK 194
Cdd:cd03271 145 KIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNT 224
|
90
....*....|....*.
gi 446370010 195 cIIVVTHSQEVAKKSD 210
Cdd:cd03271 225 -VVVIEHNLDVIKCAD 239
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
137-201 |
1.71e-06 |
|
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: 46.80 E-value: 1.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370010 137 KRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTH 201
Cdd:cd03222 66 KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEH 130
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-189 |
2.89e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 2 ETILQFKNLDYYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTT---TLSLGCGLDVPKNGYVLYNGKDI-----R 73
Cdd:TIGR00956 757 EDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTllnVLAERVTTGVITGGDRLVNGRPLdssfqR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 74 KIGldrYRNQN-----VSVIFQSYNLITYMTALQNVLTAMEITGVKvqnktaRALQLLERVGLSEAEAKRNVLQLSGGQQ 148
Cdd:TIGR00956 837 SIG---YVQQQdlhlpTSTVRESLRFSAYLRQPKSVSKSEKMEYVE------EVIKLLEMESYADAVVGVPGEGLNVEQR 907
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446370010 149 QRVAIARALSCNVDLLI-ADEPTGNLDEQTAMDIIELFQELA 189
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA 949
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-201 |
2.97e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 25 ENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYV-LYNGKDIRKIGLDRYRNQNVSVIfqsynlITYM---TA 100
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQDQFAFEEFTVL------DTVImghTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 101 LQNVLT----------AMEITGVKVQN------------KTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALS 158
Cdd:PRK15064 92 LWEVKQerdriyalpeMSEEDGMKVADlevkfaemdgytAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446370010 159 CNVDLLIADEPTGNLDeqtaMDIIELFQELAHKENKCIIVVTH 201
Cdd:PRK15064 172 SNPDILLLDEPTNNLD----INTIRWLEDVLNERNSTMIIISH 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-205 |
3.70e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 4 ILQFKNLDYYYESNgknvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPK--NGYVLYNGKDIRKIGLDRYR 81
Cdd:PRK09580 1 MLSIKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 82 NQNVSVIFQsynlitymtalqnvlTAMEITGVKVQN--KTA-------RALQLLERVGLSE-AEAKRNVLQL-------- 143
Cdd:PRK09580 77 GEGIFMAFQ---------------YPVEIPGVSNQFflQTAlnavrsyRGQEPLDRFDFQDlMEEKIALLKMpedlltrs 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370010 144 -----SGGQQQRVAIARALSCNVDLLIADEPTGNLDEQtAMDIIELFQELAHKENKCIIVVTHSQEV 205
Cdd:PRK09580 142 vnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDID-ALKIVADGVNSLRDGKRSFIIVTHYQRI 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-209 |
4.33e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdirkIGLDRYRNQNVSVIFQSYNLITYMTALq 102
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK----VRMAVFSQHHVDGLDLSSNPLLYMMRC- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 nvltameITGVKVQNKTARalqlLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDeqtaMDII 182
Cdd:PLN03073 599 -------FPGVPEQKLRAH----LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAV 663
|
170 180
....*....|....*....|....*...
gi 446370010 183 E-LFQELAHKENKcIIVVTHSQEVAKKS 209
Cdd:PLN03073 664 EaLIQGLVLFQGG-VLMVSHDEHLISGS 690
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-213 |
8.35e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 123 LQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD--LLIADEPTGNLDEQTAMDIIELFQELAHKENKcIIVVT 200
Cdd:PRK00635 457 LSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNT-VLLVE 535
|
90
....*....|...
gi 446370010 201 HSQEVAKKSDRAV 213
Cdd:PRK00635 536 HDEQMISLADRII 548
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-221 |
9.34e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 22 AILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGlDVPK---------NGYVLYNGKDIRKIG---LDRYRnqnvSVIF 89
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDaprLARLR----AVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 90 QSYNLITYMTALQNVLTA----MEITGVKVQNKTARALQLLERVGlSEAEAKRNVLQLSGGQQQRVAIARALS------- 158
Cdd:PRK13547 90 QAAQPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAG-ATALVGRDVTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446370010 159 --CNVDLLIADEPTGNLDEQTAMDIIELFQELAHKENKCIIVVTHSQEVAKK-SDRAVYLSKKKLV 221
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIV 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-191 |
1.09e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 28 NFSFQKGHFYTILGPSGSGKTttlSLGCGLdvpKNGYVLYNGK---DIRKIGLDRYRNQN--VSVIFQSYNlitymTALQ 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS---ALARAL---AGELPLLSGErqsQFSHITRLSFEQLQklVSDEWQRNN-----TDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 103 NV------LTAMEItgvkVQN---KTARALQLLERVGLSeAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNL 173
Cdd:PRK10938 92 SPgeddtgRTTAEI----IQDevkDPARCEQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170
....*....|....*...
gi 446370010 174 DEQTAMDIIELFQELAHK 191
Cdd:PRK10938 167 DVASRQQLAELLASLHQS 184
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
116-208 |
1.20e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 116 QNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKC 195
Cdd:NF000106 119 KDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGAT 196
|
90
....*....|...
gi 446370010 196 IIVVTHSQEVAKK 208
Cdd:NF000106 197 VLLTTQYMEEAEQ 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-177 |
1.42e-05 |
|
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: 44.90 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 5 LQFKNLDYYYESNGKNVaiLENVNFSFQKGHFYTILGPSGSGKTT-TLSLGCGLDVpKNGYVLYNGKDIRKIGLDRYRNQ 83
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSlSLAFFRMVDI-FDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 84 nVSVIFQS---------YNLITYMTALQNVL-TAMEITGVKVQNKTARAlqllervGLSE--AEAKRNvlqLSGGQQQRV 151
Cdd:cd03288 97 -LSIILQDpilfsgsirFNLDPECKCTDDRLwEALEIAQLKNMVKSLPG-------GLDAvvTEGGEN---FSVGQRQLF 165
|
170 180
....*....|....*....|....*.
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMAT 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
140-199 |
1.85e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 1.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 140 VLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVV 199
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVI 460
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
118-201 |
2.50e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 118 KTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALScnvdlLIADepTGNLDEQTAMDIIELFQELAhkenkcii 197
Cdd:COG0419 134 EELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------- 198
|
....
gi 446370010 198 VVTH 201
Cdd:COG0419 199 IITH 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-221 |
2.72e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKdiRKIGldrYRNQNVSVIF-QSYNLITYMTal 101
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--ANIG---YYAQDHAYDFeNDLTLFDWMS-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 102 qnvltamEITGVKVQNKTARALqlLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDeqtaMDI 181
Cdd:PRK15064 407 -------QWRQEGDDEQAVRGT--LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD----MES 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446370010 182 IELFQELAHKENKCIIVVTHSQE-VAKKSDRAVYLSKKKLV 221
Cdd:PRK15064 474 IESLNMALEKYEGTLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-170 |
3.66e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAiLENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKiglDRYRNQNVSVIfqSY----- 92
Cdd:NF033858 12 GKTVA-LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVCPRI--AYmpqgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 93 --NLitYMTalqnvLTAME-------ITGVKVQNKTARALQLLERVGLSeAEAKRNVLQLSGGQQQRVAIARALSCNVDL 163
Cdd:NF033858 86 gkNL--YPT-----LSVFEnldffgrLFGQDAAERRRRIDELLRATGLA-PFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
....*..
gi 446370010 164 LIADEPT 170
Cdd:NF033858 158 LILDEPT 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-200 |
3.85e-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: 44.13 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYVLYNGKDIRKIGLDRYRnQNVSV 87
Cdd:TIGR01271 1221 QGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWR-KAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQsyNLITYMTALQNVLTAMEitgvkvQNKTARALQLLERVGL-SEAEAKRNVLQ---------LSGGQQQRVAIARAL 157
Cdd:TIGR01271 1297 IPQ--KVFIFSGTFRKNLDPYE------QWSDEEIWKVAEEVGLkSVIEQFPDKLDfvlvdggyvLSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446370010 158 SCNVDLLIADEPTGNLDEQTaMDIIElfQELAHKENKCIIVVT 200
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVT-LQIIR--KTLKQSFSNCTVILS 1408
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-174 |
4.76e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 23 ILENVNFSFQKGHFYTILGPSGSGKTTTLSL------GCGldvpknGYVLYNGKDIRKIGLDRYRNQnVSVIFQSYNLIT 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTfmrmveVCG------GEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 97 yMTALQNVLTAMEITGVKVQnktaRALQLL---ERVGlSEAEA-KRNVLQ----LSGGQQQRVAIARA-LSCNVDLLIAD 167
Cdd:PTZ00243 1398 -GTVRQNVDPFLEASSAEVW----AALELVglrERVA-SESEGiDSRVLEggsnYSVGQRQLMCMARAlLKKGSGFILMD 1471
|
....*..
gi 446370010 168 EPTGNLD 174
Cdd:PTZ00243 1472 EATANID 1478
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
79-215 |
7.54e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 79 RYRNQNVSVIFQSYNL--ITYMTALQnvLTAMEITGVKVQNKtaraLQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARA 156
Cdd:PRK00635 750 RFLPQVLEVRYKGKNIadILEMTAYE--AEKFFLDEPSIHEK----IHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYE 823
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446370010 157 LSCNVD---LLIADEPTGNLDEQTAMDIIELFQELAHkENKCIIVVTHSQEVAKKSDRAVYL 215
Cdd:PRK00635 824 LLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
76-208 |
8.76e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 76 GLDRYRNQNVSVIFQSYnlITYMTALQNVLTAME-----ITGVKVQNKTARALQLL-ERVGLSEAEAKRNVLQLSGGQQQ 149
Cdd:TIGR00618 880 GINQIKIQFDGDALIKF--LHEITLYANVRLANQsegrfHGRYADSHVNARKYQGLaLLVADAYTGSVRPSATLSGGETF 957
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446370010 150 RVAIARAL----------SCNVDLLIADEPTGNLDEQTAMDIIELFQELAhKENKCIIVVTHSQEVAKK 208
Cdd:TIGR00618 958 LASLSLALaladllstsgGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIR-EGSKMIGIISHVPEFRER 1025
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-177 |
9.48e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.53 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 8 KNLDYYYESNGKnvAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLdVPKNGYVLYNGKDIRKIGLDRYRnQNVSV 87
Cdd:cd03289 6 KDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWR-KAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 88 IFQSYnLITYMTALQNvltaMEITGvkvQNKTARALQLLERVGLseaeakRNVLQ----------------LSGGQQQRV 151
Cdd:cd03289 82 IPQKV-FIFSGTFRKN----LDPYG---KWSDEEIWKVAEEVGL------KSVIEqfpgqldfvlvdggcvLSHGHKQLM 147
|
170 180
....*....|....*....|....*.
gi 446370010 152 AIARALSCNVDLLIADEPTGNLDEQT 177
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPIT 173
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-176 |
1.56e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 24 LENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVLYNGKDIRKIgldryRNQNVSVIFQSYNLITYMTALQN 103
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446370010 104 VLTAMEItgvkvQNKTARALQLLERVGLSEAEAKRnVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDEQ 176
Cdd:PRK13541 91 LKFWSEI-----YNSAETLYAAIHYFKLHDLLDEK-CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| PRK09191 |
PRK09191 |
two-component response regulator; Provisional |
121-206 |
2.64e-04 |
|
two-component response regulator; Provisional
Pssm-ID: 236402 [Multi-domain] Cd Length: 261 Bit Score: 40.99 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 121 RALQL--LErvGLSEAEAKRnVLQLSGGQ------QQRVAIARALSCNVdLLIADEPTgnldeqTAMDIIELFQELAHke 192
Cdd:PRK09191 95 QAFLLtaLE--GFSVEEAAE-ILGVDPAEaealldDARAEIARQVATRV-LIIEDEPI------IAMDLEQLVESLGH-- 162
|
90
....*....|....
gi 446370010 193 NKCIIVVTHSQEVA 206
Cdd:PRK09191 163 RVTGIARTRAEAVA 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
143-217 |
3.33e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 143 LSGGQQQ------RVAIARALSCNVDLLIADEPTGNLDEQTAMDIIELFqELAHKENKCI---IVVTHSQEVAKKSDRAV 213
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDII-EYSLKDSSDIpqvIMISHHRELLSVADVAY 880
|
....
gi 446370010 214 YLSK 217
Cdd:PRK01156 881 EVKK 884
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-177 |
5.28e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 3 TILQFKNLDYYYesnGKNVAIlENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVlyngkdirKIG------ 76
Cdd:PRK11819 323 KVIEAENLSKSF---GDRLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI--------KIGetvkla 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 77 -LDRYR-----NQNVsviFQsynlitymtalqnvltamEITG----VKVQNKT--ARALqlLERVGLSEAEAKRNVLQLS 144
Cdd:PRK11819 391 yVDQSRdaldpNKTV---WE------------------EISGgldiIKVGNREipSRAY--VGRFNFKGGDQQKKVGVLS 447
|
170 180 190
....*....|....*....|....*....|....*
gi 446370010 145 GGQQQRVAIARAL--SCNVDLLiaDEPTGNLDEQT 177
Cdd:PRK11819 448 GGERNRLHLAKTLkqGGNVLLL--DEPTNDLDVET 480
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
67-217 |
7.73e-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: 40.03 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 67 YNGKDIRKIGLDRYRNQNVSVIFQSYNLiTYMTALQNVLTAMEITGvkvqnktaralqllervglseaeakrnvlQLSGG 146
Cdd:TIGR00606 1154 YRGQDIEYIEIRSDADENVSASDKRRNY-NYRVVMLKGDTALDMRG-----------------------------RCSAG 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 147 QQQ------RVAIARALSCNVDLLIADEPTGNLDEQT----AMDIIELFQELAHKENKCIIVVTHSQEVAKKSDRAVYLS 216
Cdd:TIGR00606 1204 QKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVE 1283
|
.
gi 446370010 217 K 217
Cdd:TIGR00606 1284 K 1284
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
109-216 |
8.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 109 EITGVKVQNKTARALQLLERVGLSEAEAKRNVLQLSGGQQQ------RVAIARALSCNVDLLIADEPTGNLDEQTAMDII 182
Cdd:PRK03918 755 ELTEGKYSGVRVKAEENKVKLFVVYQGKERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLV 834
|
90 100 110
....*....|....*....|....*....|....
gi 446370010 183 ELFQELAHKENKcIIVVTHSQEVAKKSDRAVYLS 216
Cdd:PRK03918 835 DIMERYLRKIPQ-VIIVSHDEELKDAADYVIRVS 867
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-202 |
9.82e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 18 GKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGyvlyngkdirkiglDRYRNQNVSVIFQSYNLITY 97
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG--------------KVDRNGEVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 98 MTALQNVLTAMEITGVKVQNKTARALQLLERVGLSEAeAKRNVLQLSGGQQQRVAIARALSCNVDLLIADEPTGNLDE-- 175
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEF-IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQtf 178
|
170 180
....*....|....*....|....*...
gi 446370010 176 -QTAMDIIELFQElahkENKCIIVVTHS 202
Cdd:PRK13546 179 aQKCLDKIYEFKE----QNKTIFFVSHN 202
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-202 |
1.02e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 12 YYYESNGKNVAILENVNFSFQKGHFYTILGPSGSGKTTTLSLGCGLDVPKNGYVlyngkDIRKigldryrnqNVSVIFQS 91
Cdd:PRK13545 28 FFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG---------SAALIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 92 YNLITYMTALQNVLTA---MEITGVKVQNKTARALQLLErVGlseAEAKRNVLQLSGGQQQRVAIARALSCNVDLLIADE 168
Cdd:PRK13545 94 SGLNGQLTGIENIELKglmMGLTKEKIKEIIPEIIEFAD-IG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 446370010 169 PTGNLDEQTAMDIIELFQELahKEN-KCIIVVTHS 202
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEF--KEQgKTIFFISHS 202
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
120-210 |
2.93e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 120 ARALQLLERVGLSeaeakrnVLQ-------LSGGQQQRVAIARALScNVD----LLIADEPTGNLDEQtamDI---IELF 185
Cdd:COG0178 804 ARKLQTLQDVGLG-------YIKlgqpattLSGGEAQRVKLASELS-KRStgktLYILDEPTTGLHFH---DIrklLEVL 872
|
90 100
....*....|....*....|....*
gi 446370010 186 QELAHKENKcIIVVTHSQEVAKKSD 210
Cdd:COG0178 873 HRLVDKGNT-VVVIEHNLDVIKTAD 896
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
142-217 |
3.72e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 142 QLSGGQQQ------RVAIARALSCNVD------LLIADEPTGNLDE---QTAMDIIELFQELAHKEnkcIIVVTHSQEVA 206
Cdd:PRK02224 781 QLSGGERAlfnlslRCAIYRLLAEGIEgdaplpPLILDEPTVFLDSghvSQLVDLVESMRRLGVEQ---IVVVSHDDELV 857
|
90
....*....|.
gi 446370010 207 KKSDRAVYLSK 217
Cdd:PRK02224 858 GAADDLVRVEK 868
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
41-81 |
4.44e-03 |
|
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).
Pssm-ID: 349782 [Multi-domain] Cd Length: 189 Bit Score: 36.76 E-value: 4.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446370010 41 GPSGSGKTTTLSlgcgldvpK--NGYVLYNGKDIRKIGLDRYR 81
Cdd:cd17873 7 GPTGVGKTTTLA--------KlaARYVLKKGKKVALITTDTYR 41
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
118-210 |
4.80e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 118 KTARALQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALScnvdlliaDEPTGN----LDEQT----AMDI---IELFQ 186
Cdd:PRK00349 806 KIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELS--------KRSTGKtlyiLDEPTtglhFEDIrklLEVLH 877
|
90 100
....*....|....*....|....
gi 446370010 187 ELAHKENKcIIVVTHSQEVAKKSD 210
Cdd:PRK00349 878 RLVDKGNT-VVVIEHNLDVIKTAD 900
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-213 |
5.73e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 123 LQLLERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCNVD--LLIADEPTGNLDEQTAMDIIELFQELAHKENKcIIVVT 200
Cdd:TIGR00630 469 LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNT-LIVVE 547
|
90
....*....|...
gi 446370010 201 HSQEVAKKSDRAV 213
Cdd:TIGR00630 548 HDEDTIRAADYVI 560
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
116-201 |
8.47e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 37.09 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370010 116 QNKTARALQLlERVGLSEAEAKRNVLQLSGGQQQRVAIARALSCN--------VDLLIADEPTGNLDEQT---AMDIIEL 184
Cdd:PRK10246 924 QRKASEALEL-EVVDTWQADAVRDTRTLSGGESFLVSLALALALSdlvshktrIDSLFLDEGFGTLDSETldtALDALDA 1002
|
90
....*....|....*..
gi 446370010 185 FqelaHKENKCIIVVTH 201
Cdd:PRK10246 1003 L----NASGKTIGVISH 1015
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
22-81 |
9.01e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 36.38 E-value: 9.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446370010 22 AILENVNFS----FQKGHFYTILGPSGSGKTTTL----SLgcgldvpkngYVLYNGKDIRKIGLDRYR 81
Cdd:COG1419 148 ALARRLPVAedplLDEGGVIALVGPTGVGKTTTIaklaAR----------FVLRGKKKVALITTDTYR 205
|
|
| |
