|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
5.43e-145 |
|
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: 405.13 E-value: 5.43e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKF 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPELQEFI 237
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-236 |
2.68e-127 |
|
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: 360.28 E-value: 2.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPELQEF 236
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
1.49e-81 |
|
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: 244.16 E-value: 1.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL-YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKF 80
Cdd:COG1122 1 IELENLsFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQ--ESALFDSlTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:COG1122 78 GLVFQnpDDQLFAP-TVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-225 |
3.76e-81 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 247.32 E-value: 3.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVD-EKllkkirRK 79
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpEK------RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
4.40e-81 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 246.53 E-value: 4.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTH--DVpnIFAIADKIAVLSSGKII 217
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHemDV--VRRICDRVAVLENGRIV 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-220 |
1.80e-78 |
|
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: 235.49 E-value: 1.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACD 220
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-225 |
1.84e-78 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 236.43 E-value: 1.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkVDEKLLKKIRRKF 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 161 YDEPTTGLDPittasiyELI---LNMEKRL---GVTSIIVTHDVPniFA--IADKIAVLSSGKIIACDTPENI 225
Cdd:COG1126 160 FDEPTSALDP-------ELVgevLDVMRDLakeGMTMVVVTHEMG--FAreVADRVVFMDGGRIVEEGPPEEF 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.88e-78 |
|
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: 245.20 E-value: 1.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKK 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 IRRKFGFLFQ--ESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAI 152
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
1.17e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 234.19 E-value: 1.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvdeKLLKKIRRKFG 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFpLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMEL 230
Cdd:COG1131 156 DEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-217 |
6.67e-77 |
|
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: 232.47 E-value: 6.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFG----KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-235 |
2.37e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 231.90 E-value: 2.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDekllkki 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 rRKFGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:COG1116 80 -PDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSS--GKIIA-----CDTPENIVKME 229
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEeidvdLPRPRDRELRT 237
|
....*.
gi 1053795292 230 LPELQE 235
Cdd:COG1116 238 SPEFAA 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
9.30e-76 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 229.16 E-value: 9.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFG----KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIkHVVGLL-KPDKGHIFIDGIDITKVDEKLLKK 75
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLdRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 IRR-KFGFLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:COG1136 83 LRRrHIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKIIA 218
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
4.15e-75 |
|
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: 227.77 E-value: 4.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQE--SALFDSLTVEENVAFPLREHLKLS-EKKLREIVRQKLELVGLSE-FGNKMPNELSGGMKKRVGLARAI 152
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-237 |
2.74e-74 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 226.96 E-value: 2.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKF 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPELQEFI 237
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFL 243
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-247 |
1.33e-71 |
|
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: 220.40 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL---YKKFGKLEV--LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:TIGR04521 1 IKLKNVsyiYQPGTPFEKkaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQ--ESALFdSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSE-FGNKMPNELSGGMKKRVGLARAIA 153
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPK-NLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI-------- 225
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVfsdvdele 238
|
250 260
....*....|....*....|...
gi 1053795292 226 -VKMELPELQEFitvqMKKFQSK 247
Cdd:TIGR04521 239 kIGLDVPEITEL----ARKLKEK 257
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-227 |
1.80e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 221.12 E-value: 1.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRK 79
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPLREhLKLSEKKLREIVRQKLELVGL--SEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-216 |
5.76e-71 |
|
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: 216.59 E-value: 5.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG----KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIR 77
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RK-FGFLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKI 216
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-218 |
2.27e-70 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 215.41 E-value: 2.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG----KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdekllkkiR 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSS--GKIIA 218
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-225 |
2.53e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 219.25 E-value: 2.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDI-TKVDEKllkkiRRKF 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPR-----ERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-226 |
2.82e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 218.05 E-value: 2.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFG---------------KLEVL---------RGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKG 56
Cdd:COG4175 3 KIEVRNLYKIFGkrperalklldqgksKDEILektgqtvgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 57 HIFIDGIDITKVDEKLLKKIRR-KFGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMP 135
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGL-EIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 136 NELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPittasiyeLI--------LNMEKRLGVTSIIVTHDVPNIFAIADK 207
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDP--------LIrremqdelLELQAKLKKTIVFITHDLDEALRLGDR 233
|
250
....*....|....*....
gi 1053795292 208 IAVLSSGKIIACDTPENIV 226
Cdd:COG4175 234 IAIMKDGRIVQIGTPEEIL 252
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
3.60e-69 |
|
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: 210.89 E-value: 3.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvDEKLLKKIRRKFG 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD-LEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPlrehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGK 215
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
5.46e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.83 E-value: 5.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRK 79
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 160 VYDEPTTGLDPITTASIYELI--LNmekRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLeeIN---RRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-217 |
9.13e-69 |
|
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: 214.53 E-value: 9.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKP---DKGHIFIDGIDITKVDEKLL 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 74 KKIR-RKFGFLFQESalFDSL----TVEENVAFPLREHLKLSEKKLREIVRQKLELVGLS---EFGNKMPNELSGGMKKR 145
Cdd:COG0444 81 RKIRgREIQMIFQDP--MTSLnpvmTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 146 VGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-225 |
1.46e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 214.94 E-value: 1.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKF 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-----DRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-216 |
3.08e-68 |
|
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: 209.69 E-value: 3.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvDEKLLKKIRRKFG 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-226 |
7.60e-68 |
|
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: 210.58 E-value: 7.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG---------------KLEVL---------RGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGH 57
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllakgksKEEILkktgqtvgvNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 58 IFIDGIDITKVDEKLLKKIRRK-FGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPN 136
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 137 ELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
250
....*....|
gi 1053795292 217 IACDTPENIV 226
Cdd:cd03294 240 VQVGTPEEIL 249
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-215 |
8.76e-68 |
|
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: 208.48 E-value: 8.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKF 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQ--ESALFdSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:cd03225 78 GLVFQnpDDQFF-GPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGK 215
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-237 |
8.07e-67 |
|
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: 207.15 E-value: 8.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLE-VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkKIRRKF 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFpLREHLKLSEKKLREIVRQKLELVGL--SEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPE-LQEFI 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDfVAEFV 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-217 |
1.08e-66 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 210.04 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-225 |
9.48e-65 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 201.57 E-value: 9.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR-----DRKIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:TIGR00968 76 FVFQHYALFKHLTVRDNIAFGL-EIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-225 |
1.88e-64 |
|
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: 200.54 E-value: 1.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-225 |
3.23e-64 |
|
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: 204.12 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdeklLKKIRRKFG 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR-----LPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-225 |
5.60e-64 |
|
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: 199.49 E-value: 5.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLRE---HLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-225 |
6.43e-64 |
|
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: 198.94 E-value: 6.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLK-----PDKGHIFIDGIDITKVDEKLLKkI 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLE-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDsLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLS-EFGNKM-PNELSGGMKKRVGLARAIAL 154
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRLhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRlgVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-218 |
1.61e-63 |
|
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: 198.87 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK----LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdeKLLKKI 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQ--ESALFDSLTVEENVAFPLREHLKLSEkklREIVRQKLELVGL-SEFGNKMPNELSGGMKKRVGLARAIA 153
Cdd:COG1124 78 RRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDR---EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
2.25e-63 |
|
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: 199.19 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKF--GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDItkVDEKLLKKIRRK 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQ--ESAlFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:TIGR04520 79 VGMVFQnpDNQ-FVGATVEDDVAFGL-ENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREI 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-226 |
8.29e-63 |
|
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: 197.19 E-value: 8.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKF 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS---RRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVA---FPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVAlgrYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIV 226
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
1.97e-62 |
|
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: 196.41 E-value: 1.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT--KVDEKLLKKIRR 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFgflfQESALFDSLTVEENVAFPLREHLKLS--------------EKKLREIVRQKLELVGLSEFGNKMPNELSGGMKK 144
Cdd:COG0411 84 TF----QNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 145 RVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPEN 224
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
.
gi 1053795292 225 I 225
Cdd:COG0411 240 V 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-216 |
2.03e-62 |
|
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: 193.38 E-value: 2.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEkllkKIRRKFG 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE----EVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVafplrehlklsekklreivrqklelvglsefgnkmpnELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-217 |
5.00e-62 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 194.71 E-value: 5.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKL-EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKF 80
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAF-------PLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
8.87e-62 |
|
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: 194.31 E-value: 8.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIrrkf 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFpLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
2.71e-61 |
|
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: 200.90 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF--GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGIDITKVDEKLLkk 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 iRRKFGFLFQE-SALFDSLTVEENVAFPLREhLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:COG1123 82 -GRRIGMVFQDpMTQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-227 |
4.80e-61 |
|
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: 191.88 E-value: 4.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT--KVDEKLLKKIRRK 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 fgflFQESALFDSLTVEENVAFPLREHLKLS---------EKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLAR 150
Cdd:cd03219 81 ----FQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 151 AIALEPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
6.16e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 192.19 E-value: 6.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRK 79
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENV---AFP----LREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAI 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGrtstWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-225 |
6.10e-60 |
|
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: 188.73 E-value: 6.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDekllKKIRRKFG 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLY-GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
3.36e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.60 E-value: 3.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdekllkkiRRKF 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQeSALFDS---LTVEENVAFPLREHLKLSE---KKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:COG1121 78 GYVPQ-RAEVDWdfpITVRDVVLMGRYGRRGLFRrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLsSGKIIACDTPENIVKME 229
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
8.30e-58 |
|
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: 182.84 E-value: 8.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-247 |
2.52e-57 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 184.10 E-value: 2.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL---YKKFGKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvDEKL-LKK 75
Cdd:PRK13637 3 IKIENLthiYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVkLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 IRRKFGFLFQ--ESALFDSlTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLS--EFGNKMPNELSGGMKKRVGLARA 151
Cdd:PRK13637 81 IRKKVGLVFQypEYQLFEE-TIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKmELP 231
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK-EVE 237
|
250 260
....*....|....*....|..
gi 1053795292 232 ELQEF------ITVQMKKFQSK 247
Cdd:PRK13637 238 TLESIglavpqVTYLVRKLRKK 259
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-232 |
3.72e-56 |
|
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: 179.45 E-value: 3.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEvLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvdekLLKKIRRKFG 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPE 232
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-225 |
5.76e-56 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 179.42 E-value: 5.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK-LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRK 79
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFP-------LREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAI 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-225 |
7.84e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 182.59 E-value: 7.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR-----DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLR---EHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-237 |
1.21e-55 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 182.36 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRR-KFGFLFQES 87
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 88 ALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTG 167
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 168 LDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPE-LQEFI 237
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEyVEEFI 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-218 |
5.10e-55 |
|
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: 176.47 E-value: 5.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 R-RKFGFLFQESALFDSLTVEENVAFPLREhlkLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLEL---AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKIIA 218
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVE 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-216 |
6.00e-55 |
|
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: 175.80 E-value: 6.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdekllkkiRRKFGF 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 83 LFQ-ESALFDS-LTVEENVAFPLREHLKLSE---KKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:cd03235 73 VPQrRSIDRDFpISVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-222 |
6.10e-55 |
|
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: 175.77 E-value: 6.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdeklLKKIRRK 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD----RKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPLRehLK-LSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYAR--LKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILnmEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTP 222
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLIL--EVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-216 |
1.48e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.62 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFG 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSlTVEENVAFPLR-EHLKLSEKKLREIvrqkLELVGLSE-FGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQlRERKFDRERALEL----LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.51e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 176.81 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK-LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDItKVDEKLLKKIRRK 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQ--ESALFdSLTVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK13639 80 VGIVFQnpDDQLF-APTVEEDVAFgPL--NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-227 |
1.50e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 176.45 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdekllKKIR-RKFGF 82
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQqRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 83 LFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYD 162
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 163 EPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-218 |
6.41e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.09 E-value: 6.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEvLRgVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKF 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-----ERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKLSEKKlREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-225 |
1.93e-52 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 172.19 E-value: 1.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLlkkiRRKFGFLFQESA 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKV----RRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 89 LFDSLTVEENVAFpLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:TIGR01188 77 VDEDLTGRENLEM-MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 169 DPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR01188 156 DPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-230 |
2.61e-52 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 169.82 E-value: 2.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDekLLKKIRRKF 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--MHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVL-ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKR-LGVtsIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMEL 230
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERgIGV--LITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
2.91e-52 |
|
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: 180.03 E-value: 2.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRK 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFdSLTVEENVAFplrEHLKLSEKKLREIvrqkLELVGLSEFGNKMPN-----------ELSGGMKKRVGL 148
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENITL---GDPDATDEEIIEA----ARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 149 ARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKrlGVTSIIVTHDvPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
3.07e-52 |
|
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: 168.53 E-value: 3.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGeITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkIRRKFG 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 162 DEPTTGLDPITTASIYELIlnmeKRLGVTSIIV--THDVPNIFAIADKIAVLSSGKIIAC 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLL----SELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-216 |
4.04e-52 |
|
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: 168.66 E-value: 4.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG----KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIR 77
Cdd:TIGR02982 2 ISIRNLNHYYGhgslRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKI 216
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-230 |
4.35e-52 |
|
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: 168.88 E-value: 4.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdeKLLKKIRRKFG 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKR-LGVtsIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMEL 230
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRgIGV--LITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-217 |
6.35e-52 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 171.45 E-value: 6.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 19 GVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQESalFDSL----T 94
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDP--YASLnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPLREHLKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpitt 173
Cdd:COG4608 114 VGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD---- 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1053795292 174 ASIYELILNM----EKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG4608 190 VSIQAQVLNLledlQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-237 |
3.28e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.19 E-value: 3.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT--KVDEKLlkkIRR 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERL---IRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 159 LVYDEPTTGLDPittasiyEL---ILNMEKRL---GVTSIIVTHDVPniFA--IADKIAVLSSGKIIACDTPENIVKME- 229
Cdd:PRK09493 158 MLFDEPTSALDP-------ELrheVLKVMQDLaeeGMTMVIVTHEIG--FAekVASRLIFIDKGRIAEDGDPQVLIKNPp 228
|
....*...
gi 1053795292 230 LPELQEFI 237
Cdd:PRK09493 229 SQRLQEFL 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
8.97e-51 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 166.37 E-value: 8.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIK------------HVvgllkpdKGHIFIDGIDI--TK 67
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndlipgaRV-------EGEILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 68 VDeklLKKIRRKFGFLFQESALFdSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGL-SEFGNKM---PNELSGGMK 143
Cdd:COG1117 85 VD---VVELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDRLkksALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 144 KRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRlgVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPE 223
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238
|
..
gi 1053795292 224 NI 225
Cdd:COG1117 239 QI 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-225 |
2.18e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 166.35 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT-KVDEKLLKKIRRKFGFLFQ--ESALFDSl 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSE-FGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPI 171
Cdd:PRK13634 102 TVEKDICFgPM--NFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 172 TTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.26e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 165.93 E-value: 2.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdeKLLKKIRR 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQE-SALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFaIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-225 |
3.08e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 168.48 E-value: 3.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdekllKKIRRKF 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-----PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-198 |
7.42e-50 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 161.82 E-value: 7.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDItKVDEKLLKKIRRKFGFLFQ--ESAL 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERRQRVGLVFQdpDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 90 FdSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLD 169
Cdd:TIGR01166 82 F-AADVDQDVAFGPL-NLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*....
gi 1053795292 170 PITTASIYELILNMEKRlGVTSIIVTHDV 198
Cdd:TIGR01166 160 PAGREQMLAILRRLRAE-GMTVVISTHDV 187
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
8.26e-50 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 164.26 E-value: 8.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK----LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEkllkki 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRkfGFLFQESALFDSLTVEENVAFPLRehLK-LSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLR--LRgVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSS--GKIIA 218
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-215 |
1.54e-49 |
|
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: 160.24 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG--KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRK 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSlTVEENVafplrehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEIL 159
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGK 215
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-225 |
2.32e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 166.28 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 162 DEPTTGLDpittasiYELILNM-------EKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK09452 169 DESLSALD-------YKLRKQMqnelkalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-219 |
4.42e-49 |
|
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: 159.52 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGF 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 83 lfqesalfdsltveenvafplrehlklsekklreiVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYD 162
Cdd:cd03214 78 -----------------------------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 163 EPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIAC 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-218 |
9.51e-49 |
|
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: 159.77 E-value: 9.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 26 KGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKL-LKKIRRKFGFLFQESALFDSLTVEENVAFPLR 104
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 105 EHlklSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNME 184
Cdd:cd03297 102 RK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|....
gi 1053795292 185 KRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-217 |
2.17e-48 |
|
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: 167.17 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK----LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLkPD-----KGHIFIDGIDITKVDEK 71
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDpaahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 72 LLKKIR-RKFGFLFQE--SALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKM---PNELSGGMKKR 145
Cdd:COG4172 85 ELRRIRgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 146 VGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVpNIFA-IADKIAVLSSGKII 217
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL-GVVRrFADRVAVMRQGEIV 236
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-225 |
2.81e-48 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 162.55 E-value: 2.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEvLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvdekLLKKIRRKF 80
Cdd:NF040840 1 MIRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDIT-----NLPPEKRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:NF040840 75 AYVYQNYMLFPHKTVFENIAFGLKLR-KVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 161 YDEPTTGLDPITTAsiyELILNME---KRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:NF040840 154 LDEPLSALDVQTRD---ELIREMKrwhREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREV 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
3.18e-48 |
|
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: 158.15 E-value: 3.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdeklLKKIRRKFG 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENvafpLREHLKLSEKKlREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03268 76 ALIEAPGFYPNLTAREN----LRLLARLLGIR-KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-225 |
4.39e-48 |
|
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: 161.51 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 32 IIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFGFLFQESALFDSLTVEENVAFPLREHlKLSE 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQSYALFPHMTVEENVAFGLKMR-KVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 112 KKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTS 191
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....
gi 1053795292 192 IIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
6.04e-48 |
|
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: 157.64 E-value: 6.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLlkkiRRKF 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY----RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFplreHLKLSEKKL-REIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRF----WAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1053795292 160 VYDEPTTGLDPITTASIYELIlNMEKRLGVTSIIVTHD 197
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELI-AAHLARGGAVLLTTHQ 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-197 |
1.27e-47 |
|
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: 157.18 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKF-GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKF 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLRehlkLSEKKLREI---VRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALE----VTGVPPREIrkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHD 197
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
4.45e-47 |
|
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: 153.55 E-value: 4.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGF 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 83 LFQesalfdsltveenvafplrehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVYD 162
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 163 EPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGK 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
9.05e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 154.56 E-value: 9.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGIDITKvdeklLKKIR 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA-----LPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQESALFDSLTVEENVAFPLREHLKLSEKKLReiVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRAR--VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNI 201
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-227 |
2.33e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 162.24 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFDSlTV 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRRIAVVPQRPHLFDT-TL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENvafplrehLKL-----SEKKLREIvrqkLELVGLSEFGNKMPN-------E----LSGGMKKRVGLARAIALEPEIL 159
Cdd:COG4987 426 REN--------LRLarpdaTDEELWAA----LERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 160 VYDEPTTGLDPITTASIYELILN-MEKRlgvTSIIVTHDvPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:COG4987 494 LLDEPTEGLDAATEQALLADLLEaLAGR---TVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-217 |
2.52e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKhVVGLLK-PDKGHIFIDGIDI---TKVDEKLLKKIR 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAGHQFdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQESALFDSLTVEEN-VAFPLREhLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPniFA--IADKIAVLSSGKII 217
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVE--FArkVASQVVYMEKGRII 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-218 |
2.71e-46 |
|
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: 153.42 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 22 LTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFGFLFQESALFDSLTVEENVAF 101
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 102 PLREHLKLSEKKlREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELIL 181
Cdd:cd03298 94 GLSPGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1053795292 182 NMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-227 |
3.10e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 155.56 E-value: 3.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIditKVDEKLLKKIRRK 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQE-SALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVpNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDL-DEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-214 |
5.49e-46 |
|
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: 153.39 E-value: 5.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkirrkfgFLFQESALFDSLTVE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 97 ENVAFPLREHLK-LSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTAS 175
Cdd:TIGR01184 73 ENIALAVDRVLPdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1053795292 176 IYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSG 214
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-226 |
5.97e-46 |
|
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: 153.58 E-value: 5.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdeKLLKKIRRKFG 81
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL--PMHERARLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKR-LGVtsIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIV 226
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERgIGV--LITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
6.30e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 154.19 E-value: 6.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITK--------VDE 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeIRLKPdrdgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 71 KLLKKIRRKFGFLFQESALFDSLTVEENVAF-PLREhLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLA 149
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHV-LGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 150 RAIALEPEILVYDEPTTGLDPittasiyEL---ILNMEKRL---GVTSIIVTHDVPniFA--IADKIAVLSSGKI 216
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDP-------ELvgeVLKVMRDLaeeGRTMLVVTHEMG--FArdVSSHVVFLHQGRI 232
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-197 |
8.68e-46 |
|
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: 152.51 E-value: 8.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF--GKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:TIGR02211 1 LLKCENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 R-RKFGFLFQESALFDSLTVEENVAFPLrehL--KLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA 153
Cdd:TIGR02211 81 RnKKLGFIYQFHHLLPDFTALENVAMPL---LigKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHD 197
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-223 |
1.28e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 160.33 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFdSLT 94
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPLREHlklSEKKLREIvrqkLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:COG1132 430 IRENIRYGRPDA---TDEEVEEA----AKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 164 PTTGLDPITTASIYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPE 223
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHE 559
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-166 |
1.75e-45 |
|
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: 149.34 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFDSLTVE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 97 ENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGN----KMPNELSGGMKKRVGLARAIALEPEILVYDEPTT 166
Cdd:pfam00005 78 ENLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-227 |
1.32e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 151.52 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT-KVDEKLLKKIRRKFGFLFQ--ESALFDSl 93
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSE-FGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPI 171
Cdd:PRK13641 102 TVLKDVEFgPK--NFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 172 TTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13641 180 GRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
2.27e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 151.03 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDekllkkiRRKF 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLRehLK-LSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVYLAR--LKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
3.07e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 150.38 E-value: 3.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENL-YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKvdeKLLKKIR 77
Cdd:PRK13636 5 ILKVEELnYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSR---KGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQ--ESALFdSLTVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:PRK13636 82 ESVGMVFQdpDNQLF-SASVYQDVSFgAV--NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
4.49e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 149.95 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENL-YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRK 79
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQES--ALFdSLTVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK13652 80 VGLVFQNPddQIF-SPTVEQDIAFgPI--NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI---------VK 227
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIflqpdllarVH 236
|
250
....*....|
gi 1053795292 228 MELPELQEFI 237
Cdd:PRK13652 237 LDLPSLPKLI 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
5.82e-44 |
|
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: 147.90 E-value: 5.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLE----VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdEKLlkKI 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPA--EA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENVAFPLREH-LKLSEKKLReiVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYgLKGDELTAR--LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
7.63e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 148.77 E-value: 7.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRrkf 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPlREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA------L 154
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 155 EPEILVYDEPTTGLDpittasIY--ELILNMEKRL----GVTSIIVTHDVpNIFAI-ADKIAVLSSGKIIACDTPEN 224
Cdd:PRK13548 158 PPRWLLLDEPTSALD------LAhqHHVLRLARQLaherGLAVIVVLHDL-NLAARyADRIVLLHQGRLVADGTPAE 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-217 |
1.55e-43 |
|
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: 154.07 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLkPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQE-- 86
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 87 SALFDSLTVEENVAFPLREH-LKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLRVHgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 165 TTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-227 |
1.79e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 148.73 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVD-EKLLKKIRRKFGFLFQ--ESALFDSlTVE 96
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIKPVRKKVGVVFQfpESQLFEE-TVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 97 ENVAFPlREHLKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTAS 175
Cdd:PRK13643 104 KDVAFG-PQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 176 IYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-227 |
2.26e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 147.93 E-value: 2.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLE------VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvDEKLLK 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 75 KIRRKFGFLFQ--ESALFDSLtVEENVAF-PlrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARA 151
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVATI-VEEDVAFgP--ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-223 |
5.48e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 146.41 E-value: 5.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRrkf 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESAL-FDsLTVEENVAFPLREHLkLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA------ 153
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRAPHG-SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 154 -LEPEILVYDEPTTGLDpittasIYE--LILNMEKRL---GVTSIIVTHDVpNIFA-IADKIAVLSSGKIIACDTPE 223
Cdd:COG4559 156 dGGPRWLFLDEPTSALD------LAHqhAVLRLARQLarrGGGVVAVLHDL-NLAAqYADRILLLHQGRLVAQGTPE 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-225 |
6.22e-43 |
|
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: 145.27 E-value: 6.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdeKLLKKIRRKFG 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENV---AFPLRehlklsEKKLREIVRQKLELV-GLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:cd03224 79 YVPEGRRIFPELTVEENLllgAYARR------RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-225 |
1.16e-42 |
|
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: 148.33 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIeNLYKKFGKLEvLRgVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdEKLL---KKI- 76
Cdd:COG4148 2 MLEV-DFRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-------EVLQdsaRGIf 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 ----RRKFGFLFQESALFDSLTVEENVAFPLReHLKLSEKKLR--EIVrqklELVGLSEFGNKMPNELSGGMKKRVGLAR 150
Cdd:COG4148 72 lpphRRRIGYVFQEARLFPHLSVRGNLLYGRK-RAPRAERRISfdEVV----ELLGIGHLLDRRPATLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 151 AIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:COG4148 147 ALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
1.29e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 146.77 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGK-----LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHI---FIDGIDITKVDE--- 70
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 71 ---------------KLLKKIRRKFGFLFQ--ESALFDSlTVEENVAFPLREhLKLSEKKLREIVRQKLELVGLSE-FGN 132
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDEsYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 133 KMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLS 212
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
....*
gi 1053795292 213 SGKII 217
Cdd:PRK13651 240 DGKII 244
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-223 |
1.41e-42 |
|
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: 151.83 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFdSLT 94
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPYLF-AGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPLREhlkLSEKKLREIvrqkLELVGLSEFGNKMPN-------E----LSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:COG4988 427 IRENLRLGRPD---ASDEELEAA----LEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 164 PTTGLDPITTASIYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPE 223
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHE 556
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-216 |
5.13e-42 |
|
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: 142.69 E-value: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 21 NLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdeklLKKIRRKFGFLFQESALFDSLTVEENVA 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQRPVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 101 FPLREHLKLS---EKKLREIVRQklelVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIY 177
Cdd:TIGR01277 93 LGLHPGLKLNaeqQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1053795292 178 ELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-217 |
7.03e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 143.23 E-value: 7.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKhVVGLLK-PDKGHIFIDG--IDI-TKVDEKLLKKIR 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGnhFDFsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQESALFDSLTVEEN-VAFPLREhLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRV-LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKrLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-216 |
8.00e-42 |
|
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: 140.81 E-value: 8.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFDSlTV 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVafplrehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTAS 175
Cdd:cd03246 93 AENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1053795292 176 IYELILNMEKRlGVTSIIVTHDvPNIFAIADKIAVLSSGKI 216
Cdd:cd03246 135 LNQAIAALKAA-GATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-226 |
8.52e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 143.97 E-value: 8.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENL-YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvDEKLLKKIRRK 79
Cdd:PRK13644 1 MIRLENVsYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQE-SALFDSLTVEENVAF-PlrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFgP--ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAiADKIAVLSSGKIIACDTPENIV 226
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-225 |
1.20e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 143.73 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDE-KLLKKIRRKFGFLFQ--ESALFDSl 93
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAF-PlrEHLKLSEKKLREIVRQKLELVGLSE-FGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPI 171
Cdd:PRK13649 102 TVLKDVAFgP--QNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 172 TTASIYELILNMEkRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK13649 180 GRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-226 |
1.76e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 146.33 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 5 ENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRK-FGFL 83
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 FQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 164 PTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIV 226
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
2.49e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.81 E-value: 2.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT-----KVDEKLLKK 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 IRRKFGFLFQESALFDSLTVEENVAfplrEHLKLSEKKLREIV----RQKLELVGLSEFGNKMPNELSGGMKKRVGLARA 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENII----EGPVIVKGEPKEEAtaraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELI--LNMEKRlgvTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIrqLAQEKR---TMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
2.74e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.56 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENL---YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvdEKLLKKIR 77
Cdd:PRK13650 4 IIEVKNLtfkYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQE-SALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPE 223
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPR 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
3.09e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.57 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL--YKKFGKlEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkKIRRK 79
Cdd:PRK13647 5 IEVEDLhfRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQE--SALFdSLTVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK13647 81 VGLVFQDpdDQVF-SSTVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 157 EILVYDEPTTGLDPITTASIYElILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPE 223
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
3.96e-41 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 141.37 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKirrKF 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK---RL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAF---PlreHLK--LSEKKlREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFgrfP---YSKgrLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVpNiFAI--ADKIAVLSSGKIIACDTPENIV 226
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDI-N-FAScyADHIVAMKDGRVVAQGTPEEII 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-242 |
8.10e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.87 E-value: 8.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKV----------DEK 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 72 LLKKIRRKFGFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGN-KMPNELSGGMKKRVGLAR 150
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 151 AIALEPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIV-KME 229
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFgNPQ 244
|
250
....*....|...
gi 1053795292 230 LPELQEFITVQMK 242
Cdd:PRK10619 245 SPRLQQFLKGSLK 257
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-217 |
8.43e-41 |
|
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: 139.31 E-value: 8.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKL-EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdekllKKIRRKFGF 82
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 83 LFQESalfDSLTVEENVAFPLREHLKLSEKKLrEIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYD 162
Cdd:cd03226 76 VMQDV---DYQLFTDSVREELLLGLKELDAGN-EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 163 EPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-217 |
1.63e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 140.05 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGL--LKPD---KGHIFIDGIDITKVDeklLKKI 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMD---VIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENVAFPLR-EHLKLSEKKLREIVRQKLELVGL-SEFGNKM---PNELSGGMKKRVGLARA 151
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKlNRLVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELILNMEKRLgvTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-225 |
4.33e-40 |
|
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: 141.40 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKL-LKKIRRKFGFLFQESALFDSLTVEEN 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIfLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 99 vafpLREHLKLSEKKLREIVRQKL-ELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIY 177
Cdd:TIGR02142 96 ----LRYGMKRARPSERRISFERViELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1053795292 178 ELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-218 |
4.87e-40 |
|
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: 137.72 E-value: 4.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFdSLT 94
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRNIGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAfplrehLKLSEKKLREIVRqKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:cd03245 94 LRDNIT------LGAPLADDERILR-AAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 164 PTTGLDpitTASIYELILNMEKRL-GVTSIIVTHDvPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03245 167 PTSAMD---MNSEERLKERLRQLLgDKTLIIITHR-PSLLDLVDRIIVMDSGRIVA 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-217 |
5.47e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.05 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 6 NLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQ 85
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 86 ES--ALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYD 162
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 163 EPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-214 |
1.28e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 137.52 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLlkkirrkf 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSG 214
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-228 |
1.30e-39 |
|
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: 143.74 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFDSlTV 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAfplrehlklsekKLREIVRQKL----ELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILV 160
Cdd:COG4618 423 AENIA------------RFGDADPEKVvaaaKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDvPNIFAIADKIAVLSSGKIIACDTPENIVKM 228
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHR-PSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-227 |
1.87e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.01 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 13 KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGIDITkvdEKLLKKIRRKFGFLFQE-SA 88
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLT---AKTVWDIREKVGIVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 89 LFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:PRK13640 96 QFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 169 DPITTASIYELILNMEKRLGVTSIIVTHDVpNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDI-DEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
1.88e-39 |
|
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: 136.65 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVD-EKLlkkIRRK 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRI---ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEEN---VAFPLREhlklsekklREIVRQKLELVG-----LSEFGNKMPNELSGGMKKRVGLARA 151
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENlllGAYARRD---------RAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIvkMELP 231
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL--LADP 227
|
....*
gi 1053795292 232 ELQEF 236
Cdd:COG0410 228 EVREA 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
2.32e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 138.83 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK-----LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDI-TKVDE---- 70
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgDKKNNheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 71 --------KLLKKIRRKFGFLFQ--ESALFDSlTVEENVAF-PLreHLKLSEKKLREIVRQKLELVGLSE-FGNKMPNEL 138
Cdd:PRK13631 101 tnpyskkiKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPV--ALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 139 SGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNmEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250 260
....*....|....*....|....*...
gi 1053795292 219 CDTPENI---------VKMELPELQEFI 237
Cdd:PRK13631 257 TGTPYEIftdqhiinsTSIQVPRVIQVI 284
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
2.51e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.12 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFidgiditkVDEKLLKKIRRKFGFL 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 FQESALFDSLTVEENVAFPLREHLklsekklREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQW-------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 164 PTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
1.08e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKVDEKLLKKIrr 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 kfGFLFQESALFDSLTVEENVAF--PLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:COG1129 82 --AIIHQELNLVPNLSVAENIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACD-----TPENIVKM 228
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-226 |
1.11e-38 |
|
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: 140.71 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFI----DGIDITKVDEK 71
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 72 LLKKIRRKFGFLFQESALFDSLTVEENvafpLREHLKLSEKKlrEIVRQK----LELVGLSE-----FGNKMPNELSGGM 142
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDN----LTEAIGLELPD--ELARMKavitLKMVGFDEekaeeILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 143 KKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTP 222
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....
gi 1053795292 223 ENIV 226
Cdd:TIGR03269 513 EEIV 516
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-217 |
1.50e-38 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 134.06 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIrrkfG 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD---LHKI----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENvafpLREH---LKLSEKKLREIvrqkLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:TIGR03740 74 SLIESPPLYENLTAREN----LKVHttlLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
1.94e-38 |
|
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: 133.89 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL---YKKfgKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRR 78
Cdd:cd03254 3 IEFENVnfsYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFdSLTVEENVAFPlrehlklSEKKLREIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVG 147
Cdd:cd03254 78 MIGVVLQDTFLF-SGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 148 LARAIALEPEILVYDEPTTGLDPITTASIYELILN-MEKRlgvTSIIVTHDvPNIFAIADKIAVLSSGKIIACDTPE 223
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGR---TSIIIAHR-LSTIKNADKILVLDDGKIIEEGTHD 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
1.95e-38 |
|
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: 133.17 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdEKLLKKIRRKFG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLRehLK-LSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQ--LKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-240 |
2.07e-38 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 134.37 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKkirRKF 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHL----KLSEKKlREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYGRSPWLslwgRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELpeLQEF 236
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGL--LRTV 234
|
....
gi 1053795292 237 ITVQ 240
Cdd:PRK11231 235 FDVE 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
4.74e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 132.69 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRK 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIA-GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
8.08e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 132.40 E-value: 8.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEvLRgVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKF 80
Cdd:PRK10771 1 MLKLTDITWLYHHLP-MR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKLSE---KKLREIVRQklelVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQNIGLGLNPGLKLNAaqrEKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-222 |
1.29e-37 |
|
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: 131.46 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL---YKKFGKLeVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRR 78
Cdd:cd03244 3 IEFKNVslrYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFDSlTVEENVAfPLREHlklSEKKLREIvrqkLELVGLSEFGNKMP-----------NELSGGMKKRVG 147
Cdd:cd03244 79 RISIIPQDPVLFSG-TIRSNLD-PFGEY---SDEELWQA----LERVGLKEFVESLPggldtvveeggENLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 148 LARAIALEPEILVYDEPTTGLDPITTASIYELIlnMEKRLGVTSIIVTHDVPNIFAiADKIAVLSSGKIIACDTP 222
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTI--REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-217 |
1.35e-37 |
|
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: 131.58 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFDSlTV 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLREhlklsekKLREIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:cd03251 93 AENIAYGRPG-------ATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 165 TTGLDPITTASIYELILN-MEKRlgvTSIIVTHDVPNIfAIADKIAVLSSGKII 217
Cdd:cd03251 166 TSALDTESERLVQAALERlMKNR---TTFVIAHRLSTI-ENADRIVVLEDGKIV 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-225 |
2.75e-37 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 131.65 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkKIRRKf 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH---QIARM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFL--FQESALFDSLTVEENVAFPLREHLKL--------------SEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKK 144
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVAQHQQLKTglfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 145 RVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPEN 224
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
.
gi 1053795292 225 I 225
Cdd:PRK11300 241 I 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-198 |
4.54e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 130.32 E-value: 4.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 6 NLYKKF--GKL--EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIR-RKF 80
Cdd:PRK11629 10 NLCKRYqeGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLRehlkLSEKKLREIVRQKLEL---VGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLL----IGKKKPAEINSRALEMlaaVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDV 198
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-198 |
7.59e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 129.51 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFG----KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKI 76
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 R-RKFGFLFQESALFDSLTVEENVAFP--LREHlklSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA 153
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPalLRGE---SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDV 198
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-229 |
8.37e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 130.01 E-value: 8.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 5 ENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdeKLLKKIRRKFGFLF 84
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL--PLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 85 QESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 165 TTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKME 229
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-211 |
1.34e-36 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 127.74 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 11 FGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkiRRKFGFLFQESALF 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------------GARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSL--TVEENVA---FPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPT 165
Cdd:NF040873 68 DSLplTVRDLVAmgrWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1053795292 166 TGLDPITTASIYELIlNMEKRLGVTSIIVTHDvPNIFAIADKIAVL 211
Cdd:NF040873 148 TGLDAESRERIIALL-AEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-225 |
1.60e-36 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 129.03 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 19 GVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD----KGHIFIDGIDITKvdeklLKKIRRKFGFLFQE--SALFDS 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLP-----LSIRGRHIATIMQNprTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 93 LTVEENVAFPLREHLKLSeKKLREIVRQKLELVGL---SEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLD 169
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLS-KQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 170 PITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-223 |
1.97e-36 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 128.89 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG-KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKF 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSlTVEENVAFplrEHLKLSEKKLREIVRQklelVGLSEFGNKMPN-----------ELSGGMKKRVGLA 149
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRY---GRPDATDEEVIEAAKA----AQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 150 RAIALEPEILVYDEPTTGLDPITTASIYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPE 223
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHE 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-226 |
3.73e-36 |
|
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: 127.99 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG--KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRK 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFdSLTVEENVAFPlrehlklSEKKLREIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGL 148
Cdd:cd03252 78 VGVVLQENVLF-NRSIRDNIALA-------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 149 ARAIALEPEILVYDEPTTGLDpitTASIYELILNMEKRL-GVTSIIVTHDVPNIFAiADKIAVLSSGKIIACDTPENIV 226
Cdd:cd03252 150 ARALIHNPRILIFDEATSALD---YESEHAIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
1.06e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.95 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQE-SALFDSLTV 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN---FEKLRKHIGIVFQNpDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLREHLkLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTAS 175
Cdd:PRK13648 102 KYDVAFGLENHA-VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 176 IYELILNMEKRLGVTSIIVTHDVPNIFAiADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-218 |
1.11e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 133.70 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRK-FGFLFQESALF 90
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSLTVEENVAFPlREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDP 170
Cdd:PRK10535 99 SHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1053795292 171 ITTASIYElILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKIIA 218
Cdd:PRK10535 178 HSGEEVMA-ILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-243 |
1.22e-35 |
|
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: 132.62 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGL--LKPDKGHI-----------FID------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 62 ------------GIDITKVDEKLLKKIRRKFGFLFQES-ALFDSLTVEENVAFPLREhlklSEKKLREIVRQKLELVGLS 128
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEE----IGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 129 EFGNKMPN---ELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIA 205
Cdd:TIGR03269 157 QLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1053795292 206 DKIAVLSSGKIIACDTPENIVK--MEL-PELQEFITVQMKK 243
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAvfMEGvSEVEKECEVEVGE 277
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-227 |
1.43e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.97 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDIT-KVDEKLLKKIRRKFGFLFQ--ESALFD 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 92 SlTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDP 170
Cdd:PRK13646 101 D-TVEREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 171 ITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-218 |
2.12e-35 |
|
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: 123.69 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllKKIRRKFG 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQesalfdsltveenvafplrehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03216 79 MVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 162 DEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-216 |
5.76e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 128.22 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRKFG 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-----ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFplreHLKLSEKKLREI---VRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSF----GLKLAGAKKEEInqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
9.78e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.76 E-value: 9.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllKK----- 75
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----------KPvrirs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 ----IRRKFGFLFQESALFDSLTVEENVA--FPLREHLKLSEKKLREIVRQKLElvglsEFG-----NKMPNELSGGMKK 144
Cdd:COG3845 74 prdaIALGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSE-----RYGldvdpDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 145 RVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA-CDTPE 223
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGtVDTAE 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
1.24e-34 |
|
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: 130.10 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFD 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 92 SlTVEENVAFPLREhlklsekKLREIVRQKLELVGLSEFGNKMP-----------NELSGGMKKRVGLARAIALEPEILV 160
Cdd:TIGR02857 410 G-TIAENIRLARPD-------ASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKrlGVTSIIVTHDvPNIFAIADKIAVL 211
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-219 |
1.30e-34 |
|
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: 123.92 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDK---GHIFIDGIDITKvdekllKKIRRKFGFLFQ 85
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP------DQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 86 ESALFDSLTVEENVAF--PLREHLKLSEKKLREIVRQK-LELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYD 162
Cdd:cd03234 89 DDILLPGLTVRETLTYtaILRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 163 EPTTGLDPITTASIYELILNMEKRlGVTSIIVTHD-VPNIFAIADKIAVLSSGKIIAC 219
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYS 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
1.49e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.87 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD-----KGHIFIDGIDITKVDEKLLKkI 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIE-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENVAFPLR-EHLKLSEKKLREIVRQKLELVGL-SEFGNKM---PNELSGGMKKRVGLARA 151
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKlNGLVKSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELILNMEKRLgvTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELP 231
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
....
gi 1053795292 232 ELQE 235
Cdd:PRK14267 242 ELTE 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-217 |
3.23e-33 |
|
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: 119.19 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKP--DKGHIFIDGIDITKvdekllKKIRRKFGFLFQESAL 89
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK------RSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 90 FDSLTVEENVAFPLrehlklsekKLREIvrqklelvglsefgnkmpnelSGGMKKRVGLARAIALEPEILVYDEPTTGLD 169
Cdd:cd03213 94 HPTLTVRETLMFAA---------KLRGL---------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1053795292 170 PITTASIYELILNMEKrLGVTSIIVTHDVPN-IFAIADKIAVLSSGKII 217
Cdd:cd03213 144 SSSALQVMSLLRRLAD-TGRTIICSIHQPSSeIFELFDKLLLLSQGRVI 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-232 |
3.42e-33 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 121.25 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 5 ENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkKIRRKFGFLF 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 85 QESALFDSLTVEENVA---FPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:PRK10253 88 QNATTPGDITVQELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMELPE 232
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIE 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-252 |
5.02e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 121.27 E-value: 5.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 13 KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKL--LKKIRRKFGFLFQ--ESA 88
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkeVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 89 LFDSlTVEENVAF-PLreHLKLSEKKLREIVRQKLELVGL-SEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTT 166
Cdd:PRK13645 103 LFQE-TIEKDIAFgPV--NLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 167 GLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI---------VKMELPELQEFi 237
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIfsnqelltkIEIDPPKLYQL- 258
|
250
....*....|....*
gi 1053795292 238 tvqMKKFQSKTASLF 252
Cdd:PRK13645 259 ---MYKLKNKGIDLL 270
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-216 |
6.56e-33 |
|
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: 117.92 E-value: 6.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllKKIRRKFGFL---FQESALFDS 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR--DAIRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 93 LTVEENVAFPLRehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVYDEPTTGLDPIT 172
Cdd:cd03215 93 LSVAENIALSSL---------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1053795292 173 TASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
6.58e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 120.50 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDK---GHIFIDGIDITKvDEKLLKKIR 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQR-EGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 R---KFGFLFQESALFDSLTVEENV------AFPL-REHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVG 147
Cdd:PRK09984 83 KsraNTGYIFQQFNLVNRLSVLENVligalgSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 148 LARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-217 |
1.87e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.84 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 7 LYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQE 86
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 87 SalFDSL----TVEENVAFPLREHLKLSEKKLREIVRQKLELVGL-SEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:PRK11308 101 P--YGSLnprkKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-214 |
2.58e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 120.58 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 13 KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQE--SALF 90
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSLTVEENVAFPLRE-HLKLSEKKLREIVRQKLELVGL-SEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:PRK15079 113 PRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1053795292 169 DPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSG 214
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-218 |
3.10e-32 |
|
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: 117.82 E-value: 3.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGflfQESA 88
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFG---QKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 89 LFDSLTVEENVAFpLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:cd03267 106 LWWDLPVIDSFYL-LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1053795292 169 DPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
1.26e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.50 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENL---YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIR 77
Cdd:PRK13642 4 ILEVENLvfkYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN---VWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFLFQE-SALFDSLTVEENVAFPLrEHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-235 |
2.50e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 116.30 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGI------DITKVDEKllk 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 75 KIRRKFGFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGL----SEFGNKMPNELSGGMKKRVGLAR 150
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 151 AIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVtsIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMEL 230
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
....*
gi 1053795292 231 PELQE 235
Cdd:PRK14246 245 NELTE 249
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-217 |
3.53e-31 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 115.33 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVlikhVVGLLK----PDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALF 90
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSlTVEENVAFPlREHLKLSEkklreiVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEIL 159
Cdd:cd03249 90 DG-TIAENIRYG-KPDATDEE------VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMekRLGVTSIIVTHDVPNIFAiADKIAVLSSGKII 217
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
3.58e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.95 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGK---LE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKV-DEKLLK 74
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 75 KIRRkfgfLFQESAL--FDSLTVEENVA--------FPLREHLKlseKKLREIVRQKLELVGLS-EfgNKMPNE---LSG 140
Cdd:COG1101 81 YIGR----VFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLT---KKRRELFRELLATLGLGlE--NRLDTKvglLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 141 GMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-222 |
4.74e-31 |
|
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: 121.27 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKF---GKLEVLRgVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDItkvdEKLLKKIRRKF 80
Cdd:TIGR01257 931 VKNLVKIFepsGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIvRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 161 YDEPTTGLDPITTASIYELILnmEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTP 222
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLL--KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-197 |
9.13e-31 |
|
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: 119.39 E-value: 9.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFDSlT 94
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPLREhlkLSEKKLREIvrqkLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:TIGR02868 425 VRENLRLARPD---ATDEELWAA----LERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 1053795292 164 PTTGLDPITTASIYELILNMEKRLGVtsIIVTHD 197
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-226 |
1.03e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 117.64 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEkllKKIRRKF 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESAL---FDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:PRK09536 80 ASVPQDTSLsfeFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 158 ILVYDEPTTGLDpittasIYELILNME--KRL---GVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIV 226
Cdd:PRK09536 160 VLLLDEPTASLD------INHQVRTLElvRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-222 |
2.04e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 113.95 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKvdeKLLKKIRR 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSK---RGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQ--ESALFDSlTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK13638 78 QVATVFQdpEQQIFYT-DIDSDIAFSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTP 222
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-238 |
2.30e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.33 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHV--VGLLKPD---KGHIFIDGIDI--TKVDEKll 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 74 kKIRRKFGFLFQESALFdSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGL-SEFGNKMPNE---LSGGMKKRVGLA 149
Cdd:PRK14239 83 -DLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 150 RAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLgvTSIIVTHDVPNIFAIADKIAVLSSGKIIAC-DTPENIVKM 228
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYnDTKQMFMNP 238
|
250
....*....|
gi 1053795292 229 ELPELQEFIT 238
Cdd:PRK14239 239 KHKETEDYIS 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-227 |
4.70e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 114.62 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKpDKGHI-----FIDGIDITKVDEKLLKKI-RRKFGFLFQ 85
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVtadrfRWNGIDLLKLSPRERRKIiGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 86 E--SALFDSLTVEENV--AFP---LREHL--KLSEKKLREIvrQKLELVGLSEFGNKM---PNELSGGMKKRVGLARAIA 153
Cdd:COG4170 97 EpsSCLDPSAKIGDQLieAIPswtFKGKWwqRFKWRKKRAI--ELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-216 |
5.73e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 114.56 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF-GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkiRRK 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-----DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPLREHlKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-214 |
1.07e-29 |
|
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: 110.99 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF------GK-LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFID----GIDITKVD 69
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 70 EKLLKKIRRK-FGFLFQesalFdsLTV------EENVAFPLREhLKLSEKKLREIVRQKL-------ELVGLSefgnkmP 135
Cdd:COG4778 84 PREILALRRRtIGYVSQ----F--LRViprvsaLDVVAEPLLE-RGVDREEARARARELLarlnlpeRLWDLP------P 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 136 NELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSG 214
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-222 |
1.57e-29 |
|
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: 110.19 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGK--LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRK 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSlTVEENVAfPLREHlklSEKKLREIVRqklelvgLSEFGNKmpneLSGGMKKRVGLARAIALEPEIL 159
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLD-PFDEY---SDEEIYGALR-------VSEGGLN----LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 160 VYDEPTTGLDPITTASIYELIlnMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTP 222
Cdd:cd03369 148 VLDEATASIDYATDALIQKTI--REEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
1.62e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.39 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdekLLKKIRRKFG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQesalFDSLTVEenvaFPLREHL-------KLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:PRK13536 118 VVPQ----FDNLDLE----FTVRENLlvfgryfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
1.92e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.21 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdekLLKKIRRKFG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVY 161
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIVKMEL 230
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-218 |
2.48e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.12 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENL-YKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLlkkiRRKFG 81
Cdd:COG3845 259 EVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLF-----QESALFDSLTVEENVAF------PLREHLKLSEKKLREIVRQKLElvglsEFGNKMPNE------LSGGMKK 144
Cdd:COG3845 335 VAYipedrLGRGLVPDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIE-----EFDVRTPGPdtparsLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 145 RVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
2.84e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.10 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----------GKL-----------EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIF 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 60 IDGIDITKVDEKLLKKIrrkfGFLF-QESALFDSLTVEENVAFpLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNEL 138
Cdd:COG4586 81 VLGYVPFKRRKEFARRI----GVVFgQRSQLWWDLPAIDSFRL-LKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 139 SGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-215 |
3.75e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.51 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKhVVGLLKPDKGHIFIDG--------IDITKVDeklL 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGrveffnqnIYERRVN---L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 74 KKIRRKFGFLFQESALFdSLTVEENVAFPLR---EHLKLsekKLREIVRQKLELVGL-SEFGNKMPN---ELSGGMKKRV 146
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLF-PMSVYDNVAYGVKivgWRPKL---EIDDIVESALKDADLwDEIKHKIHKsalDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 147 GLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGK 215
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-218 |
3.92e-29 |
|
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: 108.17 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKvdekLLKKIRRKFGFLFQESALFDSlTV 95
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD----LEKALSSLISVLNQRPYLFDT-TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLrehlklsekklreivrqklelvglsefgnkmpnelSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTAS 175
Cdd:cd03247 92 RNNLGRRF-----------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1053795292 176 IYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGKIIA 218
Cdd:cd03247 137 LLSLIFEVLK--DKTLIWITHHLTGI-EHMDKILFLENGKIIM 176
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
4.82e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.26 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGL--LKPD---KGHIFIDGIDI--TKVDEKllk 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 75 KIRRKFGFLFQESALFdSLTVEENVAFPLR------EHLKLSEKKLREI-----VRQKLELVGLSefgnkmpneLSGGMK 143
Cdd:PRK14243 88 EVRRRIGMVFQKPNPF-PKSIYDNIAYGARingykgDMDELVERSLRQAalwdeVKDKLKQSGLS---------LSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 144 KRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLgvTSIIVTHDVPNIFAIADKIAVLSS---------G 214
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVeltegggryG 235
|
250
....*....|.
gi 1053795292 215 KIIACDTPENI 225
Cdd:PRK14243 236 YLVEFDRTEKI 246
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-227 |
1.25e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 110.60 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEV-LRGVN---LTINKGEITAIIGKSGSGKTVLIKHVVGLLK-PDK---GHIFIDGIDITKVDEKL 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 73 LKKI-RRKFGFLFQESalFDSLTVEENVAFPLREHLKLSEKKLREIVRQK----LELVGLSEFGNKM---PNELSGGMKK 144
Cdd:PRK11022 83 RRNLvGAEVAMIFQDP--MTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRaidlLNQVGIPDPASRLdvyPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 145 RVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPEN 224
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
...
gi 1053795292 225 IVK 227
Cdd:PRK11022 241 IFR 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-220 |
1.46e-28 |
|
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: 108.00 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKF----------------------GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIf 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 60 idgiditkvdekllkKIRRKFGFLFQESALFD-SLTVEENVAFPLREhLKLSEKKLREIVRQKLELVGLSEFGNKMPNEL 138
Cdd:cd03220 80 ---------------TVRGRVSSLLGLGGGFNpELTGRENIYLNGRL-LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 139 SGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
..
gi 1053795292 219 CD 220
Cdd:cd03220 223 DG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
5.65e-28 |
|
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: 107.09 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKG---HIFidGIDITKVDeklLKKIR 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGED---VWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 RKFGFL-------FQE---------SALFDSLTVEENVafplrehlklsEKKLREIVRQKLELVGLSEFGNKMPNELSGG 141
Cdd:COG1119 78 KRIGLVspalqlrFPRdetvldvvlSGFFDSIGLYREP-----------TDEQRERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 142 MKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-225 |
7.84e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.81 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIeNLYKKFGKLEVlrGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKL-LKKIRRK 79
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENvafpLREHLKlseKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGN----LRYGMA---KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 160 VYDEPTTGLD-PITTasiyELILNME---KRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK11144 151 LMDEPLASLDlPRKR----ELLPYLErlaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-228 |
8.33e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 8.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKVDEKLLKKI------RRKFGflfqe 86
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIayvpedRKGEG----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 87 saLFDSLTVEENVAFPLREHLK----LSEKKLREIVRQKLELVGLsefgnKMPN------ELSGGMKKRVGLARAIALEP 156
Cdd:COG1129 341 --LVLDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIAC-----DTPENIVKM 228
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGEldreeATEEAIMAA 489
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-227 |
8.80e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 111.37 E-value: 8.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGH--IF---IDGIDItkvdekllkKI 76
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFgqpVDAGDI---------AT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDSLTVEENvafpLREHLKL---SEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA 153
Cdd:NF033858 338 RRRVGYMSQAFSLYGELTVRQN----LELHARLfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 154 LEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHdvpniF----AIADKIAVLSSGKIIACDTPENIVK 227
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH-----FmneaERCDRISLMHAGRVLASDTPAALVA 486
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-225 |
2.85e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.94 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG----------IDIT 66
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 67 KVDEKLLKKIR-RKFGFLFQE--SALFDSLTVEENVAFPLREHLKLS-EKKLREiVRQKLELVGLSE---FGNKMPNELS 139
Cdd:PRK10261 92 EQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASrEEAMVE-AKRMLDQVRIPEaqtILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 140 GGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIAC 219
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
....*.
gi 1053795292 220 DTPENI 225
Cdd:PRK10261 251 GSVEQI 256
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-223 |
3.06e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.15 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGL--LKPDKGHIFIDGIDIT--KVDEkllkkiRR 78
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILelSPDE------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFG-FL-FQESALFDSLTVEE--NVAFPLREHLKLSEKKLREIVRQKLELVGLSE-FGNKMPNE-LSGGMKKRVGLARAI 152
Cdd:COG0396 76 RAGiFLaFQYPVEIPGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 153 ALEPEILVYDEPTTGLDpITTASIYELILNMEKRLGVTSIIVTHdVPNI--FAIADKIAVLSSGKIIACDTPE 223
Cdd:COG0396 156 LLEPKLAILDETDSGLD-IDALRIVAEGVNKLRSPDRGILIITH-YQRIldYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-217 |
3.73e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.56 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 27 GEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQE--SALFDSLTVEENVAFPLR 104
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 105 EHLKLSEKKLREIVRQKLELVGL-SEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNM 183
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190
....*....|....*....|....*....|....
gi 1053795292 184 EKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-217 |
4.06e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLR----GVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD-----KGHIFIDGIDITKVDEK 71
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRtvvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 72 LLKKIR-RKFGFLFQESALfdSLTVEENVAFPLREHLKLSEKKLREIVR----QKLELVGLSEFGNKM---PNELSGGMK 143
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEPMV--SLNPLHTLEKQLYEVLSLHRGMRREAARgeilNCLDRVGIRQAAKRLtdyPHQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 144 KRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-225 |
6.60e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.96 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 21 NLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGIDITKVDEKLLKKIR-RKFGFLFQE--SALFDSLT 94
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRaEQISMIFQDpmTSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPLREHLKLSEKK-LREIVRQkLELVGLSEFGNKM---PNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDP 170
Cdd:PRK09473 116 VGEQLMEVLMLHKGMSKAEaFEESVRM-LDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 171 ITTASIYELiLNMEKRLGVTSII-VTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK09473 195 TVQAQIMTL-LNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
1.19e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDgiditkvdekllKKIRrkFGFL 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 FQESALFDSLTVEENVAFPLREHLKLsEKKLREIVRQ----------------KLELVG-----------LSEFG----- 131
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLDGDAELRAL-EAELEELEAKlaepdedlerlaelqeEFEALGgweaearaeeiLSGLGfpeed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 132 -NKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpitTASIY---ELILNMEKrlgvTSIIVTHDVpnIF--AIA 205
Cdd:COG0488 146 lDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwleEFLKNYPG----TVLVVSHDR--YFldRVA 216
|
250
....*....|..
gi 1053795292 206 DKIAVLSSGKII 217
Cdd:COG0488 217 TRILELDRGKLT 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
1.42e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.03 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvDEKLLKKIRRKF 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVA----FPLREHLKLSEKKLREIVRQklelvgLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAmggfFAERDQFQERIKWVYELFPR------LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDT 221
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-217 |
1.43e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.72 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF---------GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEK 71
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 72 LL-KKIRrkfgFLFQESAlfDSLTVEENVA----FPLREHLKLSEKKLREIVRQKLELVGL-SEFGNKMPNELSGGMKKR 145
Cdd:PRK15112 84 YRsQRIR----MIFQDPS--TSLNPRQRISqildFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 146 VGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-219 |
1.90e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.22 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIkhvvGLL----KPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFd 91
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLtrawDPQQGEILLNGQPIADYSEAAL---RQAISVVSQRVHLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 92 SLTveenvafpLREHLKL-----SEKKLREIVRQklelVGLSEF--GNKMPN--------ELSGGMKKRVGLARAIALEP 156
Cdd:PRK11160 427 SAT--------LRDNLLLaapnaSDEALIEVLQQ----VGLEKLleDDKGLNawlgeggrQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKrlGVTSIIVTHdvpNIFAIA--DKIAVLSSGKIIAC 219
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH---RLTGLEqfDRICVMDNGQIIEQ 554
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-217 |
2.61e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.25 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 6 NLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLlkPDK-------GHIFIDGIDITKVDEKLlkKIRR 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM--NDKvsgyrysGDVLLGGRSIFNYRDVL--EFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFdSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGL----SEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:PRK14271 102 RVGMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRLgvTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-213 |
2.70e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEkllKKIRRKFGFLFQESALFDSlTV 95
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIYRQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLR-EHLKLSEKKLREivrqklelvGLSEFG------NKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:PRK10247 98 YDNLIFPWQiRNQQPDPAIFLD---------DLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1053795292 169 DPITTASIYELILNMEKRLGVTSIIVTHDVPNIfAIADKIAVLSS 213
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQP 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-241 |
3.49e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKkirRKFGFLFQESALFDSLTV 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVA---FPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPIT 172
Cdd:PRK10575 103 RELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 173 TASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIvkMELPELQEFITVQM 241
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL--MRGETLEQIYGIPM 249
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-227 |
3.65e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 106.67 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 7 LYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGIDITKvdekllKKIRRKFGFL 83
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA------KEMRAISAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 FQESALFDSLTVEENVAFP--LREHLKLSEKKLREIVRQKLELVGLSEFGNKM---PNE---LSGGMKKRVGLARAIALE 155
Cdd:TIGR00955 105 QQDDLFIPTLTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDvPN--IFAIADKIAVLSSGKIIACDTPENIVK 227
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQ-PSseLFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-217 |
4.17e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.94 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVlikhvVGL----LKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQE--SAL 89
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 90 FDSLTVEENVAFPLREHLK-LSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTG 167
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1053795292 168 LDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-215 |
4.57e-26 |
|
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: 101.01 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkirrKFGFLFQESALFdSLTV 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------------SIAYVSQEPWIQ-NGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFplreHLKLSEKKLREIVR--------QKLELVGLSEFGNKMPNeLSGGMKKRVGLARAIALEPEILVYDEPTTG 167
Cdd:cd03250 83 RENILF----GKPFDEERYEKVIKacalepdlEILPDGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1053795292 168 LDPITTASIYELILNMEKRLGVTSIIVTHDVpNIFAIADKIAVLSSGK 215
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
5.24e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIrrKF 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--GI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENV---AFPLREHLKLS---EKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLyigRHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYeLILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSG-----KIIACDTPENIVKM 228
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVRL 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-227 |
1.08e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----------------------GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 59 FIDGiditkvdekllkkirrKFGFLFQESALFD-SLTVEENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNkMP-N 136
Cdd:COG1134 84 EVNG----------------RVSALLELGAGFHpELTGRENIYLNGR-LLGLSRKEIDEKFDEIVEFAELGDFID-QPvK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 137 ELSGGMKKRVGLARAIALEPEILVYDEPT-TGlDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGK 215
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|..
gi 1053795292 216 IIACDTPENIVK 227
Cdd:COG1134 224 LVMDGDPEEVIA 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-216 |
1.24e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.19 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFdSLTV 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLRehlklseKKLREIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:TIGR00958 572 RENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 165 TTGLDPITTASIYELilnmEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKI 216
Cdd:TIGR00958 645 TSALDAECEQLLQES----RSRASRTVLLIAHRLSTV-ERADQILVLKKGSV 691
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-216 |
1.53e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvdeKLLKKIRRKF 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA----RLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLF--QESALFDSLTVEENVAFPLREHLKlSEKKLREIVRQ---KLEL---VGLSEFGNKMPNELsggMKkrvGLARai 152
Cdd:PRK15439 87 GIYLvpQEPLLFPNLSVKENILFGLPKRQA-SMQKMKQLLAAlgcQLDLdssAGSLEVADRQIVEI---LR---GLMR-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 153 alEPEILVYDEPTTGLDPITTASIYELIlNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK15439 158 --DSRILILDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-196 |
3.26e-25 |
|
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: 98.58 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRrkfgFLFQESALFD 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL----YLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 92 SLTVEENVAFPLREHlklseKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPI 171
Cdd:TIGR01189 87 ELSALENLHFWAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*
gi 1053795292 172 TTASIYELILNMEKRLGVTsIIVTH 196
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIV-LLTTH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-217 |
4.24e-25 |
|
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: 98.37 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGL--LKPDKGHIFIDGIDITK--VDEKLLKKIr 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlpPEERARLGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 rkfGFLFQESALFDSLTVEEnvaFplrehlklsekkLREIvrqklelvglsefgnkmpNE-LSGGMKKRVGLARAIALEP 156
Cdd:cd03217 80 ---FLAFQYPPEIPGVKNAD---F------------LRYV------------------NEgFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 157 EILVYDEPTTGLDpITTASIYELILNMEKRLGVTSIIVTHdVPNIFA--IADKIAVLSSGKII 217
Cdd:cd03217 124 DLAILDEPDSGLD-IDALRLVAEVINKLREEGKSVLIITH-YQRLLDyiKPDRVHVLYDGRIV 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
5.28e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 5.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgiditKVDEKLlkkirrKF 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFD-SLTVEENVAfplrehlKLSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:COG0488 381 GYFDQHQEELDpDKTVLDELR-------DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEkrlGvTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-217 |
1.52e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIkhvvGLLK----PDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQES 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQrvfdPQSGRILIDGTDIRTVT---RASLRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 88 ALFDSlTVEEN--VAFP------LREHLKLSEKkLREIVRQKLEL---VGlsEFGNKmpneLSGGMKKRVGLARAIALEP 156
Cdd:PRK13657 419 GLFNR-SIEDNirVGRPdatdeeMRAAAERAQA-HDFIERKPDGYdtvVG--ERGRQ----LSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGKII 217
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTV-RNADRILVFDNGRVV 548
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-217 |
1.60e-24 |
|
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: 97.98 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKF 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 ------GFLFQESAlfDSLTVEENVAFPLREHL-KLSEK---KLREIVRQKLELVGLSEFG-NKMPNELSGGMKKRVGLA 149
Cdd:TIGR02323 83 lmrtewGFVHQNPR--DGLRMRVSAGANIGERLmAIGARhygNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 150 RAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-217 |
1.63e-24 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 98.18 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGllKPD----KGHIFIDGIDITKVDekllKKI 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLE----PEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFG-FL-FQESALFDSLTVEENVAFPL---REHLKLSEK---KLREIVRQKLELVGLSE-FGNKMPNE-LSGGMKKRV 146
Cdd:CHL00131 81 RAHLGiFLaFQYPIEIPGVSNADFLRLAYnskRKFQGLPELdplEFLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 147 GLARAIALEPEILVYDEPTTGLDPITTASIYELIlNMEKRLGVTSIIVTHdVPNI--FAIADKIAVLSSGKII 217
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGI-NKLMTSENSIILITH-YQRLldYIKPDYVHVMQNGKII 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-217 |
3.96e-24 |
|
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: 100.66 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFDSlT 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTVLFND-T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPlREHLKlsekklREIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDE 163
Cdd:COG5265 448 IAYNIAYG-RPDAS------EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 164 PTTGLDPITTASIYELILNMEKrlGVTSIIVTHDVPNIfAIADKIAVLSSGKII 217
Cdd:COG5265 521 ATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTI-VDADEILVLEAGRIV 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-216 |
4.19e-24 |
|
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: 96.39 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRRKFGFLFQESALFdSLTV 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL---HSKVSLVGQEPVLF-ARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAF-----PLREHLKLSEKKLREIVRQKLELVGLSEFGNKmPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDP 170
Cdd:cd03248 105 QDNIAYglqscSFECVKEAAQKAHAHSFISELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1053795292 171 ITTASIYELILNMEKRlgVTSIIVTHDVpNIFAIADKIAVLSSGKI 216
Cdd:cd03248 184 ESEQQVQQALYDWPER--RTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
1.46e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.17 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvdeklLKKIRRKF 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------DPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFpLREHLKLSEKKLREivrqKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK13539 76 HYLGHRNAMKPALTVAENLEF-WAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTH 196
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRAHLAQ-GGIVIAATH 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-217 |
1.78e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.38 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKF 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 ------GFLFQESA--LFDSLTVEENVAFPLrehLKLSEK---KLREIVRQKLELVGLSEfgNKM---PNELSGGMKKRV 146
Cdd:PRK11701 86 llrtewGFVHQHPRdgLRMQVSAGGNIGERL---MAVGARhygDIRATAGDWLERVEIDA--ARIddlPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 147 GLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-225 |
3.67e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.95 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVdekllkkIRRKFGFLFQESALFD---SL 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------LQKNLVAYVPQSEEVDwsfPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAFPLREH---LKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDP 170
Cdd:PRK15056 96 LVEDVVMMGRYGHmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 171 ITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIAD-----KIAVLSSGKIIACDTPENI 225
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAENL 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-225 |
6.79e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 93.61 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 18 RGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD----KGHIFIDGIDItkvdekLLKKIR-RKFGFLFQ--ESAlF 90
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV------APCALRgRKIATIMQnpRSA-F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSLtveENVAFPLREHLKLSEKKLRE-IVRQKLELVGLSEFGNKM---PNELSGGMKKRVGLARAIALEPEILVYDEPTT 166
Cdd:PRK10418 93 NPL---HTMHTHARETCLALGKPADDaTLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 167 GLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
3.92e-22 |
|
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: 88.66 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkiRRKFG 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQesalfdsltveenvafplrehlklsekklreivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVY 161
Cdd:cd03221 67 YFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 162 DEPTTGLDPITTASIYELILNMEKrlgvTSIIVTHDVPNIFAIADKIAVLSSGK 215
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-216 |
1.40e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 93.11 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIditKVDEKLLKKIRRKFGFLFQESALFDSL------ 93
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKLFSAVFTDFHLFDQLlgpegk 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAFPLREHLKLSEKklreivrqklelvgLSEFGNKMPN-ELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPIT 172
Cdd:PRK10522 419 PANPALVEKWLERLKMAHK--------------LELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1053795292 173 TASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKI 216
Cdd:PRK10522 485 RREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-217 |
1.76e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLkPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFDSlTVEENV 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELD---PESWRKHLSWVGQNPQLPHG-TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 100 AfpLREHlKLSEkklrEIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:PRK11174 444 L--LGNP-DASD----EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 169 DpittASIYELILN--MEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKII 217
Cdd:PRK11174 517 D----AHSEQLVMQalNAASRRQTTLMVTHQLEDL-AQWDQIWVMQDGQIV 562
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-232 |
5.28e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLevlRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEklLKKIRRKFGFLFQ--- 85
Cdd:PRK09700 274 RDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 86 ESALFDSLTVEENVAfpLREHLKLS-------------EKKLREIVRQKLELVGLSEfgNKMPNELSGGMKKRVGLARAI 152
Cdd:PRK09700 349 DNGFFPNFSIAQNMA--ISRSLKDGgykgamglfhevdEQRTAENQRELLALKCHSV--NQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKII----ACD--TPENIV 226
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTqiltNRDdmSEEEIM 503
|
....*.
gi 1053795292 227 KMELPE 232
Cdd:PRK09700 504 AWALPQ 509
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-215 |
5.68e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.48 E-value: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKpdkGHIFIDGIDITkvDEKLLKKIRRKFGF 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ---GNNFTGTILAN--NRKPTKQILKRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 83 LFQESALFDSLTVEENVAFP--LREHLKLSEKKLREIVRQKLELVGLSE-----FGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFCslLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 156 PEILVYDEPTTGLDpitTASIYELILNMEKRLGVTSIIVT---HDVPNIFAIADKIAVLSSGK 215
Cdd:PLN03211 225 PSLLILDEPTSGLD---ATAAYRLVLTLGSLAQKGKTIVTsmhQPSSRVYQMFDSVLVLSEGR 284
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-239 |
6.17e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.25 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgiditKVDEKLlkkirrKF 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKL------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLREHLKlsekklREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLRPGTK------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLsSGKIIACDTPEnIVKMElpelQEFITV 239
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPE-VVSLH----PEFISM 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-196 |
7.28e-21 |
|
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: 87.16 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 5 ENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditKVDEKLLKKIRRKFGFLF 84
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 85 QESALFDSLTVEENVAFPLREHLklsekklREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHS-------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|..
gi 1053795292 165 TTGLDPITTASIYELILNMEKRLGVTsIIVTH 196
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMV-VLTTH 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-196 |
7.64e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 18 RGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLlkkiRRKFGFLFQESALFDSLTVEE 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY----HQDLLYLGHQPGIKTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 98 NVAFPLREHLKLSEkklrEIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARaIALEPEIL-VYDEPTTGLDpitTASI 176
Cdd:PRK13538 94 NLRFYQRLHGPGDD----EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAID---KQGV 165
|
170 180
....*....|....*....|..
gi 1053795292 177 YELILNMEKRL--GVTSIIVTH 196
Cdd:PRK13538 166 ARLEALLAQHAeqGGMVILTTH 187
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-226 |
1.13e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 89.09 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF----GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKpDKGHIFIDGIDITKVDE-KLLKK 75
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLlRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 76 IRRKF-----GFLFQE--SALFDSLTVEENV-------AFPLREHLKLSEKKLREIvrQKLELVGLSEFGNKM---PNEL 138
Cdd:PRK15093 82 ERRKLvghnvSMIFQEpqSCLDPSERVGRQLmqnipgwTYKGRWWQRFGWRKRRAI--ELLHRVGIKDHKDAMrsfPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 139 SGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
....*...
gi 1053795292 219 CDTPENIV 226
Cdd:PRK15093 240 TAPSKELV 247
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-217 |
2.31e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDItkvDEKLLKKIRRKFGFLFQESALFDSlTVE 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 97 ENVAFPLREHLKlsekklREIVRQKLELVGLSEFGNKMPN-----------ELSGGMKKRVGLARAIALEPEILVYDEPT 165
Cdd:PRK11176 435 NNIAYARTEQYS------REQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 166 TGLDPITTASIYELILNMEKRLgvTSIIVTHDVPNIfAIADKIAVLSSGKII 217
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNR--TSLVIAHRLSTI-EKADEILVVEDGEIV 557
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-217 |
2.37e-20 |
|
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: 85.78 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGIDITKVDEKLlkkiRRKFGFLFQ 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY----PGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 86 ESALFDSLTVEENVAFPLRehlklsekkLReivrqklelvglsefGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPT 165
Cdd:cd03233 91 EDVHFPTLTVRETLDFALR---------CK---------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 166 TGLDPITTASIYELILNMEKRLGVTSII-VTHDVPNIFAIADKIAVLSSGKII 217
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-229 |
6.33e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 88.64 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFdSLTV 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLF-SGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAfPLREH------LKLSEKKLREIVRQKleLVGL----SEFGNKmpneLSGGMKKRVGLARAIALEPEILVYDEPT 165
Cdd:PLN03130 1330 RFNLD-PFNEHndadlwESLERAHLKDVIRRN--SLGLdaevSEAGEN----FSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 166 TGLDPITTASIYELIlnMEKRLGVTSIIVTHDVPNIFAiADKIAVLSSGKIIACDTPENIVKME 229
Cdd:PLN03130 1403 AAVDVRTDALIQKTI--REEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-223 |
1.83e-19 |
|
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: 87.16 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGidiTKVDEKLLKKIRRKFGFLFQESALFDSLTVEENV 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG---QPVTADNREAYRQLFSAVFSDFHLFDRLLGLDGE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 100 AFPLR-----EHLKLSEKklreivrqklelVGLS--EFGNkmpNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPIT 172
Cdd:COG4615 428 ADPARarellERLELDHK------------VSVEdgRFST---TDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 173 TASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKIAVLSSGKIIACDTPE 223
Cdd:COG4615 493 RRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-229 |
1.91e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.34 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKF--GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRR 78
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFdSLTVEENVAfPLREH------LKLSEKKLREIVRQKleLVGLSEFGNKMPNELSGGMKKRVGLARAI 152
Cdd:PLN03232 1311 VLSIIPQSPVLF-SGTVRFNID-PFSEHndadlwEALERAHIKDVIDRN--PFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELIlnMEKRLGVTSIIVTHDVpNIFAIADKIAVLSSGKIIACDTPENIVKME 229
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTI--REEFKSCTMLVIAHRL-NTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-196 |
3.55e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.08 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 13 KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLK--PDKGHIFIDGIDITkvdekllkkirrkfgflfQESALF 90
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG------------------REASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSLTVEENVAfplrehlklsekklreivrQKLEL---VGLSE--FGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPT 165
Cdd:COG2401 104 DAIGRKGDFK-------------------DAVELlnaVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....
gi 1053795292 166 TGLDPiTTAsiYELILNMEK---RLGVTSIIVTH 196
Cdd:COG2401 165 SHLDR-QTA--KRVARNLQKlarRAGITLVVATH 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-230 |
5.37e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 83.72 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD--------KGHIFIDGIDITKVDEKLLKKIRrkfGFLFQES 87
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLR---AVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 88 ALFDSLTVEENVAFPLREHLKLS---EKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIA---------LE 155
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAgalTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELI--LNMEKRLGVTSIIvtHDvPNIFA-IADKIAVLSSGKIIACDTPENIVKMEL 230
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVrrLARDWNLGVLAIV--HD-PNLAArHADRIAMLADGAIVAHGAPADVLTPAH 247
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-229 |
2.87e-18 |
|
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: 81.49 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKL--EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRK 79
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSltveeNVAFPLREHLKLSEKKLREivrqKLELVGLSEFGNKMPNEL-----SGGMKKRVG------L 148
Cdd:cd03288 97 LSIILQDPILFSG-----SIRFNLDPECKCTDDRLWE----ALEIAQLKNMVKSLPGGLdavvtEGGENFSVGqrqlfcL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 149 ARAIALEPEILVYDEPTTGLDpITTASIYELILnMEKRLGVTSIIVTHDVPNIFAiADKIAVLSSGKIIACDTPENIVKM 228
Cdd:cd03288 168 ARAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
.
gi 1053795292 229 E 229
Cdd:cd03288 245 E 245
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-243 |
4.75e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLkPDKGHIFIDGIDITKVDEKLLKKIRrkfGFLFQES------ALFDSL 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQtppfamPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEEnvafPLREHLKLSEKKLREIVrqklELVGLSEFGNKMPNELSGGMKKRVGLA-------RAIALEPEILVYDEPTT 166
Cdd:PRK03695 91 TLHQ----PDKTRTEAVASALNEVA----EALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 167 GLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIvkMELPELQEFITVQMKK 243
Cdd:PRK03695 163 SLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV--LTPENLAQVFGVNFRR 236
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-218 |
8.77e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 81.32 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSG--KTVLIKHVVGllkPDKGHI---FIdgidiTKVDEKllKKI 76
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRpwrF*-----TWCANR--RAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQ-ESALFDSLTVEENVaFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:NF000106 84 RRTIG*HRPvR*GRRESFSGRENL-YMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-213 |
1.40e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.00 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 54 DKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFDsLTVEENVAFPlrehlklSEKKLREIVRQKLELVGLSEFGNK 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYN---LKDLRNLFSIVSQEPMLFN-MSIYENIKFG-------KEDATREDVKRACKFAAIDEFIES 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 134 MPNE-----------LSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIf 202
Cdd:PTZ00265 1344 LPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI- 1422
|
170
....*....|.
gi 1053795292 203 AIADKIAVLSS 213
Cdd:PTZ00265 1423 KRSDKIVVFNN 1433
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-227 |
1.42e-17 |
|
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: 81.92 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFDSltv 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVLFSG--- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 eenvafPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNE-----------LSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:TIGR00957 1375 ------SLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 165 TTGLDPITTASIYELILNMEKRLGVTSIivTHDVPNIFAIAdKIAVLSSGKIIACDTPENIVK 227
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTI--AHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-217 |
5.43e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 80.15 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 6 NLYKKFGK---LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHV----VGLLKPDKGHIFIDGIDItkvdEKLLKKIRR 78
Cdd:TIGR00956 63 RKLKKFRDtktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITP----EEIKKHYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFDSLTVEENVAF------PLREHLKLSEKKLREIVRQ-KLELVGLS-----EFGNKMPNELSGGMKKRV 146
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFaarcktPQNRPDGVSREEYAKHIADvYMATYGLShtrntKVGNDFVRGVSGGERKRV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 147 GLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDV-PNIFAIADKIAVLSSGKII 217
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQI 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-216 |
1.18e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKVDEKLLKKI------RRKFGFLFqesa 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDGLANGIvyisedRKRDGLVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 89 lfdSLTVEENVAFPLREHL-----KLSEKKLREIVRQKLELvglseFGNKMPN------ELSGGMKKRVGLARAIALEPE 157
Cdd:PRK10762 344 ---GMSVKENMSLTALRYFsraggSLKHADEQQAVSDFIRL-----FNIKTPSmeqaigLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELIlNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-232 |
1.86e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKVDEKllkkIR---------RKfgflfqESA 88
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA----IRagimlcpedRK------AEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 89 LFDSLTVEENVAFPLREH-----LKLSEKKLREIVRQKLELVGLsefgnKMPN------ELSGGMKKRVGLARAIALEPE 157
Cdd:PRK11288 342 IIPVHSVADNINISARRHhlragCLINNRWEAENADRFIRSLNI-----KTPSreqlimNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIAC-----DTPENIVKMELPE 232
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGElareqATERQALSLALPR 495
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-196 |
1.97e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvDEKLLkkirrkfgFLFQESALFDSlTV 95
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------GARVL--------FLPQRPYLPLG-TL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLREHlKLSEKKLREIvrqkLELVGLSEFGNKM------PNELSGGMKKRVGLARAIALEPEILVYDEPTTGLD 169
Cdd:COG4178 443 REALLYPATAE-AFSDAELREA----LEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180
....*....|....*....|....*..
gi 1053795292 170 PITTASIYELILnmEKRLGVTSIIVTH 196
Cdd:COG4178 518 EENEAALYQLLR--EELPGTTVISVGH 542
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-233 |
2.17e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 6 NLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLkPD---KGHIFIDGiditkvDEKLLKKIR---RK 79
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG------EELQASNIRdteRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 -FGFLFQESALFDSLTVEENV---AFPLREHLKLSEKKLREIVRQkLELVGLSEFGNKMPNELSGGMKKRVGLARAIALE 155
Cdd:PRK13549 83 gIAIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKL-LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 156 PEILVYDEPTTGLdpitTASIYELILNMEKRL---GVTSIIVTHDVPNIFAIADKIAVLSSGKIIACD-----TPENIVK 227
Cdd:PRK13549 162 ARLLILDEPTASL----TESETAVLLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDGRHIGTRpaagmTEDDIIT 237
|
250
....*....|
gi 1053795292 228 M----ELPEL 233
Cdd:PRK13549 238 MmvgrELTAL 247
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-222 |
2.38e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvDEKLLKKIRRKFG 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQE--SALFDSLTVEENVAFplreHLKL-----SEKKLReiVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIAL 154
Cdd:NF033858 80 YMPQGlgKNLYPTLSVFENLDF----FGRLfgqdaAERRRR--IDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVthdvpnifAIA--------DKIAVLSSGKIIACDTP 222
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLV--------ATAymeeaerfDWLVAMDAGRVLATGTP 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-212 |
3.32e-16 |
|
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: 75.52 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 13 KLEVLRGvnlTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDI------------TKVDEKLLKKIRRkf 80
Cdd:cd03237 14 TLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadyeGTVRDLLSSITKD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 gflFQESALFDSltveeNVAFPLrehlklsekKLREIVRQKLelvglsefgnkmpNELSGGMKKRVGLARAIALEPEILV 160
Cdd:cd03237 89 ---FYTHPYFKT-----EIAKPL---------QIEQILDREV-------------PELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 161 YDEPTTGLDP----ITTASIYELILNMEKrlgvTSIIVTHDVPNIFAIADKIAVLS 212
Cdd:cd03237 139 LDEPSAYLDVeqrlMASKVIRRFAENNEK----TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-225 |
3.70e-16 |
|
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: 77.17 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD--KGHIFIDGIDItkVDEKLLKKIRR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPL--KASNIRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFDSLTVEENVAF-------PLREHLKLSEKKLREIVRQklelVGLSEFGNKMP-NELSGGMKKRVGLAR 150
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLgneitlpGGRMAYNAMYLRAKNLLRE----LQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 151 AIALEPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENI 225
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-217 |
6.46e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENL---YKKfGKLeVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLkkiRR 78
Cdd:PRK10790 341 IDIDNVsfaYRD-DNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESA-LFDSLTVeeNVAFPlREhlkLSEKKlreiVRQKLELVGLSEFGNKMP-----------NELSGGMKKRV 146
Cdd:PRK10790 416 GVAMVQQDPVvLADTFLA--NVTLG-RD---ISEEQ----VWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 147 GLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRlgVTSIIVTHDVPNIFAiADKIAVLSSGKII 217
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-216 |
8.02e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDekllKKIRRKFGFLF-----QESAL 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 90 FDSLTVEENVAfPLREHLK---LSEKKLREIVRQKLELVGLS-EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPT 165
Cdd:PRK15439 353 YLDAPLAWNVC-ALTHNRRgfwIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 166 TGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-216 |
9.18e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKF-GKLE--VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPdkghifidgIDITKVDekllkkIRR 78
Cdd:PLN03232 615 ISIKNGYFSWdSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH---------AETSSVV------IRG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 79 KFGFLFQESALFDSlTVEENVAFPLREHlklSEKKLREI----VRQKLELVG---LSEFGNKMPNeLSGGMKKRVGLARA 151
Cdd:PLN03232 680 SVAYVPQVSWIFNA-TVRENILFGSDFE---SERYWRAIdvtaLQHDLDLLPgrdLTEIGERGVN-ISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 152 IALEPEILVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVpNIFAIADKIAVLSSGKI 216
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-196 |
1.14e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKllkkirRKFGFLFQESALFDSLTV 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS------RFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLREHlklsEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARaIALEPEIL-VYDEPTTGLDP--IT 172
Cdd:PRK13543 100 LENLHFLCGLH----GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLegIT 174
|
170 180
....*....|....*....|....
gi 1053795292 173 tasIYELILNMEKRLGVTSIIVTH 196
Cdd:PRK13543 175 ---LVNRMISAHLRGGGAALVTTH 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-218 |
2.86e-15 |
|
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: 74.86 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLkPDK--GHIFIDG--IDITKVDEKLLKKI------RRKFGFLFQesal 89
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGkpVDIRNPAQAIRAGIamvpedRKRHGIVPI---- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 90 fdsLTVEENVAFPLREHL----KLSEKKLREIVRQKLELVGLSEFGNKMP-NELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:TIGR02633 354 ---LGVGKNITLSVLKSFcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 165 TTGLDPITTASIYELIlNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLI-NQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-218 |
3.12e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 6 NLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKVDEKLLKKIrrkfGFL 83
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALAAGV----AII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 FQESALFDSLTVEENV---AFPLREHLkLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK11288 85 YQELHLVPEMTVAENLylgQLPHKGGI-VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 161 YDEPTTGLDPITTASIYELIlnmeKRL---GVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVI----RELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-216 |
3.77e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.60 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkirrKFGFLFQEsALFDSLTVE 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------------SVAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 97 ENVAFplreHLKLSEKKLREIVRQKLELVGL--------SEFGNKMPNeLSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:TIGR00957 717 ENILF----GKALNEKYYQQVLEACALLPDLeilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1053795292 169 DPITTASIYELILNMEKRL-GVTSIIVTHDVpNIFAIADKIAVLSSGKI 216
Cdd:TIGR00957 792 DAHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKI 839
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-212 |
6.44e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFG--KLEVLRGvnlTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDgIDIT------KVD--- 69
Cdd:PRK13409 340 LVEYPDLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpqyiKPDydg 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 70 --EKLLKKIRRKfgflfqesalFDSLTVEENVAFPLREHlKLSEKKLreivrqklelvglsefgnkmpNELSGGMKKRVG 147
Cdd:PRK13409 416 tvEDLLRSITDD----------LGSSYYKSEIIKPLQLE-RLLDKNV---------------------KDLSGGELQRVA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 148 LARAIALEPEILVYDEPTTGLD---PITTASIYELIlnMEKRlGVTSIIVTHDVPNIFAIADKIAVLS 212
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRI--AEER-EATALVVDHDIYMIDYISDRLMVFE 528
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-217 |
1.02e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 9 KKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKhVVGLLKPD---KGHIFIDGiditkvDEKLLKKIR--RKFGFL 83
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyEGEILFDG------EVCRFKDIRdsEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 F--QESALFDSLTVEENVaFPLREHLKLSEKKLREIVRQKLEL---VGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:NF040905 82 IihQELALIPYLSIAENI-FLGNERAKRGVIDWNETNRRARELlakVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-210 |
1.02e-14 |
|
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: 73.28 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG--KLEVLRGvnlTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGhifidgiditKVDEKLlkKIRRK 79
Cdd:COG1245 342 VEYPDLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDEDL--KISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLfqeSALFDsLTVEENvafpLREHLK--LSEKKLREIVRQKLelvGLSEFGNKMPNELSGGMKKRVGLARAIALEPE 157
Cdd:COG1245 407 PQYI---SPDYD-GTVEEF----LRSANTddFGSSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 158 ILVYDEPTTGLD---PITTASIYELIlnMEKRlGVTSIIVTHDVPNIFAIADKIAV 210
Cdd:COG1245 476 LYLLDEPSAHLDveqRLAVAKAIRRF--AENR-GKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-199 |
5.59e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDItkvdEKLLKKIRRKF 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVAFPLreHLKLSEKKLREIVRqkleLVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDI--HFSPGAVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVP 199
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLP 189
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-217 |
1.22e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgiditKVDEKllkkirRKFGFL 83
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 FQESAL-FDSltvEENVAFPLREHLKlsEKKLREIVRQKLelvGLSEFG----NKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PRK15064 388 AQDHAYdFEN---DLTLFDWMSQWRQ--EGDDEQAVRGTL---GRLLFSqddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLDpitTASIYELILNMEKRLGvTSIIVTHDVPNIFAIADKIAVLSSGKII 217
Cdd:PRK15064 460 LVMDEPTNHMD---MESIESLNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-218 |
1.42e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKirRKF 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFDSLTVEENVaFPLREHL----KLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEP 156
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENI-FLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELIlNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIA 218
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVI-RELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-172 |
1.50e-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: 69.94 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKF--GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDkGHIFIDGIDITKVDeklLKKIRRKFG 81
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT---LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFdSLTVEENvafpLREHLKLSEKKLREIVrqklELVGLSEFGNKMPNEL-----------SGGMKKRVGLAR 150
Cdd:TIGR01271 1296 VIPQKVFIF-SGTFRKN----LDPYEQWSDEEIWKVA----EEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLAR 1366
|
170 180
....*....|....*....|..
gi 1053795292 151 AIALEPEILVYDEPTTGLDPIT 172
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVT 1388
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-213 |
2.24e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 14 LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDgiDITKVDEKLLKKIRRKFGFLFQESALFdSL 93
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPLLF-SN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAFPLREHLKL---------------SEKKLREIVRQKL-----------------------------ELVGLS- 128
Cdd:PTZ00265 475 SIKNNIKYSLYSLKDLealsnyynedgndsqENKNKRNSCRAKCagdlndmsnttdsneliemrknyqtikdsEVVDVSk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 129 -----EFGNKMPNE-----------LSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELILNMEKRLGVTSI 192
Cdd:PTZ00265 555 kvlihDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250 260
....*....|....*....|.
gi 1053795292 193 IVTHDVPNIfAIADKIAVLSS 213
Cdd:PTZ00265 635 IIAHRLSTI-RYANTIFVLSN 654
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-197 |
3.14e-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: 68.81 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFI-DGIDITKVDEkllkkirrkf 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 gflfQESALFDSLTVEENVAFPLrEHLKLSEkklREIvrQKLELVGLSEFG----NKMPNELSGGMKKRVGLARAIALEP 156
Cdd:TIGR03719 393 ----SRDALDPNKTVWEEISGGL-DIIKLGK---REI--PSRAYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1053795292 157 EILVYDEPTTGLDPITTASIYELILNmekrLGVTSIIVTHD 197
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLN----FAGCAVVISHD 499
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-216 |
3.15e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 15 EVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDgiditkvdekllkkirRKFGFLFQESALFDSlT 94
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 95 VEENVAFPLREhlklSEKKLREIVR-QKLE--LVGLS-----EFGNKMPNeLSGGMKKRVGLARAIALEPEILVYDEPTT 166
Cdd:PTZ00243 737 VRGNILFFDEE----DAARLADAVRvSQLEadLAQLGggletEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 167 GLDP-ITTASIYELILNmekRL-GVTSIIVTHDVpNIFAIADKIAVLSSGKI 216
Cdd:PTZ00243 812 ALDAhVGERVVEECFLG---ALaGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-214 |
3.46e-13 |
|
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: 66.11 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 10 KFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKhVVGLLKPD---KGHIFIDGIditkvdeKLLKKIRRKFGFLFQE 86
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLD-VLAGRKTAgviTGEILINGR-------PLDKNFQRSTGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 87 SALFDSLTVeenvafplREHLKLSeKKLREivrqklelvglsefgnkmpneLSGGMKKRVGLARAIALEPEILVYDEPTT 166
Cdd:cd03232 88 DVHSPNLTV--------REALRFS-ALLRG---------------------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 167 GLDPITTASIYELIlnmeKRLGVT--SIIVTHDVPN--IFAIADKIAVLSSG 214
Cdd:cd03232 138 GLDSQAAYNIVRFL----KKLADSgqAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-214 |
3.65e-13 |
|
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: 67.57 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkirrKFGFLFQESALFDSlTV 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFplreHLKLSEKKLREIVRQ-KLE--LVGLSEFGNKMPNE----LSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:cd03291 115 KENIIF----GVSYDEYRYKSVVKAcQLEedITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053795292 169 DPITTASIYE-----LILNMekrlgvTSIIVTHDVPNIfAIADKIAVLSSG 214
Cdd:cd03291 191 DVFTEKEIFEscvckLMANK------TRILVTSKMEHL-KKADKILILHEG 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-216 |
4.26e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIdgiditkvdekllkkIRRKFGFLFQESALFDSlTVE 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IRGTVAYVPQVSWIFNA-TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 97 ENVAFPLREHLKLSEKKLR-EIVRQKLELV---GLSEFGNKMPNeLSGGMKKRVGLARAIALEPEILVYDEPTTGLDPIT 172
Cdd:PLN03130 697 DNILFGSPFDPERYERAIDvTALQHDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1053795292 173 TASIYELILNMEKRlGVTSIIVT---HDVPNIfaiaDKIAVLSSGKI 216
Cdd:PLN03130 776 GRQVFDKCIKDELR-GKTRVLVTnqlHFLSQV----DRIILVHEGMI 817
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-214 |
6.19e-13 |
|
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: 68.12 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 24 INKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDI-TKVDEkllkkIRRKFGFLFQESALFDSLTVeenvafp 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD-----VHQNMGYCPQFDAIDDLLTG------- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 103 lREHLKLSeKKLREIVRQKLELV--------GLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTA 174
Cdd:TIGR01257 2030 -REHLYLY-ARLRGVPAEEIEKVanwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1053795292 175 SIYELILNMeKRLGVTSIIVTHDVPNIFAIADKIAVLSSG 214
Cdd:TIGR01257 2108 MLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-216 |
8.62e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 20 VNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDK-GHIFIDG--IDITKVDEKLLKKI------RRKFGFLFQesalf 90
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkpVKIRNPQQAIAQGIamvpedRKRDGIVPV----- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 dsLTVEENVAFP-LREHLKLS----EKKLREIVR--QKLELVGLSEF---GNkmpneLSGGMKKRVGLARAIALEPEILV 160
Cdd:PRK13549 356 --MGVGKNITLAaLDRFTGGSriddAAELKTILEsiQRLKVKTASPElaiAR-----LSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 161 YDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-214 |
1.15e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkirrKFGFLFQESALFDSlTV 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFplreHLKLSEKKLREIVRQ-KLElVGLSEFGNKMPN-------ELSGGMKKRVGLARAIALEPEILVYDEPTTG 167
Cdd:TIGR01271 504 KDNIIF----GLSYDEYRYTSVIKAcQLE-EDIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1053795292 168 LDPITTASIYELILnMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSG 214
Cdd:TIGR01271 579 LDVVTEKEIFESCL-CKLMSNKTRILVTSKLEHL-KKADKILLLHEG 623
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-172 |
1.24e-12 |
|
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: 66.03 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKF--GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDkGHIFIDGIDITKVDeklLKKIRRK 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP---LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSltveenvafPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNEL-----------SGGMKKRVGL 148
Cdd:cd03289 79 FGVIPQKVFIFSG---------TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCL 149
|
170 180
....*....|....*....|....
gi 1053795292 149 ARAIALEPEILVYDEPTTGLDPIT 172
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPIT 173
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-245 |
1.86e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.45 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 3 KIENLYKKFGKLE---VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGiditkvdekllkkirrK 79
Cdd:PRK13545 23 KLKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------------S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSLTVEENVAFPlREHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEIL 159
Cdd:PRK13545 87 AALIAISSGLNGQLTGIENIELK-GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 160 VYDEPTTGLDPITTASIYELiLNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIV-----------KM 228
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDK-MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVdhydeflkkynQM 244
|
250
....*....|....*..
gi 1053795292 229 ELPELQEFITVQMKKFQ 245
Cdd:PRK13545 245 SVEERKDFREEQISQFQ 261
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-226 |
3.76e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFDSlTV 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAfplrehlKLSEKKLREiVRQKLELVGL-----SEFGNKMPNELSGGMKKRVG------LARAIALEPE--ILVyD 162
Cdd:PTZ00243 1401 RQNVD-------PFLEASSAE-VWAALELVGLrervaSESEGIDSRVLEGGSNYSVGqrqlmcMARALLKKGSgfILM-D 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053795292 163 EPTTGLDPITTASIYELIlnMEKRLGVTSIIVTHDVPNIfAIADKIAVLSSGKIIACDTPENIV 226
Cdd:PTZ00243 1472 EATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-216 |
3.93e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITkvDEKLLKKIRRKFGFLFQE---SALFDSL 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN--NHNANEAINHGFALVTEErrsTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 94 TVEENVAFPLREHLK-----LSEKKLREIVRQKLELVGLSEFGNKMP-NELSGGMKKRVGLARAIALEPEILVYDEPTTG 167
Cdd:PRK10982 342 DIGFNSLISNIRNYKnkvglLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1053795292 168 LDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-217 |
5.41e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGL--LKPDKGHIFIDGIDITKVD--EKLLKKI 76
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpeDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 77 RRKFGFLFQESALFDS--LTVEENVAFPLREHLKLSEKKLREIVRQKLELVglsefgnKMPNEL---------SGGMKKR 145
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQffLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL-------KMPEDLltrsvnvgfSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053795292 146 VGLARAIALEPEILVYDEPTTGLDpITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIA-DKIAVLSSGKII 217
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIV 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-228 |
8.29e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG--IDITKVDEKLLKKIrrkfG 81
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENGI----S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENV---AFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMwlgRYPTK-GMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1053795292 159 LVYDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACD-----TPENIVKM 228
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQplaglTMDKIIAM 229
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-180 |
8.40e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.20 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLLKKIRRKFGFLFQesalfdsLTV 95
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-------MTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFplrehlkLSE-KKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTA 174
Cdd:PRK13541 88 FENLKF-------WSEiYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
....*.
gi 1053795292 175 SIYELI 180
Cdd:PRK13541 161 LLNNLI 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-217 |
3.18e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIdgiditkvdEKLLKKIRrkf 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---------EQDLIVAR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 gfLFQ------ESALFDslTVEENVAfPLREHLK------------LSEKKLREIVR------------------QKLEL 124
Cdd:PRK11147 71 --LQQdpprnvEGTVYD--FVAEGIE-EQAEYLKryhdishlvetdPSEKNLNELAKlqeqldhhnlwqlenrinEVLAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 125 VGLSefGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpITTASIYELILnmeKRLGVTSIIVTHDVPNIFAI 204
Cdd:PRK11147 146 LGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IETIEWLEGFL---KTFQGSIIFISHDRSFIRNM 219
|
250
....*....|...
gi 1053795292 205 ADKIAVLSSGKII 217
Cdd:PRK11147 220 ATRIVDLDRGKLV 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-217 |
6.20e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.04 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDeklLKKIRRKFGFLFQESALFdSLTV 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPFLF-SDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAF--PLREHLKLSE-KKLREIVRQKLELVG--LSEFGNK--MpneLSGGMKKRVGLARAIALEPEILVYDEPTTGL 168
Cdd:PRK10789 406 ANNIALgrPDATQQEIEHvARLASVHDDILRLPQgyDTEVGERgvM---LSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1053795292 169 DPITTasiYELILNMEK-RLGVTSIIVTHDVpNIFAIADKIAVLSSGKII 217
Cdd:PRK10789 483 DGRTE---HQILHNLRQwGEGRTVIISAHRL-SALTEASEILVMQHGHIA 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-216 |
9.41e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgiditkvdeKLLKKIrrKF 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------------GLAKGI--KL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 GFLFQESALFdsLTVEENvafPLREHLKLSEKKLREIVRQKLELVGLSefGNKMPNE---LSGGMKKRVGLARAIALEPE 157
Cdd:PRK10636 378 GYFAQHQLEF--LRADES---PLQHLARLAPQELEQKLRDYLGGFGFQ--GDKVTEEtrrFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 158 ILVYDEPTTGLDPITTASIYELILNMEKRLgvtsIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-197 |
1.28e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFI-DGIditkvdekllkkirrKFGFLFQESALF 90
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI---------------KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSLTVEENVAFPLREHLKLsEKKLREI--------------------VRQKLELVGLSEFGNKM---------P------ 135
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDA-LDRFNEIsakyaepdadfdklaaeqaeLQEIIDAADAWDLDSQLeiamdalrcPpwdadv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 136 NELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPittasiyELILNMEKRL----GvTSIIVTHD 197
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLqeypG-TVVAVTHD 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-183 |
2.16e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 10 KFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGllKPDKGHIfIDGIDITKvDEKLLKKIRRKFGFLFQESAL 89
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI-TGGDRLVN-GRPLDSSFQRSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 90 FDSLTVEENVAFP--LREHLKLSEKKLREIVRQKLELVGLSEFGNKM---PNE-LSGGMKKRVGLARAIALEPEILVY-D 162
Cdd:TIGR00956 848 LPTSTVRESLRFSayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLFlD 927
|
170 180
....*....|....*....|.
gi 1053795292 163 EPTTGLDPITTASIYELILNM 183
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKL 948
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-228 |
3.48e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDK--GHIFIDG--IDITKVDEKLLKKI------RRKFGFLFQ 85
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGkeVDVSTVSDAIDAGLayvtedRKGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 86 EsalfdslTVEENVAFPlreHL-KLSEkklREIVRQKLELVGLSEFGNKM----PN------ELSGGMKKRVGLARAIAL 154
Cdd:NF040905 355 D-------DIKRNITLA---NLgKVSR---RGVIDENEEIKVAEEYRKKMniktPSvfqkvgNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 155 EPEILVYDEPTTGLDPITTASIYELIlNMEKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIAC-----DTPENIVKM 228
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTII-NELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGElpreeASQERIMRL 499
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-196 |
8.71e-10 |
|
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: 56.96 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGK-LEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG-IDITKVDEKLLKKIRRK 79
Cdd:cd03290 1 VQVTNGYFSWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNkNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 FGFLFQESALFDSlTVEENVAF--PLRehlKLSEKKLREIVRQKLELVGL-----SEFGNKMPNeLSGGMKKRVGLARAI 152
Cdd:cd03290 81 VAYAAQKPWLLNA-TVEENITFgsPFN---KQRYKAVTDACSLQPDIDLLpfgdqTEIGERGIN-LSGGQRQRICVARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1053795292 153 ALEPEILVYDEPTTGL-----DPITTASIYELiLNMEKRlgvTSIIVTH 196
Cdd:cd03290 156 YQNTNIVFLDDPFSALdihlsDHLMQEGILKF-LQDDKR---TLVLVTH 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
10-198 |
1.82e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.41 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 10 KFGKLEV--LRGVNLTINKGEITAIIGKSGSGKTVLIKHVvgllkpdkghifidgidITKVDEKLLKKIRRKFGflfqes 87
Cdd:cd03238 2 TVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFS------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 88 alfdsltveenvafplrEHLKLSEKKLREIVRQKLELVGLsefGNKMPNeLSGGMKKRVGLARAIALEPE--ILVYDEPT 165
Cdd:cd03238 59 -----------------RNKLIFIDQLQFLIDVGLGYLTL---GQKLST-LSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 1053795292 166 TGLDPITTASIYELIlnmeKRL---GVTSIIVTHDV 198
Cdd:cd03238 118 TGLHQQDINQLLEVI----KGLidlGNTVILIEHNL 149
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-197 |
3.17e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 4 IENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgiditKVDEKLlkkirrkfgfl 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKL----------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 84 fqESALFDSL--------TVEENVAfplrehlklSEKKLREIVRQKLELVG-LSEF-----GNKMP-NELSGGMKKRVGL 148
Cdd:PRK11147 383 --EVAYFDQHraeldpekTVMDNLA---------EGKQEVMVNGRPRHVLGyLQDFlfhpkRAMTPvKALSGGERNRLLL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1053795292 149 ARaIALEP-EILVYDEPTTGLDPITTASIYELILNMEKrlgvTSIIVTHD 197
Cdd:PRK11147 452 AR-LFLKPsNLLILDEPTNDLDVETLELLEELLDSYQG----TVLLVSHD 496
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-196 |
7.21e-09 |
|
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: 53.70 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgidITKVDEKLLkkirrkfgFLFQESaLFDSLTV 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------GMPEGEDLL--------FLPQRP-YLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLREhlklsekklreivrqklelvglsefgnkmpnELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTAS 175
Cdd:cd03223 81 REQLIYPWDD-------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 1053795292 176 IYELIlnmeKRLGVTSIIVTH 196
Cdd:cd03223 130 LYQLL----KELGITVISVGH 146
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-217 |
1.32e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 1 MIKIeNLYKKfGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPD---KGHIFIDGidiTKVDEKLLKKIR 77
Cdd:PLN03140 167 MLGI-NLAKK-TKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG---YRLNEFVPRKTS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 78 rkfGFLFQESALFDSLTVEENVAFPLR------EHLKLSEKKLRE---------------------------IVRQKLEL 124
Cdd:PLN03140 242 ---AYISQNDVHVGVMTVKETLDFSARcqgvgtRYDLLSELARREkdagifpeaevdlfmkatamegvksslITDYTLKI 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 125 VGL-----SEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTasiYELILNMEK--RLGVTSIIVT-- 195
Cdd:PLN03140 319 LGLdickdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTT---YQIVKCLQQivHLTEATVLMSll 395
|
250 260
....*....|....*....|..
gi 1053795292 196 HDVPNIFAIADKIAVLSSGKII 217
Cdd:PLN03140 396 QPAPETFDLFDDIILLSEGQIV 417
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-169 |
1.32e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 13 KLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGllkpDKGHIFIDG-IDITKVDEKlLKKIRRKFGFLFQESALFD 91
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG----RKTGGYIEGdIRISGFPKK-QETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 92 SLTVEENVAFP--LREHLKLSEKKLREIVRQKLELVGLSEFGNK---MP--NELSGGMKKRVGLARAIALEPEILVYDEP 164
Cdd:PLN03140 967 QVTVRESLIYSafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 1053795292 165 TTGLD 169
Cdd:PLN03140 1047 TSGLD 1051
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-169 |
1.92e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVV-----GLlkPDKGHIF-----IDGIDITKVDEK 71
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqeVVGDDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 72 LLKKIRRKFgfLFQESA--LFDSLTVEENVAF--------------PLREHLKLSEKKLREI------VRQKLELVGLS- 128
Cdd:PLN03073 256 LNTDIERTQ--LLEEEAqlVAQQRELEFETETgkgkgankdgvdkdAVSQRLEEIYKRLELIdaytaeARAASILAGLSf 333
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1053795292 129 --EFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLD 169
Cdd:PLN03073 334 tpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-243 |
2.65e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDG-IDITKVDekllkkirrkfgflfqeSALFDSLTV 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAIS-----------------AGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 96 EENVAFPLReHLKLSEKKLREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITT-- 173
Cdd:PRK13546 103 IENIEFKML-CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAqk 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 174 --ASIYELilnmeKRLGVTSIIVTHDVPNIFAIADKIAVLSSGKIIACDTPENIvkmeLPELQEFITVQMKK 243
Cdd:PRK13546 182 clDKIYEF-----KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV----LPKYEAFLNDFKKK 244
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-197 |
3.23e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFI-DGIDITKVDEkllkkirrkf 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVDQ---------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 81 gflfQESALFDSLTVEENVAFPLrEHLKLSEKKL--REIVrqklelvglSEFG------NKMPNELSGGMKKRVGLARAI 152
Cdd:PRK11819 395 ----SRDALDPNKTVWEEISGGL-DIIKVGNREIpsRAYV---------GRFNfkggdqQKKVGVLSGGERNRLHLAKTL 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1053795292 153 ALEPEILVYDEPTTGLDPITTASIYELILNmekrLGVTSIIVTHD 197
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDVETLRALEEALLE----FPGCAVVISHD 501
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-209 |
5.05e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLR-GVNL-------TINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGhIFIDGIDITKVdekll 73
Cdd:COG1245 66 ISIVNLPEELEEDPVHRyGENGfrlyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLG-DYDEEPSWDEV----- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 74 kkIRRkfgflFQESALFDSLTveenvafplrehlKLSEKKLREI----------------VRQKL-------------EL 124
Cdd:COG1245 140 --LKR-----FRGTELQDYFK-------------KLANGEIKVAhkpqyvdlipkvfkgtVRELLekvdergkldelaEK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 125 VGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpittasIYELIlNMEK------RLGVTSIIVTHDV 198
Cdd:COG1245 200 LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD------IYQRL-NVARlirelaEEGKYVLVVEHDL 272
|
250
....*....|.
gi 1053795292 199 pnifAIADKIA 209
Cdd:COG1245 273 ----AILDYLA 279
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-208 |
1.28e-07 |
|
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: 50.72 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVL--------------------IKHVVGLL-KPDKGHifIDGIDIT-KVDEKLLK 74
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayARQFLGQMdKPDVDS--IEGLSPAiAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 75 K-----------IRRKFGFLFQESALFDSLTVEENVAFplrEHLKLSekklREIvrqklelvglsefgnkmpNELSGGMK 143
Cdd:cd03270 89 RnprstvgtvteIYDYLRLLFARVGIRERLGFLVDVGL---GYLTLS----RSA------------------PTLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053795292 144 KRVGLARAI--ALEPEILVYDEPTTGLDPITTASIYELILNMeKRLGVTSIIVTHDvPNIFAIADKI 208
Cdd:cd03270 144 QRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-197 |
4.13e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 12 GKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFI-DGIDItkvdekllkkirrkfGFLFQESALF 90
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV---------------GYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 91 DSLTVEENV---------------------AFPLREHLKLSEK--KLREIvrqkLELVGLSEFGNKM----------PNE 137
Cdd:PRK11819 83 PEKTVRENVeegvaevkaaldrfneiyaayAEPDADFDALAAEqgELQEI----IDAADAWDLDSQLeiamdalrcpPWD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 138 -----LSGGMKKRVGLARAIALEPEILVYDEPTTGLDPittasiyELILNMEKRL----GvTSIIVTHD 197
Cdd:PRK11819 159 akvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLEQFLhdypG-TVVAVTHD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-209 |
1.12e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLR-GVN-------LTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGhIFIDGIDITKVdekll 73
Cdd:PRK13409 66 ISIVNLPEELEEEPVHRyGVNgfklyglPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG-DYEEEPSWDEV----- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 74 kkIRRkfgflFQESALFDSLTveenvafplrehlKLSEKKLREI----------------VRQKL-------------EL 124
Cdd:PRK13409 140 --LKR-----FRGTELQNYFK-------------KLYNGEIKVVhkpqyvdlipkvfkgkVRELLkkvdergkldevvER 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 125 VGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpittasIYELIlNMEKRL-----GVTSIIVTHDVp 199
Cdd:PRK13409 200 LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQRL-NVARLIrelaeGKYVLVVEHDL- 271
|
250
....*....|
gi 1053795292 200 nifAIADKIA 209
Cdd:PRK13409 272 ---AVLDYLA 278
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-211 |
1.87e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 21 NLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVD-EKLLKKIRRKFgflfQESALfDSLTV-EEN 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfEQLQKLVSDEW----QRNNT-DMLSPgEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 99 VAFPLREHLKLSEKKlREIVRQKLELVGLSEFGNKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYE 178
Cdd:PRK10938 98 TGRTTAEIIQDEVKD-PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190
....*....|....*....|....*....|...
gi 1053795292 179 LILNMEKRlGVTSIIVTHDVPNIFAIADKIAVL 211
Cdd:PRK10938 177 LLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-171 |
6.93e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGllkpDKGHIFIDgiDITKVDEK-----LLKKIRRKFGF----LFQE 86
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGYSN--DLTLFGRRrgsgeTIWDIKKHIGYvsssLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 87 ------------SALFDSLTVEENVAfplrehlklseKKLREIVRQKLELVGLSEFGNKMP-NELSGGMKKRVGLARAIA 153
Cdd:PRK10938 349 yrvstsvrnvilSGFFDSIGIYQAVS-----------DRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALV 417
|
170
....*....|....*...
gi 1053795292 154 LEPEILVYDEPTTGLDPI 171
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPL 435
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
136-197 |
7.84e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 7.84e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 136 NELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpITTASIYELILNMEKrlgVTSIIVTHD 197
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-INTIRWLEDVLNERN---STMIIISHD 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-216 |
1.07e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 16 VLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIF--------------IDGIDITKvdEKLLKKIRrkfg 81
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSS--NPLLYMMR---- 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 flfqesalfdsltveenvAFPlrehlKLSEKKLReivrQKLELVGLSefGN---KMPNELSGGMKKRVGLARAIALEPEI 158
Cdd:PLN03073 598 ------------------CFP-----GVPEQKLR----AHLGSFGVT--GNlalQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053795292 159 LVYDEPTTGLD-PITTASIYELILNMEkrlGVtsIIVTHDVPNIFAIADKIAVLSSGKI 216
Cdd:PLN03073 649 LLLDEPSNHLDlDAVEALIQGLVLFQG---GV--LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-210 |
3.36e-05 |
|
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: 42.75 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 26 KGEITAIIGKSGSGKTVLIKHVVGLLKPDKGH-IFIDGIDITKVDEKLLKKIRRKFGFLfqesalfdsltveenvafplr 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 105 ehlklsekklreivrqklelvglsefgnkmpnELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASI-----YEL 179
Cdd:smart00382 60 --------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRL 107
|
170 180 190
....*....|....*....|....*....|.
gi 1053795292 180 ILNMEKRLGVTSIIVTHDVPNIFAIADKIAV 210
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
2-211 |
5.10e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFG--KLEVLRGVnltINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIDGIDITKVDEKLlkkirrk 79
Cdd:cd03222 1 QLYPDCVKRYGvfFLLVELGV---VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 80 fgflfqesalfdsltveenvafplrehlklsekklreivrqklelvglsefgnkmpnELSGGMKKRVGLARAIALEPEIL 159
Cdd:cd03222 71 ---------------------------------------------------------DLSGGELQRVAIAAALLRNATFY 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1053795292 160 VYDEPTTGLDPITTASIYELILNMEKRLGVTSIIVTHDVPNIFAIADKIAVL 211
Cdd:cd03222 94 LFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-211 |
8.06e-05 |
|
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: 42.74 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 27 GEITAIIGKSGSGKTVLIKHVVGLLKPDKGHI-----------FIDGIDITKVDEKLLK---KIRRKFGFLFQESALFDS 92
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEgdvKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 93 lTVEENVAfplrehlKLSEKKLREIVRQKLELVGLSEfgnKMPNELSGGMKKRVGLARAIALEPEILVYDEPTTGLD--- 169
Cdd:cd03236 106 -KVGELLK-------KKDERGKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikq 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1053795292 170 PITTASIYELILNMEKRLgvtsIIVTHDVPNIFAIADKIAVL 211
Cdd:cd03236 175 RLNAARLIRELAEDDNYV----LVVEHDLAVLDYLSDYIHCL 212
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
105-197 |
1.49e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.34 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 105 EHLKLSEKKLREIVRQKLELVgLSEFGNKMP-NELSGGMKKRVGLARAIAL---EPEILVYDEPTTGLDPITTASIYELI 180
Cdd:COG1106 170 EDIEVEEEEIEDLVERKLIFK-HKGGNVPLPlSEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLF 248
|
90
....*....|....*..
gi 1053795292 181 LNMEKRLGVTSIIVTHD 197
Cdd:COG1106 249 LDLANKNNAQLIFTTHS 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-209 |
1.84e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053795292 138 LSGGMKKRVGLARAIALE---PEILV-YDEPTTGLDPITTASIYELILNMEKRlGVTSIIVTHDvPNIFAIADKIA 209
Cdd:cd03227 78 LSGGEKELSALALILALAslkPRPLYiLDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHL-PELAELADKLI 151
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-222 |
2.43e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 17 LRGVNLTINKGEITAIIGKSGSGKTVLI---------------KHVVGLLKPDKGHIFIDgiDITKVDE----------- 70
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkKEQPGNHDRIEGLEHID--KVIVIDQspigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 71 ----KLLKKIRRKF-----GFLFQESAL---------FDSL--TVEENVAFpLREHLKLSEKklreivRQKLELVGLS-- 128
Cdd:cd03271 89 atytGVFDEIRELFcevckGKRYNRETLevrykgksiADVLdmTVEEALEF-FENIPKIARK------LQTLCDVGLGyi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 129 EFGNKMPnELSGGMKKRVGLARAIALE---PEILVYDEPTTGLDpitTASIYELI--LNMEKRLGVTSIIVTHDVpNIFA 203
Cdd:cd03271 162 KLGQPAT-TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLH---FHDVKKLLevLQRLVDKGNTVVVIEHNL-DVIK 236
|
250 260
....*....|....*....|....*
gi 1053795292 204 IADKIAVLS------SGKIIACDTP 222
Cdd:cd03271 237 CADWIIDLGpeggdgGGQVVASGTP 261
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-238 |
3.98e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 138 LSGGMKKRVGLAR---AIALEPEILVYDEPTTGLDpitTASIYELI--LNMEKRLGVTSIIVTHDVpNIFAIADKIAVLS 212
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLH---THDIKALIyvLQSLTHQGHTVVIIEHNM-HVVKVADYVLELG 885
|
90 100 110
....*....|....*....|....*....|....*
gi 1053795292 213 ------SGKIIACDTPENIVKMELP---ELQEFIT 238
Cdd:PRK00635 886 peggnlGGYLLASCSPEELIHLHTPtakALRPYLS 920
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-208 |
5.14e-04 |
|
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: 39.90 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 29 ITAIIGKSGSGKTVLIKHVV----GLLKPDKGHIFIDGIDITK------------VDEKLLKKIRRKFGFLfqesalfds 92
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIREgevraqvklafeNANGKKYTITRSLAIL--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 93 ltveENVAFplrehlklsekklreiVRQKLELVGLSEfgnkMPNELSGGMKK------RVGLARAIALEPEILVYDEPTT 166
Cdd:cd03240 95 ----ENVIF----------------CHQGESNWPLLD----MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1053795292 167 GLDPIT-TASIYELILNMEKRLGVTSIIVTHDvPNIFAIADKI 208
Cdd:cd03240 151 NLDEENiEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHI 192
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2-197 |
5.50e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 2 IKIENLYKKFGKLEVLRGVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIfidgiditKVDEKLLKKIRRKFG 81
Cdd:pfam13304 106 EREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLL--------LEDWAVLDLAADLAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 82 FLFQESALFDSLTVEENVAFPLREHLKLSEKKLREIVRQKLELVGLSEFGNKMP---NELSGGMKKRVGLARAIAL---E 155
Cdd:pfam13304 178 FPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpaFELSDGTKRLLALLAALLSalpK 257
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1053795292 156 PEILVYDEPTTGLDPITTASIYELiLNMEKRLGVTSIIVTHD 197
Cdd:pfam13304 258 GGLLLIDEPESGLHPKLLRRLLEL-LKELSRNGAQLILTTHS 298
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-223 |
5.50e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 118 VRQKLEL---VGLS--EFGNKMPNeLSGGMKKRVGLARAI---ALEPEILVYDEPTTGLDpitTASIYELiLNMEKRL-- 187
Cdd:TIGR00630 806 ISRKLQTlcdVGLGyiRLGQPATT-LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLH---FDDIKKL-LEVLQRLvd 880
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1053795292 188 -GVTSIIVTHDVpNIFAIADKIAVL------SSGKIIACDTPE 223
Cdd:TIGR00630 881 kGNTVVVIEHNL-DVIKTADYIIDLgpeggdGGGTVVASGTPE 922
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-196 |
1.27e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 39.73 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 32 IIGKSGSGKTVLIKhVVGLLKPDKGhifidgiditkvdeKLLKKIRRKFGFLFQESALFDSLTVEENVAFPLR-EHLK-- 108
Cdd:TIGR00954 483 ICGPNGCGKSSLFR-ILGELWPVYG--------------GRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSsEDMKrr 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 109 -LSEKKLREIVrQKLEL-------VGLSEFGNKMpNELSGGMKKRVGLARAIALEPEILVYDEPTTGLDPITTASIYELI 180
Cdd:TIGR00954 548 gLSDKDLEQIL-DNVQLthilereGGWSAVQDWM-DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
170
....*....|....*.
gi 1053795292 181 lnmeKRLGVTSIIVTH 196
Cdd:TIGR00954 626 ----REFGITLFSVSH 637
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
101-208 |
1.70e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 101 FPLREHLKLSEKKLREIV---RQKLELV---GLSEFG-NKMPNELSGGMKKRVGLARAIALEPEILVY--DEPTTGLDPI 171
Cdd:PRK00635 433 FIFLSQLPSKSLSIEEVLqglKSRLSILidlGLPYLTpERALATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQ 512
|
90 100 110
....*....|....*....|....*....|....*..
gi 1053795292 172 TTASIYELILNMEKRlGVTSIIVTHDVPNIfAIADKI 208
Cdd:PRK00635 513 DTHKLINVIKKLRDQ-GNTVLLVEHDEQMI-SLADRI 547
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-208 |
2.11e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 11 FGKLEVLRGVNL-------TINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHI------------------------- 58
Cdd:PRK10636 4 FSSLQIRRGVRVlldnataTINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqetpalpqpaley 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053795292 59 FIDG-IDITKVDEKLLKKIRRKFG----FLFQESALFDSLTVEENVAfPLREHLKLSEKKLREIVRqklelvglsefgnk 133
Cdd:PRK10636 84 VIDGdREYRQLEAQLHDANERNDGhaiaTIHGKLDAIDAWTIRSRAA-SLLHGLGFSNEQLERPVS-------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053795292 134 mpnELSGGMKKRVGLARAIALEPEILVYDEPTTGLDpiTTASIYelilnMEKRLGV---TSIIVTHDVPNIFAIADKI 208
Cdd:PRK10636 149 ---DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIW-----LEKWLKSyqgTLILISHDRDFLDPIVDKI 216
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-59 |
5.98e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1053795292 19 GVNLTINKGEITAIIGKSGSGKTVLIKHVVGLLKPDKGHIF 59
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRARF 54
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
30-65 |
7.10e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.23 E-value: 7.10e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1053795292 30 TAIIGKSGSGKTVLIKHVVGLLKPDKGHIFIdgIDI 65
Cdd:COG3451 207 TLILGPSGSGKSFLLKLLLLQLLRYGARIVI--FDP 240
|
|
| |
