|
Name |
Accession |
Description |
Interval |
E-value |
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-240 |
0e+00 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 495.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHVS 240
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHVS 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
3.82e-162 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 447.90 E-value: 3.82e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHV 239
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
6.05e-132 |
|
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: 370.32 E-value: 6.05e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-238 |
1.08e-120 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 343.71 E-value: 1.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 9 KSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG------------MHITDPHASEcDIR 76
Cdd:COG4598 16 KSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgeLVPADRRQLQ-RIR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 REAGMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG4598 95 TRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:COG4598 175 VMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
|
..
gi 505397517 237 QH 238
Cdd:COG4598 255 SS 256
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
1.20e-97 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 284.98 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHI---TDPHASEC-DIRR 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIrLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDmLLNASSNPRLKEFLQ 237
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTEAFAHYLS 241
|
.
gi 505397517 238 H 238
Cdd:COG4161 242 H 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
5.95e-96 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 280.87 E-value: 5.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHI-TDPHASEC-----D 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQkglirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 IRREAGMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKE 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
...
gi 505397517 235 FLQ 237
Cdd:PRK11264 243 FLE 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-240 |
6.23e-96 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 280.36 E-value: 6.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHI---TDPHASE-CDIRR 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAiRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDmllnASSNPRLKEFLQ 237
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS----CFTQPQTEAFKN 238
|
...
gi 505397517 238 HVS 240
Cdd:PRK11124 239 YLS 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
2.15e-92 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 270.76 E-value: 2.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT----TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdpHASE---C 73
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS--SLSErelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 74 DIRREA-GMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALA 152
Cdd:COG1136 82 RLRRRHiGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARdVASRLIFIDRGTIAED 217
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
1.42e-89 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 267.71 E-value: 1.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDI 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREAGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSpdmLLNASSNPR--- 231
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP---VLDVFANPQsel 236
|
....*...
gi 505397517 232 LKEFLQHV 239
Cdd:COG1135 237 TRRFLPTV 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
4.22e-89 |
|
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: 262.99 E-value: 4.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDIRREA 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNaSSNPRLKEFL 236
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA-SDDPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
4.31e-89 |
|
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: 262.04 E-value: 4.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFG----TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD-IR 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 RE-AGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDvASRLIFIDRGTI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-236 |
1.80e-87 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 262.73 E-value: 1.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHasecdiRRE 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPE------KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTH--EIGFArdVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEF 235
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHdqEEALA--LADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235
|
.
gi 505397517 236 L 236
Cdd:COG3842 236 I 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
5.12e-87 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 258.48 E-value: 5.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHasecdir 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 REAGMVFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505397517 157 MMLFDEPTSALDP----ELRHEVLKVmrsLADEGMTMVIVTHEI 196
Cdd:COG1116 159 VLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDV 199
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-239 |
2.32e-86 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 256.68 E-value: 2.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--------PHASE- 72
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplVPADEk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 73 --CDIRREAGMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARA 150
Cdd:TIGR03005 81 hlRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSN 229
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|
gi 505397517 230 PRLKEFLQHV 239
Cdd:TIGR03005 241 ERTREFLSKV 250
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.72e-85 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 254.21 E-value: 1.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT-DPHASECDIRRE 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFG------PIR-VRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtsTWRsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-237 |
4.78e-85 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 253.35 E-value: 4.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 9 KSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHI-----TDPHASECD------IRR 77
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDGQLKVADknqlrlLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRAN-HYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
.
gi 505397517 237 Q 237
Cdd:PRK10619 253 K 253
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
6.56e-85 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 251.90 E-value: 6.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT-TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDIRRE 78
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-219 |
6.66e-85 |
|
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: 252.12 E-value: 6.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTT----PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDI 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREAGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGS 219
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
3.85e-81 |
|
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: 242.04 E-value: 3.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHasecdiRREA 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvpPE------RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
1.65e-80 |
|
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: 240.87 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD-IRREAG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFgPIRV-RKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnASSNPRLKEF 235
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR-ASDDPLVRQF 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-217 |
2.01e-80 |
|
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: 240.45 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGT----TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHasecdirR 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 158 MLFDEPTSALDPELR---HEVLkvMRSLADEGMTMVIVTHEIGFARDVASRLIFIDR--GTIAED 217
Cdd:cd03293 153 LLLDEPFSALDALTReqlQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-236 |
4.88e-80 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 243.90 E-value: 4.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHI-TDPHasecdiRREAGMVF 83
Cdd:COG1118 8 ISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTnLPPR------ERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 QQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:COG1118 82 QHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 164 TSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-221 |
7.60e-80 |
|
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: 239.16 E-value: 7.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAG 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE--LRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQ----QfhLFpHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG1122 79 LVFQnpddQ--LF-APTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-223 |
7.76e-80 |
|
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: 239.39 E-value: 7.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGT-TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT-DPHASECDIRREAG 80
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINkLKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFG------PIRV-RKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAV 153
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGrlgrrsTWRSlFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
9.26e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 231.49 E-value: 9.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMhitDPHASECDIRREAGM 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENV-MFGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG1131 78 VPQEPALYPDLTVRENLrFFA--RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
5.67e-76 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 233.43 E-value: 5.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIrreaG 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 161 DEPTSALDPELRHEvlkvMRS-----LADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:COG3839 158 DEPLSNLDAKLRVE----MRAeikrlHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
4.58e-75 |
|
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: 235.95 E-value: 4.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-D 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 IRREAGMVFQQ-FH-LFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARAL 151
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
7-236 |
2.17e-74 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 226.02 E-value: 2.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAI-----SSGTLLVAGMHITDPHASECDIRREAGM 81
Cdd:TIGR00972 7 LNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLvpgvrIEGKVLFDGQDIYDKKIDVVELRRRVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPhLTALENVMFGPIRVRKQSKAAAREQALALLDRVGL----KDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:TIGR00972 87 VFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:TIGR00972 166 LLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTEDYI 243
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
4.47e-74 |
|
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: 222.83 E-value: 4.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGpirvrkqskaaareqalalldrvglkdranhypseLSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-236 |
6.02e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 224.20 E-value: 6.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHasecDIRR 77
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRdlDPV----ELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGL--KDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 156 KMMLFDEPTSALDP----ELRHEVLKVMRSLadeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPR 231
Cdd:COG1125 156 PILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*
gi 505397517 232 LKEFL 236
Cdd:COG1125 233 VADFV 237
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
2.18e-72 |
|
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: 220.63 E-value: 2.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT-TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRRE 78
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFGpiRVRKQS---------KAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIAR 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG--RLGYKPtwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
1.93e-71 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 221.60 E-value: 1.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDI 75
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREAGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGS 219
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
2.84e-71 |
|
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: 216.56 E-value: 2.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGT--TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQ-FHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03225 79 LVFQNpDDQFFGPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-239 |
5.50e-71 |
|
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: 217.90 E-value: 5.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRRE-AGMVFQ 84
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrELRRKkISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:cd03294 110 SFALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 165 SALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHV 239
Cdd:cd03294 189 SALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-221 |
7.41e-71 |
|
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: 216.28 E-value: 7.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAI-----SSGTLLVAGMHITDPHASECDIR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 REAGMVFQQFHLFPhLTALENVMFGPIRVRKQSKAAAREQALALLDRVGL----KDRANhyPSELSGGQQQRVAIARALA 152
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
1.64e-70 |
|
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: 215.67 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdirREAGM 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGpIRVRKQ----SKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFG-LRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-229 |
3.26e-70 |
|
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: 214.79 E-value: 3.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHasecdiRREA 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpPH------KRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSN 229
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
1.64e-68 |
|
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: 210.37 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTT----PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT----DPHASe 72
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARAR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 73 cdIRRE-AGMVFQQFHLFPHLTALENVMFgPIRVRkqSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:COG4181 87 --LRARhVGFVFQSFQLLPTLTALENVML-PLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDvASRLIFIDRGTIAED 217
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
2.27e-68 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 214.18 E-value: 2.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdirREAGM 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFG----PIRVRKqSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlPRRERP-NAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 505397517 237 QHV 239
Cdd:PRK10851 238 GEV 240
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
5.26e-68 |
|
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: 208.90 E-value: 5.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 R-EAGMVFQ--QFHLFPHLTALENVMFGPIRVRKQSKAAAR-EQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARAL 151
Cdd:cd03257 81 RkEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARkEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
6.29e-68 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 208.84 E-value: 6.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVlhDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdirREAG 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLG-LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-237 |
6.40e-68 |
|
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: 209.46 E-value: 6.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAG 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE--LRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDR--ANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQ 237
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-239 |
6.14e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 211.50 E-value: 6.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 9 KSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRRE-AGMVFQQF 86
Cdd:COG4175 35 EKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrELRRKkMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 87 HLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:COG4175 115 ALLPHRTVLENVAFG-LEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 167 LDP----ELRHEVLKVMRSLadeGMTMVIVTHEIgfarDVASRLifIDRGTIAEDG------SPDMLLNASSNPRLKEFL 236
Cdd:COG4175 194 LDPlirrEMQDELLELQAKL---KKTIVFITHDL----DEALRL--GDRIAIMKDGrivqigTPEEILTNPANDYVADFV 264
|
...
gi 505397517 237 QHV 239
Cdd:COG4175 265 EDV 267
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
7.33e-67 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 206.48 E-value: 7.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPhasecdiRREAG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHL---FPhLTALENVM---FGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRDVVLmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAeDGSPDMLLNA 226
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTP 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
1.08e-65 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 202.48 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT-TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD-IRRE 78
Cdd:TIGR02673 1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPlLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRG 212
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-226 |
1.55e-65 |
|
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: 203.74 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE--LARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFG--P-IRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-237 |
1.98e-65 |
|
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: 203.11 E-value: 1.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT----TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdpHASECDIR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT--RRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 REAGMVFQQ----FHlfPHLTaLENVMFGPIRVrkQSKAAAREQALALLDRVGLKDR-ANHYPSELSGGQQQRVAIARAL 151
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHT-VDRILAEPLRI--HGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*..
gi 505397517 231 RLKEFLQ 237
Cdd:COG1124 234 YTRELLA 240
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-234 |
9.16e-65 |
|
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: 201.81 E-value: 9.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHAsecdiRRE 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpPHR-----IAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMV--FQQFHLFPHLTALENVM---------------FGPIRVRKQSkAAAREQALALLDRVGLKDRANHYPSELSGGQ 141
Cdd:COG0411 79 LGIArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREE-REARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 142 QQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250
....*....|....
gi 505397517 221 DMLLNassNPRLKE 234
Cdd:COG0411 238 AEVRA---DPRVIE 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
1.31e-64 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 208.99 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF--GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL---EAISSGTLLVAGMHITDphASECDI 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLE--LSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREAGMVFQQF--HLFPhLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAV 153
Cdd:COG1123 82 GRRIGMVFQDPmtQLNP-VTVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-236 |
6.98e-64 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 199.49 E-value: 6.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 11 FGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL-----EAISSGTLLVAGMHITDPHASECDIRREAGMVFQQ 85
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPDVDVVELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPHlTALENVMFGP--IRVRKQSKAAAR-EQAL---ALLDRVglKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG1117 101 PNPFPK-SIYDNVAYGLrlHGIKSKSELDEIvEESLrkaALWDEV--KDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 160 FDEPTSALDP-------ELrhevlkvMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRL 232
Cdd:COG1117 178 MDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
....
gi 505397517 233 KEFL 236
Cdd:COG1117 250 EDYI 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-231 |
1.34e-63 |
|
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: 198.04 E-value: 1.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHAsecdiRREAGMV-- 82
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlpPHE-----IARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 FQQFHLFPHLTALENVMFGPIRVRK---------QSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAV 153
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNassNPR 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN---NPR 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-236 |
1.35e-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: 195.85 E-value: 1.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhiTDPHASECDIRREAG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG---EDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENV-MFGPIRvrKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG4555 78 VLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-235 |
1.69e-62 |
|
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: 199.11 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHAsecdiRREAGMVFQQ 85
Cdd:TIGR03265 10 IRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlPPQ-----KRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:TIGR03265 85 YALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 166 ALDPE----LRHEVLKVMRSLadeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEF 235
Cdd:TIGR03265 164 ALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADF 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
4.22e-62 |
|
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: 193.39 E-value: 4.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD-IRREA 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-220 |
9.46e-61 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 195.17 E-value: 9.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecdiRREAGM 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----NRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 162 EPTSALDPELR----HEVLKVMRSLadeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK09452 170 ESLSALDYKLRkqmqNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
1.28e-60 |
|
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: 189.77 E-value: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIrreaGM 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI----AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
5.53e-60 |
|
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: 186.45 E-value: 5.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhiTDPHASECDIRREAGM 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---KDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVmfgpirvrkqskaaareqalalldrvglkdranhypsELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-225 |
5.86e-60 |
|
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: 188.41 E-value: 5.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHASecdIRREAG 80
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpPHER---ARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRvgLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-239 |
1.03e-59 |
|
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: 192.37 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 9 KSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHASECDIRREAGMVFQQF 86
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqSPVELREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 87 HLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 167 LDP----ELRHEVLKVMRSLadeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHV 239
Cdd:TIGR01186 160 LDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-220 |
1.37e-59 |
|
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: 188.79 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF--GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPhasEC--DIRR 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE---ENlwEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQ----QFhlfPHLTALENVMFGP---------IRVRKQSkaaareqalaLLDRVGLKDRANHYPSELSGGQQQR 144
Cdd:TIGR04520 78 KVGMVFQnpdnQF---VGATVEDDVAFGLenlgvpreeMRKRVDE----------ALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSP 220
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTP 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-214 |
4.48e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 4.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMV 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE--WRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 FQQFHLFPHlTALENVMFgPIRVRKqsKAAAREQALALLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:COG4619 80 PQEPALWGG-TVRDNLPF-PFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 162 EPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-209 |
2.33e-58 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 183.59 E-value: 2.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRREA-GMVFQ 84
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAsKFRREKlGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMFGPIRVRKqSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:TIGR03608 84 NFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505397517 165 SALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFArDVASRLIFI 209
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-216 |
4.28e-58 |
|
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: 183.71 E-value: 4.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 13 TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDIR-REAGMVFQQFHLFP 90
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErAKLRnKKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:TIGR02211 97 DFTALENVAM-PLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505397517 171 LRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAE 216
Cdd:TIGR02211 176 NAKIIFDLMLELnRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-220 |
3.10e-57 |
|
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: 183.04 E-value: 3.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT-DPHASECDIRREAGMVFQqfhlFPH- 91
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDLRKKVGLVFQ----FPEh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 ----LTALENVMFGPIRVrKQSKAAAREQALALLDRVGL----KDRAnhyPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:TIGR04521 94 qlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 164 TSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-236 |
6.24e-57 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 185.20 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL--EAISSGTLLVAGMHITD--PHasecdiRR 77
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFvkAAGLTGRIAIADRDLTHapPH------KR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:TIGR03258 80 GLALLFQNYALFPHLKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADE--GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEF 235
Cdd:TIGR03258 159 LLLDEPLSALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEF 238
|
.
gi 505397517 236 L 236
Cdd:TIGR03258 239 L 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-231 |
8.37e-57 |
|
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: 183.33 E-value: 8.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLE---AISSGTLLVAGMHITdpHASEC 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLL--KLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 74 DIR----REAGMVFQQfhlfPhLTALENVMfgpiRVRKQ-----------SKAAAREQALALLDRVGL---KDRANHYPS 135
Cdd:COG0444 79 ELRkirgREIQMIFQD----P-MTSLNPVM----TVGDQiaeplrihgglSKAEARERAIELLERVGLpdpERRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 136 ELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....*..
gi 505397517 215 AEDGSPDMLLNassNPR 231
Cdd:COG0444 230 VEEGPVEELFE---NPR 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
1.94e-56 |
|
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: 178.88 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphasecdIRREAGMV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-------ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 FQQFHL---FPhLTALENVM---FGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIA 215
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
6.31e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 179.29 E-value: 6.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFG----TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAsecdir 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 rEAGMVFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG4525 77 -DRGVVFQKDALLPWLNVLDNVAFG-LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 157 MMLFDEPTSALDPELRHE----VLKVMRslaDEGMTMVIVTHEIGFARDVASRLI 207
Cdd:COG4525 155 FLLMDEPFGALDALTREQmqelLLDVWQ---RTGKGVFLITHSVEEALFLATRLV 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-223 |
1.95e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 180.69 E-value: 1.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIrreaGM 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI----CM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQ---ALALLDRVGLKDRanhYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRvkeALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
2.53e-55 |
|
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: 176.71 E-value: 2.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHAsecdiRRE 78
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpPHR-----IAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVF--QQFHLFPHLTALENVMFGPIRVRKQSKAAAR-EQALALLDRvgLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:COG0410 78 LGIGYvpEGRRIFPSLTVEENLLLGAYARRDRAEVRADlERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNassNPRLKEF 235
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA---DPEVREA 232
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-194 |
2.61e-55 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 176.45 E-value: 2.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT----TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASECDI 75
Cdd:NF038007 1 MLNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RRE-AGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:NF038007 81 RRElIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-220 |
5.36e-55 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 180.23 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdirREAGM 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGpIRVRKQSKAAAR---EQALALLDRVGLKDRAnhyPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFG-LKLAGAKKEEINqrvNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 159 LFDEPTSALDPEL----RHEVLKVMRSLadeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK11000 156 LLDEPLSNLDAALrvqmRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
7.65e-54 |
|
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: 170.14 E-value: 7.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPhaSECDIRREAGMVFQQFHLFPHLTALE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 97 NVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANH----YPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:pfam00005 79 NLRLG-LLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-238 |
1.60e-53 |
|
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: 176.06 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--------PHasecdiRREAGMVFQQFHLFP 90
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargiflpPH------RRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HLTALENVMFGPIRVRKQSKAAAREQALALLdrvGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 171 LRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnasSNPRLKEFLQH 238
Cdd:COG4148 168 RKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL---SRPDLLPLAGG 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
2.27e-53 |
|
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: 182.73 E-value: 2.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFG--TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHasecDIRR 77
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPA----SLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFpHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVA 146
Cdd:COG2274 550 QIGVVLQDVFLF-SGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-240 |
2.55e-53 |
|
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: 174.60 E-value: 2.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 32 IIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHasecdiRREAGMVFQQFHLFPHLTALENVMFgPIRVRKQS 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNvpPH------LRHINMVFQSYALFPHMTVEENVAF-GLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 110 KAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR----HEVLKVMRSLade 185
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRdqmqLELKTIQEQL--- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 186 GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHVS 240
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEIN 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-217 |
4.25e-53 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 181.08 E-value: 4.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE-CDI 75
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREA-GMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK10535 84 RREHfGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAED 217
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-218 |
7.22e-53 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 177.90 E-value: 7.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASEcdirrE 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQ-----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AG--MVFQQFHLFPHLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG1129 79 AGiaIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 155 PKMMLFDEPTSALDpelRHEV---LKVMRSLADEGMTMVIVTH---EIgfaRDVAsrlifiDRGTIAEDG 218
Cdd:COG1129 159 ARVLILDEPTASLT---EREVerlFRIIRRLKAQGVAIIYISHrldEV---FEIA------DRVTVLRDG 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
1.37e-52 |
|
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: 168.00 E-value: 1.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMV 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE--LARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 fqqfhlfphltalenvmfgpirvrkqskaaarEQALALLDRVGLKDRanhYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:cd03214 79 --------------------------------PQALELLGLAHLADR---PFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 163 PTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
4.42e-51 |
|
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: 164.96 E-value: 4.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhiTDPHASECDIRREAG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG---EPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFgpirVRKQSK-AAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG4133 79 YLGHADGLKPELTVRENLRF----WAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-227 |
1.10e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.43 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSksF---GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASecdIRR 77
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLES---LRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFpHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVA 146
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
.
gi 505397517 227 S 227
Cdd:COG1132 565 G 565
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-218 |
1.27e-50 |
|
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: 164.20 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVlhDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdirREAGM 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD----RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLG-LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 162 EPTSALDPELRHEVLK-VMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03298 154 EPFAALDPALRAEMLDlVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
2.56e-50 |
|
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: 161.64 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE--LRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 FQqfhlfphltalenvmfgpirvrkqskaaareqalalldrvglkdranhypseLSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505397517 163 PTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-217 |
3.71e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.47 E-value: 3.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 6 AVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLvAGmhitdpHASECDIRREAGMVFQQ 85
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AG------TAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:PRK11247 90 ARLLPWKKVIDNVGLG-------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 166 ALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAED 217
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-218 |
2.03e-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: 161.31 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 18 HDINLKIEA-GEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphaSECDI-----RREAGMVFQQFHLFPH 91
Cdd:cd03297 13 FTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD---SRKKInlppqQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFGpirVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:cd03297 90 LNVRENLAFG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505397517 172 RHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
16-236 |
2.03e-49 |
|
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: 161.73 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PhasecdIRREAGMVFQQFHLFPHLT 93
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlpP------EKRDISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:cd03299 88 VYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 174 EVLKVMRSLADEGMTMVI-VTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:cd03299 167 KLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
2.94e-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: 159.09 E-value: 2.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTT--PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREA 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD--LDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFpHLTALENVmfgpirvrkqskaaareqalalldrvglkdranhypseLSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADeGMTMVIVTHEIGFARDvASRLIFIDRG 212
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-228 |
4.18e-49 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 160.90 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 21 NLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhitDPHASECDIRREAGMVFQQFHLFPHLTALENVMF 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 101 G--P-IRVrkqsKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK 177
Cdd:PRK10771 95 GlnPgLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505397517 178 VMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASS 228
Cdd:PRK10771 171 LVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-234 |
1.11e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 160.33 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 11 FGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL-----EAISSGTLLVAGMHITDPHASECDIRREAGMVFQQ 85
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPhLTALENVMFGpIRVR----KQSKAAAREQAL---ALLDRVglKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK14239 95 PNPFP-MSIYENVVYG-LRLKgikdKQVLDEAVEKSLkgaSIWDEV--KDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAE-DGSPDMLLnassNPRLKE 234
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEyNDTKQMFM----NPKHKE 242
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-220 |
3.70e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 160.21 E-value: 3.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGMVFQ--QFHLFPHlTA 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMFGPIR-------VRKQSKAAAReqaLALLDRVGLKDRAnhyPSELSGGQQQRVAIARALAVKPKMMLFDEPTSAL 167
Cdd:PRK13637 102 EKDIAFGPINlglseeeIENRVKRAMN---IVGLDYEDYKDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 168 DPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-220 |
4.22e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 159.80 E-value: 4.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 13 TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAGMVFQ----QFhl 88
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVWDVRRQVGMVFQnpdnQF-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 89 fPHLTALENVMFGpirvrKQSKAAAREQAL----ALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK13635 95 -VGATVQDDVAFG-----LENIGVPREEMVervdQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 165 SALDPELRHEVLKVMRSLADEGMTMVI-VTHEIGFARDvASRLIFIDRGTIAEDGSP 220
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
8.86e-48 |
|
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: 157.21 E-value: 8.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF------GTT-PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLV--AGMHITDPHAS 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 72 ECDI----RREAGMVFQQFHLFPHLTALENVMfGPIRVRKQSKAAAREQALALLDRVGLKDRANH-YPSELSGGQQQRVA 146
Cdd:COG4778 84 PREIlalrRRTIGYVSQFLRVIPRVSALDVVA-EPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-223 |
1.32e-47 |
|
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: 159.09 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 9 KSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphaSECD-IRREAGMVFQQFH 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRkVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 LFPHLTALEN-VMFGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:TIGR01188 77 VDEDLTGRENlEMMG--RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 167 LDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
2.24e-47 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 160.01 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIrrea 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFGpIRVRKQSKA--AAR-EQALALLDRVGLKDRAnhyPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYG-LKIRGMPKAeiEERvAEAARILELEPLLDRK---PRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 157 MMLFDEPTSALDPELRH----EVLKVMRSLadeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVqmrlEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-238 |
2.38e-47 |
|
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: 164.55 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF--GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREA 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFpHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIA 148
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTH-EIGFARdvASRLIFIDRGTIAEDGSPDMLLNAs 227
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHrLAGLER--MDRILVLEDGRIVEQGTHEELLAQ- 559
|
250
....*....|.
gi 505397517 228 sNPRLKEFLQH 238
Cdd:COG4987 560 -NGRYRQLYQR 569
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
4.19e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 154.95 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI--NKLEAIS-SGTLLVAGMHITD--PHasecdi 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSaSGEVLLNGRRLTAlpAE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREAGMVFQQFHLFPHLTALENVMFG-PIRVrkqSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFAlPPTI---GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLK-VMRSLADEGMTMVIVTHEIGFARDvASRLIFIDR 211
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-227 |
8.65e-47 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 155.66 E-value: 8.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRReaG 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHL-FPhLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRanHYPsELSGGQQQRVAIARALA----- 152
Cdd:COG4559 79 VLPQHSSLaFP-FTVEEVVALGraPHGSSAAQDRQIVREALALVGLAHLAGR--SYQ-TLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 153 --VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNAS 227
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-231 |
2.65e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 156.43 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRREAGMVFQ--QFHLFPHLTAL 95
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrPLRRRMQMVFQdpYASLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMFgPIRV-RKQSKAAAREQALALLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:COG4608 116 DIIAE-PLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 174 EVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnasSNPR 231
Cdd:COG4608 195 QVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY---ARPL 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-231 |
2.69e-46 |
|
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: 161.01 E-value: 2.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKS----TLLRCINKLEAISSGTLLVAGMHITdpHASE---CDIR-REAGMVF 83
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL--GLSErelRRIRgNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 QQfhlfPhLTALENVMfgpiRVRKQ-----------SKAAAREQALALLDRVGLKD---RANHYPSELSGGQQQRVAIAR 149
Cdd:COG4172 99 QE----P-MTSLNPLH----TIGKQiaevlrlhrglSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnasS 228
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF---A 246
|
...
gi 505397517 229 NPR 231
Cdd:COG4172 247 APQ 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
7.45e-46 |
|
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: 160.31 E-value: 7.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFpHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIAR 149
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLG-------RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-220 |
8.44e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 154.09 E-value: 8.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDpHASECDIRREAGMVFQQfhlfP--H 91
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD-EENLWDIRNKAGMVFQN----PdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTAL---ENVMFGPIRVRKQSKAAaREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK13633 98 IVATiveEDVAFGPENLGIPPEEI-RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 169 PELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSP 220
Cdd:PRK13633 177 PSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-205 |
8.65e-46 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.04 E-value: 8.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASecdIRRE 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDA---IALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASR 205
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADR 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
9.54e-46 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 152.93 E-value: 9.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT--TPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFG--PI---RVRKQSKAAArEQALALLDRVGLKDRanhYPSELSGGQQQRVAIARALAVKP 155
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGrfPYskgRLTAEDREII-DEAIAYLDLEDLADR---YLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 156 KMMLFDEPTSALDpeLRHEV--LKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:COG4604 155 DYVLLDEPLNNLD--MKHSVqmMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-220 |
1.10e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 153.83 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC--DIRREAGMVFQ--QFHLFPHl 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 TALENVMFGPIRVrKQSKAAAREQALALLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK13641 102 TVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-226 |
1.30e-45 |
|
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: 152.55 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSG-TLLVAG--MHITDPHasecDIRR 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerRGGEDVW----ELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLF--PHLTALENVM---FGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALA 152
Cdd:COG1119 79 RIGLVSPALQLRfpRDETVLDVVLsgfFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEG-MTMVIVTH---EI--GFardvaSRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKEEVLTS 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-218 |
1.52e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 152.30 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 11 FGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL-----EAISSGTLLVAGMHITDPHASECDIRREAGMVFQQ 85
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPHLTALENVMFGpIRVRKQSKAAAR-----EQAL---ALLDRVglKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIG-VKLNGLVKSKKEldervEWALkkaALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-226 |
1.61e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 152.62 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRReaG 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHL-FPhLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRanHYPsELSGGQQQRVAIARALA----- 152
Cdd:PRK13548 80 VLPQHSSLsFP-FTVEEVVAMGraPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 153 -VKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-221 |
1.63e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.55 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAsecdirrEAG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 161 DEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFI--DRGTIAEDGSPD 221
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPLN 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-236 |
2.98e-45 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 150.75 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHAsecdiRREAG 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlpPHE-----RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 M--VFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRvgLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:TIGR03410 77 IayVPQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLlnasSNPRLKEFL 236
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYL 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
4.71e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.61 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHasecdiRRE 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvpPY------QRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 159 LFDEPTSALDPELRHEV-LKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-214 |
1.52e-44 |
|
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: 148.17 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhitdPHASECDIRREAGMVFQ--QFHLFphlt 93
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----KPIKAKERRKSIGYVMQdvDYQLF---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 alENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:cd03226 86 --TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505397517 174 EVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-239 |
1.77e-44 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 153.65 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRREA-GMVFQQFHLFPHLTALE 96
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrEVRRKKiAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 97 NVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVL 176
Cdd:PRK10070 126 NTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 177 KVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHV 239
Cdd:PRK10070 205 DELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
8.54e-44 |
|
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: 146.59 E-value: 8.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHasecDIRREAGM 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI----EALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGPIRVRKQSKAAAReqalaLLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.74e-43 |
|
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: 145.98 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT-DPHasecDIRREAG 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEPR----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENV-MFGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03265 77 IVFQDLSVDDELTGWENLyIHA--RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-206 |
1.83e-43 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 146.50 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASECDIR-REAGMVFQQFHLFPH 91
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK11629 102 FTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 505397517 172 RHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRL 206
Cdd:PRK11629 181 ADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-215 |
1.93e-43 |
|
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: 145.77 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 21 NLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHitdpHASECDIRREAGMVFQQFHLFPHLTALENVMF 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS----HTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 101 GpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMR 180
Cdd:TIGR01277 94 G-LHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 505397517 181 SLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIA 215
Cdd:TIGR01277 173 QLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-220 |
2.17e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.86 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVaGMHITDPHASECD---IRREAGMVFQ--QFHLFPH 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlkpLRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 lTALENVMFGPIRVrKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:PRK13634 102 -TVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505397517 171 LRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13634 180 GRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-231 |
2.36e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 146.60 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 10 SFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL-----EAISSGTLLVAGMHITDPHASEcdIRREAGMVFQ 84
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE--LRRRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMFGPIRVR-KQSKAAAREQALALLDRVGL----KDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnasSNPR 231
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF---TNPR 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
4.22e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 147.54 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC---------------------- 73
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 74 DIRREAGMVFQ--QFHLFPHlTALENVMFGPIRVrKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARA 150
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
7.01e-43 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 145.93 E-value: 7.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL---EAISSGTLLVAGMHITDPHASECDIRR 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 ---EAGMVFQQFHLFPHLTALENVMFGPI-------RVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAI 147
Cdd:PRK09984 84 sraNTGYIFQQFNLVNRLSVLENVLIGALgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGS 219
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
8.87e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 146.41 E-value: 8.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHasecdIRR--- 77
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-----RRRigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 ---EAGmvfqqfhLFPHLTALENVM-FGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAV 153
Cdd:COG4152 76 lpeERG-------LYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-232 |
1.60e-42 |
|
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: 147.57 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC--DIRREAGMVFQQFHLFPHLTALE 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlpPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 97 NVMFGPIRVRKQSKAAAREQALALLDRVGLKDRanhYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVL 176
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 177 KVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRL 232
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
2.08e-42 |
|
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: 142.56 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGMVFQ--QFHLF 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 pHLTALENVMFGPIRV-RKQSKAAAR-EQALALLDRVGLKDRANHYpseLSGGQQQRVAIARALAVKPKMMLFDEPTSAL 167
Cdd:TIGR01166 83 -AADVDQDVAFGPLNLgLSEAEVERRvREALTAVGASGLRERPTHC---LSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 505397517 168 DPELRHEVLKVMRSLADEGMTMVIVTHEIGFA 199
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-231 |
2.14e-42 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 152.33 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF--GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPhaseCDIRR 77
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDP----ADLRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFpHLTALENVMFGpirvrkqsKAAAREQA-LALLDRVGLKDRANHYPS-----------ELSGGQQQRV 145
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALG--------APYADDEEiLRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAV 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFArDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVLE 688
|
....*.
gi 505397517 226 ASSNPR 231
Cdd:TIGR03375 689 ALRKGR 694
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
4.88e-42 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 142.32 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD-IRRE 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRG 212
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-220 |
8.61e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 144.61 E-value: 8.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD--------------IRREAGM 81
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQ--QFHLFPHlTALENVMFGPIRVrKQSKAAAREQALALLDRVGLKDR-ANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-218 |
1.50e-41 |
|
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: 141.45 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAsecdirrEAGMVFQQFHLFPHLTALE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-------DRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 97 NVMFGPIRVRKQSKAAAREQAL-ALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEV 175
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVeEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505397517 176 L-KVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:TIGR01184 154 QeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-220 |
4.48e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 141.37 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGMVFQQ--FHLFPH 91
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNpdDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 lTALENVMFGPIRVrKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK13639 95 -TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-208 |
6.19e-41 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 141.07 E-value: 6.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 6 AVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL-EAISS----GTLLVAGMHITDPHASECDIRREAG 80
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIPGfrveGKVTFHGKNLYAPDVDPVEVRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHlTALENVMFGP-IRVRKQSKAAAREQAL---ALLDRVglKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGArINGYKGDMDELVERSLrqaALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDVASRLIF 208
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTAF 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
7.88e-41 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 139.53 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFG----TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASECD 74
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqpLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 IRREAGMVFQQFHLFPHLTALENVMFgPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDrGTIAED 217
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVN-GQLQEE 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-230 |
2.27e-40 |
|
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: 145.21 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAiSSGTLLVAGMHITDPHASEC-DIRREAGMVFQQ-F-HLFPHLT 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALrPLRRRMQVVFQDpFgSLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGpIRV--RKQSKAAAREQALALLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:COG4172 381 VGQIIAEG-LRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 171 LRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:COG4172 460 VQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
5.04e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.59 E-value: 5.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGT--TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRRE 78
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE--IRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQ----QFhlfPHLTALENVMFG--PIRV-RKQSKAAAREQAlallDRVGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:PRK13632 85 IGIIFQnpdnQF---IGATVEDDIAFGleNKKVpPKKMKDIIDDLA----KKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVI-VTHEIGFARdVASRLIFIDRGTIAEDGSPDMLLNAssnp 230
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN---- 232
|
....*..
gi 505397517 231 rlKEFLQ 237
Cdd:PRK13632 233 --KEILE 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
1.28e-39 |
|
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: 136.18 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF--GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecDIRREA 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA--DLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFpHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIA 148
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLG-------APLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFArDVASRLIFIDRGTIAEDG 218
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-233 |
1.52e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.81 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcDIRREA 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ-GIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHL-FPHLTALENVMFGP-------IRVRKQSkaaarEQALAlldRVGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGPenlclppIEIRKRV-----DRALA---EIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLnasSNPR 231
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL---SDVS 227
|
..
gi 505397517 232 LK 233
Cdd:PRK13644 228 LQ 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.58e-39 |
|
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: 134.09 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGM--HITDPHASecdirREA 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDA-----RRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 G--MVFQqfhlfphltalenvmfgpirvrkqskaaareqalalldrvglkdranhypseLSGGQQQRVAIARALAVKPKM 157
Cdd:cd03216 76 GiaMVYQ----------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIA 215
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
2.24e-39 |
|
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: 135.82 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTT-PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFpHLTALENVMFGPIRVRKQSKAAAREQAlALLDRV--------------GLKdranhypseLSGGQQQRVA 146
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAA-QIHDKImrfpdgydtivgerGLK---------LSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-220 |
2.42e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 137.24 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTT--PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL---EAISSGTLLVAGMHITDphASECDIR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 REAGMVFQQ-FHLFPHLTALENVMFGpirvrKQSKAAAREQALAL----LDRVGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFG-----LENRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLA-DEGMTMVIVTHEIGFArDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSP 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
2.94e-39 |
|
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: 135.01 E-value: 2.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGeVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMhitDPHASECDIRREAGM 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIA-WLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 162 EPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
8.30e-39 |
|
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: 134.28 E-value: 8.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFG--TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecDIRREA 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLA--SLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFpHLTALENVMFG-PIRVRKQSKAAARE-QALALLDRV--GLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYGrPGATREEVEEAARAaNAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLL 224
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-223 |
1.78e-38 |
|
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: 133.01 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFG--TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHI-TDPHAsecdIRREAGMVF 83
Cdd:cd03263 6 LTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKA----ARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 QQFHLFPHLTALENVMFGpIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:cd03263 82 QFDALFDELTVREHLRFY-ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 164 TSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-220 |
1.94e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 134.87 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDpHASECDI---RREAGMVFQ--QFHLF 89
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-TSKNKDIkqiRKKVGLVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHlTALENVMFGPIRV---RKQSKAAAREQaLALldrVGL-KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:PRK13649 100 EE-TVLKDVAFGPQNFgvsQEEAEALAREK-LAL---VGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 166 ALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
2.65e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.02 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAI------SSGTLLVAGMHITDPHASEcdIRREAGMVFQQFHLF 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIK--LRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHLTALENVMFgPIRVRK-QSKAAAREQALALLDRVGL----KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK14246 103 PHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 165 SALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-240 |
3.34e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 134.07 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 11 FGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL-EAIS----SGTLLVAGMHITDpHASECDIRREAGMVFQQ 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFN-YRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPhLTALENVMFGpIRVRKQ-SKAAAREQALALLDRVGL----KDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK14271 110 PNPFP-MSIMDNVLAG-VRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnasSNPRLKEFLQHVS 240
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF---SSPKHAETARYVA 263
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-224 |
5.66e-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: 132.35 E-value: 5.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASecdIRREA 79
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHlTALENVMFG-PIRVRKQSKAAARE-QALALLDRvgLKDRANHYPSE----LSGGQQQRVAIARALAV 153
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLGrPNATDEEVIEAAKEaGAHDFIMK--LPNGYDTVLGEnggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLL 224
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-212 |
9.77e-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: 130.86 E-value: 9.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphasecDIRREAGM 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI------AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALENVM-FGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRG 212
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-228 |
1.36e-37 |
|
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: 131.45 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHAsecdIRREAGMVFQQFHLFpHLT 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdLALADPAW----LRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFG-PIRVRKQSKAAAR---EQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:cd03252 92 IRDNIALAdPGMSMERVIEAAKlagAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 170 ELRHEVLKVMRSLADeGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNASS 228
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-218 |
1.95e-37 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 129.59 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 8 SKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCIN--KLEAISSGTLLVAGMHItdphaSECDIRREAGMVFQQ 85
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL-----DKRSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPHLTALENVMFgpirvrkqskaAAREQAlalldrvglkdranhypseLSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:cd03213 91 DILHPTLTVRETLMF-----------AAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 166 ALDPELRHEVLKVMRSLADEGMTMVIVTH----EIGFARDvasRLIFIDRGTIAEDG 218
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTGRTIICSIHqpssEIFELFD---KLLLLSQGRVIYFG 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-236 |
4.08e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 131.04 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRREA 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFgPIRVRKQ-SKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAY-PLREHTQlPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 159 LFDEPTSALDPelrhEVLKVMRSLADE-----GMTMVIVTHEIGFARDVASR-LIFIDRGTIAEdGSPDMlLNASSNPRL 232
Cdd:PRK11831 166 MFDEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHaYIVADKKIVAH-GSAQA-LQANPDPRV 239
|
....
gi 505397517 233 KEFL 236
Cdd:PRK11831 240 RQFL 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-208 |
4.80e-37 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.51 E-value: 4.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 10 SFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhitdphasecdiRREAGMVFQQFHL- 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 89 --FPhLTALENVMFGPIRVR---KQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:NF040873 68 dsLP-LTVRDLVAMGRWARRglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505397517 164 TSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIF 208
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
8.09e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 130.63 E-value: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAGMVFQQ--FHLFPh 91
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKWVRSKVGLVFQDpdDQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFGPIRVRkQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK13647 95 STVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-231 |
1.61e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.85 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDP-HASECDIRREAGMVFQQFH--LFPHLT 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdPEAQKLLRQKIQIVFQNPYgsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 aLENVMFGPIRVRKQ-SKAAAREQALALLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK11308 111 -VGQILEEPLLINTSlSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 172 RHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNassNPR 231
Cdd:PRK11308 190 QAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN---NPR 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-220 |
2.10e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.85 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFG-----TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASE--C 73
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 74 DIRREAGMVFQ--QFHLFPHlTALENVMFGPIRVrKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARA 150
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
2.32e-36 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 134.34 E-value: 2.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhITDPHASECDIRREAG 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--VPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHlTALENVMFGpirvRKQSKAAAREQALAL--LDRV------GLKDRANHYPSELSGGQQQRVAIARALA 152
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLA----RPDASDAEIREALERagLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARD 201
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL 522
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-225 |
2.29e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.20 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGT-TP----VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT----DPHASE 72
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 73 cdIRREAGMVFQqfhlFPHLTALEN-----VMFGPiRVRKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVA 146
Cdd:PRK13646 83 --VRKRIGMVFQ----FPESQLFEDtvereIIFGP-KNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLA-DEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
2.41e-35 |
|
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: 125.17 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMhitDPHASECDIR 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 REAGMVFQQFHLFPHLTALENVM-FGPIRVRKQSKAAAREQALAllDRVGLKDRANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEELA--DRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-223 |
2.49e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.77 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 13 TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAseCDIRREAGMVFQQ-FHLFPH 91
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENV--WDIRHKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFGpirvrKQSKAAARE-------QALALldrVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK13650 97 ATVEDDVAFG-----LENKGIPHEemkervnEALEL---VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 165 SALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGfarDVA--SRLIFIDRGTIAEDGSPDML 223
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.23e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 126.48 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdiRREAGM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA---RARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFPHLTALEN-VMFGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK13536 119 VPQFDNLDLEFTVRENlLVFG--RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
1.35e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.69 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHAsecdiRREA 79
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSraRHA-----RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVM-FGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLvFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
1.54e-34 |
|
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: 123.42 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTP---VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAseCDIRRE 78
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL--RWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPhLTALENVMFG-PIRVRKQSKAAAReQALALLDRVGLKDRAN----HYPSELSGGQQQRVAIARALAV 153
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYGkPDATDEEVEEAAK-KANIHDFIMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLL 224
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
13-229 |
1.99e-34 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 129.86 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 13 TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMH--ITDPHAsecdIRREAGMVFQQFHLFP 90
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDlaIADPAW----LRRQMGVVLQENVLFS 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HlTALENVMFGP-----IRVRKQSKAAAREQALALLDRvGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:TIGR01846 545 R-SIRDNIALCNpgapfEHVIHAAKLAGAHDFISELPQ-GYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 166 ALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNASSN 229
Cdd:TIGR01846 623 ALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLALQGL 684
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-234 |
5.42e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 121.88 E-value: 5.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdiRREAGMVF--Q 84
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK---RARLGIGYlpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMfGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:cd03218 83 EASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 165 SALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNassNPRLKE 234
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA---NELVRK 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-215 |
7.82e-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: 121.22 E-value: 7.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLE--AISSGTLLVAGMHItDPHASecdiRREAGMVFQQFHLFPHL 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEggGTTSGQILFNGQPR-KPDQF----QKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 TALENVMFGPI-RVRKQSKAAAREQ--ALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:cd03234 97 TVRETLTYTAIlRLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505397517 170 ELRHEVLKVMRSLADEGMTMVIVTHEIG---FarDVASRLIFIDRGTIA 215
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-226 |
1.23e-33 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 127.77 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHAsecdIRREAGMVFQQFHLFPHl 92
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQA----VRRQLGVVLQNGRLMSG- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 TALENVMFGPIRVRKQSKAAAReqalalldRVGLKDRANHYP-------SE----LSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:TIGR03797 542 SIFENIAGGAPLTLDEAWEAAR--------MAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLLIARALVRKPRILLFD 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 162 EPTSALDPELRHevlKVMRSLADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:TIGR03797 614 EATSALDNRTQA---IVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMAR 674
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-231 |
1.45e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 121.64 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREaG 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ--IARM-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MV--FQQFHLFPHLTALENVMFGPIRVRK--------------QSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQR 144
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
....*...
gi 505397517 224 LNassNPR 231
Cdd:PRK11300 242 RN---NPD 246
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-230 |
1.58e-33 |
|
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: 121.48 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAgMHITDPHA----SECDIR 76
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYI-MRSGAELElyqlSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 R----EAGMVFQQFH--LFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIAR 149
Cdd:TIGR02323 82 RlmrtEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLA-DEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASS 228
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
..
gi 505397517 229 NP 230
Cdd:TIGR02323 242 HP 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
1.71e-33 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 126.32 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFpHLTALENVMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIAR 149
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSlADEGMTMVIVTH 194
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-239 |
1.78e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 123.28 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC-DIRREAGMVFQQ--FHLFPHLTAL 95
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWrAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 EnVMFGPIRVR--KQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:PRK15079 119 E-IIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 173 HEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQHV 239
Cdd:PRK15079 198 AQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-236 |
2.13e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 121.30 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 8 SKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISS-----GTLLVAGMHITDPHASECDIRREAGMV 82
Cdd:PRK14258 14 SFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 FQQFHLFPhLTALENVMFGPIRVRKQSKAAAR---EQALA---LLDRVglKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK14258 94 HPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDdivESALKdadLWDEI--KHKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLA-DEGMTMVIVTHEI----------GFARDVASRLifidrGTIAEDGSPDMLLN 225
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLhqvsrlsdftAFFKGNENRI-----GQLVEFGLTKKIFN 245
|
250
....*....|.
gi 505397517 226 ASSNPRLKEFL 236
Cdd:PRK14258 246 SPHDSRTREYV 256
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
2.54e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.96 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF--GT---TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphaSECDI 75
Cdd:COG1101 1 MLELKNLSKTFnpGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT----KLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 RREA--GMVFQQFHL--FPHLTALENVM----------FGpIRVRKQSKAAAREQaLALLDRvGLKDRANHYPSELSGGQ 141
Cdd:COG1101 77 KRAKyiGRVFQDPMMgtAPSMTIEENLAlayrrgkrrgLR-RGLTKKRRELFREL-LATLGL-GLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 142 QQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAED 217
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-224 |
2.99e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.80 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDP---HASECDIRR----EA 79
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyALSEAERRRllrtEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQqfH----LFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK11701 92 GFVHQ--HprdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLL 224
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
4.78e-33 |
|
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: 124.91 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTL---LRCINKLEAISSGTLLVAGM-----HITDP----- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIIYHVALcekcgYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 69 HASEC--------------------DIRREAGMVFQQ-FHLFPHLTALENVMFGPIRVRKQSKAAArEQALALLDRVGLK 127
Cdd:TIGR03269 81 PCPVCggtlepeevdfwnlsdklrrRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAV-GRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 128 DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE---LRHEVLKvmRSLADEGMTMVIVTHEIGFARDVAS 204
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNALE--EAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260
....*....|....*....|.
gi 505397517 205 RLIFIDRGTIAEDGSPDMLLN 225
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVA 258
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-221 |
5.69e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.12 E-value: 5.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 8 SKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMVFQQfH 87
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALLPQH-H 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 LFPH-LTALENVMFGpirvrkqskaaaREQALALLDRVGLKDR---------------ANHYPSELSGGQQQRVAIARAL 151
Cdd:PRK11231 86 LTPEgITVRELVAYG------------RSPWLSLWGRLSAEDNarvnqameqtrinhlADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
6.47e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.41 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 4 FSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhitdphasecDIRreAGMVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 QQFHLFPHLTALENVM--FGPIRVRKQSKAAARE-----------------------------QALALLDRVGLKDRANH 132
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgDAELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 133 YP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE----LRHEvlkvmrsLADEGMTMVIVTHEIGFARDVASRLI 207
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEF-------LKNYPGTVLVVSHDRYFLDRVATRIL 220
|
....*..
gi 505397517 208 FIDRGTI 214
Cdd:COG0488 221 ELDRGKL 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-226 |
6.84e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 119.94 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAS-EC-DIRreagMVFQ--QFHLFPH 91
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKyRCkHIR----MIFQdpNTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTA---LEnvmfGPIRVRKQSKAAAREQAL-ALLDRVGL-KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:COG4167 104 LNIgqiLE----EPLRLNTDLTAEEREERIfATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 167 LDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG4167 180 LDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
2.73e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF----------------------GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTL 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 59 LVAGmhitdphasecdirR-----EAGMVFQqfhlfPHLTALENVMFGpirvrkqskAAA----REQALALLDRV----G 125
Cdd:COG1134 84 EVNG--------------RvsallELGAGFH-----PELTGRENIYLN---------GRLlglsRKEIDEKFDEIvefaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 126 LKDRAN----HYPSelsgGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARD 201
Cdd:COG1134 136 LGDFIDqpvkTYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....*
gi 505397517 202 VASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-237 |
3.37e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 118.37 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMVFQQF--HLF 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE--VRKFVGLVFQNPddQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHlTALENVMFGPIRVRKQSKAAAR--EQALALLDRVGLKDRANHYpseLSGGQQQRVAIARALAVKPKMMLFDEPTSAL 167
Cdd:PRK13652 93 SP-TVEQDIAFGPINLGLDEETVAHrvSSALHMLGLEELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 168 DPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGS-------PDML----LNASSNPRLKEF 235
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveeiflqPDLLarvhLDLPSLPKLIRS 248
|
..
gi 505397517 236 LQ 237
Cdd:PRK13652 249 LQ 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-217 |
4.02e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 118.25 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASECDIRREAGMVFQ--------QF 86
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 87 HL-------FPHLTALenvmfgpirvrkqSKAAAREQALALLDRVGLKDR-ANHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK10419 107 TVreiirepLRHLLSL-------------DKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 159 LFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAED 217
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-226 |
5.85e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 120.33 E-value: 5.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA--ASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTALENVMFG--PIRVR----KQSKAAAREQALallDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtPHRSRfdtwTETDRAAVERAM---ERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 155 PKMMLFDEPTSALDpeLRHEV--LKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:PRK09536 158 TPVLLLDEPTASLD--INHQVrtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-226 |
1.72e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 120.98 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTT--PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREA 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD--YTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHlTALENVMFGPIR--VRKQSKAAARE-QALALLDRV--GLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEqaDRAEIERALAAaYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-220 |
1.74e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.87 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGMVFQQ--FHLFPh 91
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDpdNQLFS- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFGPIRVrKQSKAAAREQALALLDRVG---LKDRANHYpseLSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK13636 98 ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGiehLKDKPTHC---LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 169 PELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-214 |
2.08e-31 |
|
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: 113.47 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMVFQQFHLFPH 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE--LGDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 lTALENVmfgpirvrkqskaaareqalalldrvglkdranhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:cd03246 91 -SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEIGFARdVASRLIFIDRGTI 214
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
2.78e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.00 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSF-GTTP-VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecDIRRE 78
Cdd:PRK13648 7 IIVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE--KLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQ-FHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDrVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQ-VDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSP 220
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTP 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-226 |
4.69e-31 |
|
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: 119.92 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSksFGTTP---VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASecdIRR 77
Cdd:COG5265 358 VRFENVS--FGYDPerpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQAS---LRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 EAGMVFQQFHLFpHLTALENVMFG-PIRVRKQSKAAAReqaLALLD------------RVG---LKdranhypseLSGGQ 141
Cdd:COG5265 433 AIGIVPQDTVLF-NDTIAYNIAYGrPDASEEEVEAAAR---AAQIHdfieslpdgydtRVGergLK---------LSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 142 QQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPD 221
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHA 577
|
....*
gi 505397517 222 MLLNA 226
Cdd:COG5265 578 ELLAQ 582
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-236 |
4.87e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.42 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKS----TLLRCINKLEAI-SSGTLLVAGMHITdpHASECDIRREAG----MVFQQ 85
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLL--HASEQTLRGVRGnkiaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 --FHLFPhLTALENVMFGPIRV-RKQSKAAAREQALALLDRVGL---KDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK15134 101 pmVSLNP-LHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFL 236
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-224 |
5.67e-31 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 119.77 E-value: 5.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLL-----RCINKLEAisSGTLLVAGMHITDPhasecDIRREAGMVFQQFHLFPH 91
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAK-----EMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMF-GPIRV-RKQSKAAAREQALALLDRVGLKDRAN------HYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:TIGR00955 114 LTVREHLMFqAHLRMpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 164 TSALDPELRHEVLKVMRSLADEGMTMVIVTH----EIGFARDvasRLIFIDRGTIAEDGSPDMLL 224
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpssELFELFD---KIILMAEGRVAYLGSPDQAV 255
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
8.80e-31 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 113.82 E-value: 8.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREA- 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK--IMREAv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRvgLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIA-EDGSPDMLLNAS 227
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVlEDTGDALLANEA 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-235 |
1.26e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.20 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-P-HAsecdiRREAGMVF- 83
Cdd:COG1137 9 LVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPmHK-----RARLGIGYl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 -QQFHLFPHLTALENVMfGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:COG1137 84 pQEASIFRKLTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 163 PTSALDPELRHEVLKVMRSLADEGMTMVIVTHeigfarDVASRLIFIDR------GTIAEDGSPDMLLNassNPRLKEF 235
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDH------NVRETLGICDRayiiseGKVLAEGTPEEILN---NPLVRKV 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
2.35e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.00 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF--GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREA 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD--YSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFPHlTALENVMFGpirvrkqSKAAAREQALALLDRVGL------KDRANHYPSE----LSGGQQQRVAIAR 149
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLeklledDKGLNAWLGEggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIgFARDVASRLIFIDRGTIAEDGSPDMLLnaSSN 229
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELL--AQQ 564
|
250
....*....|
gi 505397517 230 PRLKEFLQHV 239
Cdd:PRK11160 565 GRYYQLKQRL 574
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
3.47e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.37 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSF-GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT--VTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLTAlENvmfgpIRVRKQS-------KAAAREQALALLDR--VGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:PRK13657 413 VVFQDAGLFNRSIE-DN-----IRVGRPDatdeemrAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLL 224
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELV 557
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-202 |
3.64e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.73 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHAsecdIRREAGMVFQQFHLF 89
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEI----YRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHlTALENVMFgPIRVRKQskAAAREQALALLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK10247 94 GD-TVYDNLIF-PWQIRNQ--QPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 505397517 169 PELRHEVLKVMRSLA-DEGMTMVIVTH---EIGFARDV 202
Cdd:PRK10247 170 ESNKHNVNEIIHRYVrEQNIAVLWVTHdkdEINHADKV 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-194 |
4.91e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.83 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCInkleaissgtllvAGMhitDPHASecdirreaGMVfqqfhlfpHLT 93
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------------AGL---WPYGS--------GRI--------ARP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGPIRVR-------------KQSKAAAREQALALLDRVGLK------DRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG4178 424 AGARVLFLPQRPYlplgtlreallypATAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSlADEGMTMVIVTH 194
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-220 |
5.44e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 5.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD--PHASEC-DIRREAGMVFQ--QFHLFPH 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVkRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 lTALENVMFGPIRVrKQSKAAAREQALALLDRVGL-KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:PRK13645 107 -TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505397517 171 LRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13645 185 GEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
6.12e-30 |
|
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: 109.71 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFG--TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhiTDPHASECDIRREA 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG---VPVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFphltalenvmfgpirvrkqskaaareqALALLDRVGLKdranhypseLSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03247 78 SVLNQRPYLF---------------------------DTTLRNNLGRR---------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEI-GFARdvASRLIFIDRGTIAEDG 218
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLtGIEH--MDKILFLENGKIIMQG 178
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-226 |
7.75e-30 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 116.76 E-value: 7.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFG-TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAG 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHlTALENVMFGpirvrkQSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIAR 149
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLG------AKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEgmTMVIVTHEIGFARDVaSRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDR 698
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-223 |
1.10e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.36 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTP---VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRRE 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ--YDHHYLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHlTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRAN----HYPSELSGGQQQRVAIARALAVK 154
Cdd:TIGR00958 557 VALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSladEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDML 223
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-231 |
1.53e-29 |
|
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: 115.62 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdpHASECDIRREAGMVFQQFHLFPH 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS--QWDREELGRHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 lTALENV-MFGPIRVRKQSKAAAREQA----LALLD----RVGlkdrANHYPseLSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:COG4618 421 -TIAENIaRFGDADPEKVVAAAKLAGVhemiLRLPDgydtRIG----EGGAR--LSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 163 PTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARdVASRLIFIDRGTIAEDGSPDMLLNASSNPR 231
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARLARPA 561
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-237 |
4.74e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.03 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKST----LLRCINkleaiSSGTLLVAGM--HITDPHASeCDIRREAGMVFQQFH-- 87
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplHNLNRRQL-LPVRHRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 LFPHLTALENVMFGpIRV-RKQSKAAAREQA-LALLDRVGLKDRANH-YPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK15134 375 LNPRLNVLQIIEEG-LRVhQPTLSAAQREQQvIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 165 SALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNPRLKEFLQ 237
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-196 |
9.12e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 9.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 9 KSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASecdIRreAGMVF--- 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA---IR--AGIAYvpe 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 --QQFHLFPHLTALENVM---------FGPIRVRKQSKAAAReqalaLLDRVGLKDRANHYP-SELSGGQQQRVAIARAL 151
Cdd:COG1129 335 drKGEGLVLDLSIRENITlasldrlsrGGLLDRRRERALAEE-----YIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWL 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEI 196
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSEL 454
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-219 |
1.24e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 112.57 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGM---HITDPHASECDIrr 77
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynKLDHKLAAQLGI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 eaGMVFQQFHLFPHLTALENVMFGPIRVRKQ------SKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARAL 151
Cdd:PRK09700 83 --GIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 152 AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVAsrlifiDRGTIAEDGS 219
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIC------DRYTVMKDGS 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
1.64e-28 |
|
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: 106.78 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEAISsGTLLVAGMhitdphasecdirreAG 80
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELEKLS-GSVSVPGS---------------IA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPhLTALENVMFG----PIRVRKQSKAAAREQALALLD-----RVGLKDRAnhypseLSGGQQQRVAIARAL 151
Cdd:cd03250 70 YVSQEPWIQN-GTIRENILFGkpfdEERYEKVIKACALEPDLEILPdgdltEIGEKGIN------LSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 152 AVKPKMMLFDEPTSALDPEL-RHEVLKVMRSLADEGMTMVIVTHEIGFARDvASRLIFIDRGT 213
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
3.66e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVA-GMHITdphasecdirrea 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIG------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 gmVFQQFH--LFPHLTALENvmfgpirVRKQSKAAAREQALALLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG0488 382 --YFDQHQeeLDPDKTVLDE-------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 157 MMLFDEPTSALDPELRhEVLKvmRSLAD-EGmTMVIVTHEIGFARDVASRLIFIDRGTIAE 216
Cdd:COG0488 453 VLLLDEPTNHLDIETL-EALE--EALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
3.73e-28 |
|
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: 105.21 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdiRREAGMVF-----QQFHLFP 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYvpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HLTALENVMFgpirvrkqskaaareqalalldrvglkdranhyPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:cd03215 92 DLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505397517 171 LRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-221 |
5.79e-28 |
|
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: 105.94 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphasECDIRrEAGMVFQQF 86
Cdd:TIGR03740 6 LSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-----RKDLH-KIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 87 HLFPHLTALENVmfgpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:TIGR03740 80 PLYENLTARENL-----KVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 167 LDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:TIGR03740 155 LDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-229 |
2.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHAseCDIRREAGMVFQQ-FHLFPHLTAL 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENV--WNLRRKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMFGpirvrKQSKAAAREQALALLDR----VGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK13642 101 DDVAFG-----MENQGIPREEMIKRVDEallaVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 172 RHEVLKVMRSLADE-GMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNASSN 229
Cdd:PRK13642 176 RQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-226 |
2.96e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 105.07 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 11 FGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdpHASECDIRREAGMVFQQFHLFP 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HLTALENVMFG-----PI--RVRKQSKAAAREQALAlldrVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:PRK10253 95 DITVQELVARGryphqPLftRWRKEDEEAVTKAMQA----TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 164 TSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-221 |
3.62e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.60 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG---MHITDPHASECDIRr 77
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPAKAHQLGIY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 78 eagMVFQQFHLFPHLTALENVMFGPIRvrkqsKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK15439 90 ---LVPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-225 |
4.10e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.21 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHASEcdiRREAGMVFQ 84
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARA---RRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMfGPIRVRKQSKAAARE-QALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:PRK10895 86 EASIFRRLSVYDNLM-AVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 164 TSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-213 |
5.36e-27 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 103.50 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFG------TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCInkleaissgtllvAGMHITDPHASECDI 75
Cdd:COG2401 25 ERVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------------AGALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 rreagmvfQQFHLFPHLTALENVmfgpirVRKQSKAaareQALALLDRVGLKDRANHY--PSELSGGQQQRVAIARALAV 153
Cdd:COG2401 92 --------PDNQFGREASLIDAI------GRKGDFK----DAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVA-SRLIFIDRGT 213
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGG 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-194 |
3.46e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.76 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASecdirREAG 80
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAA-----LAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 --MVFQQFHLFPHLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK11288 81 vaIIYQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-224 |
8.62e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 104.88 E-value: 8.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLV----AGMHITDPHASE-CDIRREAGMVFQQFHLFPHLTA 94
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrGRAKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMfGPIRVrKQSKAAAREQALALLDRVGLKDRA-----NHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:TIGR03269 383 LDNLT-EAIGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 170 ELRHEVLK-VMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLL 224
Cdd:TIGR03269 461 ITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-218 |
1.64e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.17 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 27 GEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECD-IRREAGMVFQQFH--LFPHLTALENVMfGPI 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQaLRRDIQFIFQDPYasLDPRQTVGDSIM-EPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 104 RVRK--QSKAAAREQALaLLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMR 180
Cdd:PRK10261 429 RVHGllPGKAAAARVAW-LLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190
....*....|....*....|....*....|....*....
gi 505397517 181 SLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:PRK10261 508 DLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-230 |
1.95e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 101.74 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKS----TLLRCINKLEAISSGTLLVAGMHITDPHASEcdiRR-----EAGMVFQQ--FHL 88
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE---RRnlvgaEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 89 FPHLTALENVMfGPIRVRKQ-SKAAAREQALALLDRVGLKD---RANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK11022 103 NPCYTVGFQIM-EAIKVHQGgNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 165 SALDPELRHEVLKVMRSLAD-EGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHP 248
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-197 |
2.52e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.34 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEA---ISSGTLLVAGMHITD-PHASECDIRREA-GMVFQQ- 85
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNlPEKELNKLRAEQiSMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 -FHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGL---KDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADEGMTMVI-VTHEIG 197
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLG 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-220 |
2.72e-25 |
|
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: 98.72 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHasecDIRREAGMVFQQFHLFPhl 92
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLH----DLRSRISIIPQDPVLFS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 talenvmfGPIRV----RKQSKAAAREQAlalLDRVGLKDRANHYP-----------SELSGGQQQRVAIARALAVKPKM 157
Cdd:cd03244 92 --------GTIRSnldpFGEYSDEELWQA---LERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSlADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSP 220
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-218 |
4.31e-25 |
|
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: 98.37 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmHITDPhasecdirREAGMVFQqfhlfPHLTAL 95
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL--------LGLGGGFN-----PELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMF-GPIRVRKQSKAAAREQalALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHE 174
Cdd:cd03220 103 ENIYLnGRLLGLSRKEIDEKID--EIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505397517 175 VLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-214 |
4.64e-25 |
|
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: 98.31 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGT---TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRRE 78
Cdd:cd03248 12 VKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHlTALENVMFGPIRVRKQSKAAAREQALA----LLDRVGLKDRANHYPSELSGGQQQRVAIARALAVK 154
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAhsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSlADEGMTMVIVTHEIGFARDvASRLIFIDRGTI 214
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-214 |
7.84e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 100.33 E-value: 7.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphaSECDI-----RREAGMVFQQFHLFPHLT 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD---AEKGIclppeKRRIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGpirVRKQSKAaareQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:PRK11144 93 VRGNLRYG---MAKSMVA----QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505397517 174 EVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:PRK11144 166 ELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-225 |
1.11e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 101.63 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGT--TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecDIRREA 79
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA--SLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GMVFQQFHLFpHLTALENVMF--GPIRVRKQSKAAAReQALAL-----LDRvGLKDRANHYPSELSGGQQQRVAIARALA 152
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYarTEQYSREQIEEAAR-MAYAMdfinkMDN-GLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIvTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-219 |
1.23e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 98.32 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASECDIRreagMVFQ--QFHLFPHlTA 94
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIR----MIFQdpSTSLNPR-QR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMFGPIRVRKQSKAAAREQAL-ALLDRVGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQIiETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505397517 173 HEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGS 219
Cdd:PRK15112 186 SQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-225 |
1.46e-24 |
|
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: 102.01 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhiTDPHASECDIRREAGMVFQQFHLFPHLTA 94
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHE 174
Cdd:TIGR01257 1021 AEHILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 175 VLKVM---RSladeGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:TIGR01257 1100 IWDLLlkyRS----GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-219 |
2.20e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 100.63 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRcinkleaissgtlLVAGMHitdPHAS----------E 72
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-------------VLSGVY---PHGSyegeilfdgeV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 73 C---DIR--REAGMVF--QQFHLFPHLTALENVMFGPIRVRKQ--SKAAAREQALALLDRVGLKDRANHYPSELSGGQQQ 143
Cdd:NF040905 67 CrfkDIRdsEALGIVIihQELALIPYLSIAENIFLGNERAKRGviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 144 RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVAsrlifiDRGTIAEDGS 219
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVA------DSITVLRDGR 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-238 |
3.59e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.30 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKSTLLrciNKLEAISS--GTLLVAGMHITDphASECDIRREAGMVFQQFHLFpHLTALEN 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPyqGSLKINGIELRE--LDPESWRKHLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 98 VMFGpirvrkqSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:PRK11174 443 VLLG-------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 167 LDpelRHEVLKVMRSL--ADEGMTMVIVTHEIGFARDVaSRLIFIDRGTIAEDGSPDMLlnASSNPRLKEFLQH 238
Cdd:PRK11174 516 LD---AHSEQLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL--SQAGGLFATLLAH 583
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-194 |
3.60e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.71 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHasecdirreagmVFQQFH------- 87
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD------------VAEACHylghrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 LFPHLTALENVMFGpirvrKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSAL 167
Cdd:PRK13539 84 MKPALTVAENLEFW-----AAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 505397517 168 DPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-226 |
8.01e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 99.34 E-value: 8.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHasecDIRREAGMVFQQFHLF 89
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRE----TFGKHIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHlTALENV-----MFGPIRVRKQSKAA-AREQALALldrvglkdrANHYPSE-------LSGGQQQRVAIARALAVKPK 156
Cdd:TIGR01842 405 PG-TVAENIarfgeNADPEKIIEAAKLAgVHELILRL---------PDGYDTVigpggatLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGfARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-226 |
9.00e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMVFQQFHLFPHLTAL 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMFG--PIR-VRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:PRK10575 104 ELVAIGryPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 173 HEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:PRK10575 184 VDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-239 |
1.32e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.77 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKS----TLLRCINKLEA-ISSGTLLVAGMH---ITDPHASECDIRREAG--- 80
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGlVQCDKMLLRRRSrqvIELSEQSAAQMRHVRGadm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 -MVFQQ--FHLFPHLTALENVMfGPIRVRKqskAAAREQALA----LLDRVGLKDRA---NHYPSELSGGQQQRVAIARA 150
Cdd:PRK10261 107 aMIFQEpmTSLNPVFTVGEQIA-ESIRLHQ---GASREEAMVeakrMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSN 229
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
250
....*....|
gi 505397517 230 PRLKEFLQHV 239
Cdd:PRK10261 263 PYTRALLAAV 272
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-230 |
1.47e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.51 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCInkLEAISSGTLLVAG-MHITD-------PHASECDIRREAGMVF 83
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNWHVTADrFRWNGidllklsPRERRKIIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 Q--QFHLFPHLTALENVMFG-PIRVRK----QSKAAAREQALALLDRVGLKDRA---NHYPSELSGGQQQRVAIARALAV 153
Cdd:COG4170 96 QepSSCLDPSAKIGDQLIEAiPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 154 KPKMMLFDEPTSALDPELRHEVLKVMRSLAD-EGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHP 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
1.91e-23 |
|
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: 91.74 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAgmhitdphasecdirreagm 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 vfqqfhlfphltalENVMFGpirvrkqskaaareqalalldrvglkdranhYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03221 61 --------------STVKIG-------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505397517 162 EPTSALDPELRhEVLKVMrsLADEGMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:cd03221 96 EPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-194 |
4.16e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.92 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL--------EAISSGTLLVAGmHITDphaSEcd 74
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQAS-NIRD---TE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 irrEAGMV--FQQFHLFPHLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARA 150
Cdd:PRK13549 81 ---RAGIAiiHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505397517 151 LAVKPKMMLFDEPTSAL-DPELRHeVLKVMRSLADEGMTMVIVTH 194
Cdd:PRK13549 158 LNKQARLLILDEPTASLtESETAV-LLDIIRDLKAHGIACIYISH 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-195 |
6.61e-23 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 96.87 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 5 SAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEAIS-SGTLLVAGMHITDPhasecdIRREAGMV 82
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKPTKQ------ILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 83 FQQFHLFPHLTALENVMFG-----PIRVRKQSKAAAREQALALLDRVGLKDR--ANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCsllrlPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-194 |
8.90e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.82 E-value: 8.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI--NKLEAISSGTLLVAGMHITDPHASEcdiRREAG--MVFQQFHLFP 90
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE---RARAGifLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HLTaleNVMF-----GPIRVRKQSKAAAREQALALLDRVGL-KDRANHYPSE-LSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:COG0396 91 GVS---VSNFlrtalNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190
....*....|....*....|....*....|..
gi 505397517 164 TSALDPE-LRHeVLKVMRSLADEGMTMVIVTH 194
Cdd:COG0396 168 DSGLDIDaLRI-VAEGVNKLRSPDRGILIITH 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-194 |
1.37e-22 |
|
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: 90.29 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLlvagmhitdphasecdirreagmvfqqfhlfpHLT 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------------------------GMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGPIRvrkqskaaareqalALLDRVGLKDRANhYP--SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:cd03223 62 EGEDLLFLPQR--------------PYLPLGTLREQLI-YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|...
gi 505397517 172 RHEVLKVMRslaDEGMTMVIVTH 194
Cdd:cd03223 127 EDRLYQLLK---ELGITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-218 |
1.37e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 95.46 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT--DPHASEcdirrE 78
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQ-----E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGM--VFQQFHLFPHLTALENVM--------FGPIRVRKQskaaaREQALALLDRVGLKDRANHYPSELSGGQQQRVAIA 148
Cdd:PRK10762 79 AGIgiIHQELNLIPQLTIAENIFlgrefvnrFGRIDWKKM-----YAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 149 RALAVKPKMMLFDEPTSAL-DPELRhEVLKVMRSLADEGMTMVIVTHEIgfardvasRLIF--IDRGTIAEDG 218
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRL--------KEIFeiCDDVTVFRDG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-224 |
3.12e-22 |
|
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: 90.28 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEA--ISSGTLLVAGMHITDPHASEcdiRREAGMvFQQFHLFPHLT 93
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEE---RARLGI-FLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFgpirvrkqskaaareqalalLDRVGLKdranhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:cd03217 91 GVKNADF--------------------LRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505397517 174 EVLKVMRSLADEGMTMVIVTH--EIgFARDVASRLIFIDRGTIAEDGSPDMLL 224
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHyqRL-LDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-231 |
4.31e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.46 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMhitDPHASECDIRREAGMVF-QQFHLFPHLTAL 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY---VPFKRRKEFARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 EN-VMFGPI-RVrkqSKAAAREQALALLDRVGLKD------RanhypsELSGGQQQRVAIARALAVKPKMMLFDEPTSAL 167
Cdd:COG4586 115 DSfRLLKAIyRI---PDAEYKKRLDELVELLDLGElldtpvR------QLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 168 DPELRHEVLKVMRSL-ADEGMTMVIVTHEIGfarDV---ASRLIFIDRGTIAEDGSPDMLLNASSNPR 231
Cdd:COG4586 186 DVVSKEAIREFLKEYnRERGTTILLTSHDMD---DIealCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
4.47e-22 |
|
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: 94.12 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKL--EAISSGTLLVAGMHITDPHASECDirrE 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTE---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVF--QQFHLFPHLTALENVMFG---PIRVRKQSKAAAREQALALLDRVGLKDRANHYP-SELSGGQQQRVAIARALA 152
Cdd:TIGR02633 78 AGIVIihQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRG 212
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-220 |
5.68e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGMVFQQFHLFPHLTA 94
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMFGPIR---VRKQSKAAAREQALALLDRVGLKdranHYPSE-LSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:PRK13638 95 IDSDIAFSLRnlgVPEAEITRRVDEALTLVDAQHFR----HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505397517 171 LRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP 220
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-191 |
6.18e-22 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 89.63 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 8 SKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEAISS--GTLLVAGMHItDPHASECdiRREAGMVFQ 84
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIPY-KEFAEKY--PGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTalenvmfgpirVRKQSKAAAREQAlalldrvglkdraNHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:cd03233 91 EDVHFPTLT-----------VRETLDFALRCKG-------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180
....*....|....*....|....*...
gi 505397517 165 SALDPELRHEVLKVMRSLADE-GMTMVI 191
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVlKTTTFV 174
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-218 |
6.25e-22 |
|
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: 90.47 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMhitDPHASECDIRREAGMVF-QQFHLFPHLT 93
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGPiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:cd03267 112 VIDSFYLLA-AIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505397517 174 EVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:cd03267 191 NIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-194 |
9.61e-22 |
|
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: 88.95 E-value: 9.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphasecdirREAGMVFQQFHLFPH 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA----------EQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 -------LTALENVMF-GPIRvrkqskAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:TIGR01189 81 lpglkpeLSALENLHFwAAIH------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 505397517 164 TSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-219 |
1.10e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 93.50 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 4 FSAVSKSfgTTPVLHDINLKIEAGEVVVIIGPSGSGKstllrcinkleaissgTLLVAGMHITDPHA--SECDIRREAGM 81
Cdd:PLN03232 622 FSWDSKT--SKPTLSDINLEIPVGSLVAIVGGTGEGK----------------TSLISAMLGELSHAetSSVVIRGSVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 VFQQFHLFpHLTALENVMFG----PIRVRKQSKAAAREQALALL---DRVGLKDRAnhypSELSGGQQQRVAIARALAVK 154
Cdd:PLN03232 684 VPQVSWIF-NATVRENILFGsdfeSERYWRAIDVTALQHDLDLLpgrDLTEIGERG----VNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVaSRLIFIDRGTIAEDGS 219
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-227 |
1.27e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.85 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 13 TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMVFQQFHLFPHL 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS--WRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 TAlENVMFG-PIRVRKQSKAAAR-----EQALALldrvglkdrANHYPSE-------LSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK10789 405 VA-NNIALGrPDATQQEIEHVARlasvhDDILRL---------PQGYDTEvgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 160 FDEPTSALDPELRHEVLKVMRSLAdEGMTMVIVTHEIGfARDVASRLIFIDRGTIAEDGSPDMLLNAS 227
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-206 |
2.50e-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: 87.93 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmhiTDPHASECDIRREAGMVFQQFHLFPHLTAL 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMFgpirVRKQSKAAAREQALALLDRVGLKDRANHYpseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEV 175
Cdd:cd03231 92 ENLRF----WHADHSDEQVEEALARVGLNGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 505397517 176 LKVMRSLADEGMTMVIVTH-EIGFARDVASRL 206
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-220 |
5.46e-21 |
|
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: 87.08 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdpHASECDIRREAGMVFQQFHLFPhlta 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--TIPLEDLRSSLTIIPQDPTLFS---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 lenvmfGPIRVRkqskaaareqalalLDRVGLKDRANHYP--------SELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:cd03369 96 ------GTIRSN--------------LDPFDEYSDEEIYGalrvseggLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505397517 167 LDPELRHEVLKVMRSLAdEGMTMVIVTHEIGFARDVAsRLIFIDRGTIAEDGSP 220
Cdd:cd03369 156 IDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-240 |
6.18e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.40 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD----------PHASECDIRreagmvfqqf 86
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknlvayvPQSEEVDWS---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 87 hlFPHLtaLENVM----FGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:PRK15056 93 --FPVL--VEDVVmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 163 PTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIdRGTIAEDGSPDMLLNASSNPR-LKEFLQHVS 240
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELaFSGVLRHVA 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-216 |
7.19e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDI-----------RREAGmvfqqfh 87
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAvkkgmayitesRRDNG------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 LFPHLTALENV-------------MFGPIRVRKQSKAAAREQALALLDRVGLkdraNHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK09700 352 FFPNFSIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLALKCHSV----NQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAE 216
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-221 |
7.92e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 7.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAiSSGTLLVAGMHITDPHASECdIRREAGMVFQQFHLFP----HLTAL 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAEL-ARHRAYLSQQQSPPFAmpvfQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 envmFGPirvrKQSKAAAREQALA-LLDRVGLKDRANHYPSELSGGQQQRVAIARA-LAVKP------KMMLFDEPTSAL 167
Cdd:COG4138 93 ----HQP----AGASSEAVEQLLAqLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPtinpegQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 168 DpeLRHEV--LKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:COG4138 165 D--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-225 |
7.97e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.95 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRC-INKLEAISSGTLLvagmhitdphasecdIRREAGMVFQQFHLFpHLT 93
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVV---------------IRGTVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFG----PIRVRKQSKAAAREQALALL---DRVGLKDRAnhypSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:PLN03130 695 VRDNILFGspfdPERYERAIDVTALQHDLDLLpggDLTEIGERG----VNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 167 LDPELRHEVLKvmRSLADE--GMTMVIVTHEIGFARDVaSRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PLN03130 771 LDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSN 828
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-214 |
1.23e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdiRREAGMVF-----QQFHLF 89
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHLTALENVMFGPIRVRKQSK------AAAREQALALLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:COG3845 349 PDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505397517 163 PTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI 214
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-216 |
1.15e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.33 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphASECDIRREAGMVFQQFHLFPHLTalenvm 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA--EQPEDYRKLFSAVFTDFHLFDQLL------ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 100 fGPirvrkQSKAAAREQALALLDRVGLKDRANHYPSE-----LSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR-- 172
Cdd:PRK10522 414 -GP-----EGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRre 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505397517 173 --HEVLKVMRslaDEGMTMVIVTHEIGFArDVASRLIFIDRGTIAE 216
Cdd:PRK10522 488 fyQVLLPLLQ---EMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-223 |
1.18e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 86.33 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSgkstllrcinkleAISSGTLLVagmHITDPHASE--------C 73
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA-------------A**RGALPA---HV*GPDAGRrpwrf*twC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 74 DIRREAGMVFQQFHLF-----PHLTALENV-MFGpiRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAI 147
Cdd:NF000106 78 ANRRALRRTIG*HRPVr*grrESFSGRENLyMIG--R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDML 223
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-230 |
1.71e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.37 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKStlLRCINKLEAISSGTLLVAGMHITDPHA-SECDIR-REAGMVFQQfhlfphl 92
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPvAPCALRgRKIATIMQN------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 talENVMFGPIR---------VRKQSKAAAREQALALLDRVGLKDRA---NHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK10418 88 ---PRSAFNPLHtmhtharetCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 161 DEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-212 |
4.88e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 85.39 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 10 SFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHIT-----DPHasecdiRREAGMVF- 83
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqDPP------RNVEGTVYd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 84 -------------QQFHLFPHLtalenVMFGPirVRKQSKAAAREQALalLDRVG---LKDRAN----------HYP-SE 136
Cdd:PRK11147 86 fvaegieeqaeylKRYHDISHL-----VETDP--SEKNLNELAKLQEQ--LDHHNlwqLENRINevlaqlgldpDAAlSS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 137 LSGGQQQRVAIARALAVKPKMMLFDEPTSALDP---ELRHEVLKVMRSladegmTMVIVTHEIGFARDVASRLIFIDRG 212
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIetiEWLEGFLKTFQG------SIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-212 |
5.43e-19 |
|
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: 85.37 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTT-PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSG-TLLVAGMHItdphasecdirreaGMVFQ 84
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGIKV--------------GYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMFGpirVRKQSKAAAREQAL------------ALLDRVG-LKDR------------------ANHY 133
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEG---VAEIKDALDRFNEIsakyaepdadfdKLAAEQAeLQEIidaadawdldsqleiamdALRC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 134 P------SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElrhEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLI 207
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWIL 229
|
....*
gi 505397517 208 FIDRG 212
Cdd:TIGR03719 230 ELDRG 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-226 |
6.54e-19 |
|
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: 85.38 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecDIRREAGMVFQQFHLFPhltal 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH--DLRFKITIIPQDPVLFS----- 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 envmfGPIRVRKQSKAAAREQ----ALALLDRVG----LKDRANHYPSE----LSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:TIGR00957 1374 -----GSLRMNLDPFSQYSDEevwwALELAHLKTfvsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 164 TSALDPELRHEVLKVMRSLADEgMTMVIVTHEIGFARDVaSRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-195 |
8.52e-19 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 81.14 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAIS--SGTLLVAGMHITDphasecDIRREAGMVFQQFHLF 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK------NFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHLTALENVMFgpirvrkqsKAAAReqalalldrvglkdranhypsELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:cd03232 92 PNLTVREALRF---------SALLR---------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*.
gi 505397517 170 ELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-168 |
9.51e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 9.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 18 HDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHItdphasecdirREAGMVFQQFHLF-------- 89
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----------RRQRDEYHQDLLYlghqpgik 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 90 PHLTALENVMFgpirVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK13538 87 TELTALENLRF----YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-168 |
2.64e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLlvagmhitdphasECDIRREAG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPHLT-ALENVMfgpiRVRKQSKaaaREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK09544 71 YVPQKLYLDTTLPlTVNRFL----RLRPGTK---KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
....*....
gi 505397517 160 FDEPTSALD 168
Cdd:PRK09544 144 LDEPTQGVD 152
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-223 |
3.28e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.03 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI--NKLEAISSGTLLVAG--------MHITDPHASECdirREAGMVFQQ 85
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVTGdvtlngepLAAIDAPRLAR---LRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPhLTALENVMFGPIRVRKQSKAAARE------QALALLDRVGLKDRAnhyPSELSGGQQQRVAIARALA------- 152
Cdd:PRK13547 93 QPAFA-FSAREIVLLGRYPHARRAGALTHRdgeiawQALALAGATALVGRD---VTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505397517 153 --VKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSP-DML 223
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPaDVL 243
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-214 |
8.52e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 81.60 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 10 SFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRcinkleaissgtlLVAGMHitdPHA--------------SEC-- 73
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS-------------LITGDH---PQGysndltlfgrrrgsGETiw 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 74 DIRREAGMVFQQFHL-FPHLTALENVM----FGPIRVRKQSKAAAREQALALLDRVGLKDR-ANHYPSELSGGQQQRVAI 147
Cdd:PRK10938 333 DIKKHIGYVSSSLHLdYRVSTSVRNVIlsgfFDSIGIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505397517 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVI-VTHEigfARD----VASRLIFIDRGTI 214
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHH---AEDapacITHRLEFVPDGDI 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-198 |
1.06e-17 |
|
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: 78.91 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGMVF-QQFHLFPHLT 93
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYaAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFG-PI---RVRKQSKAAAREQALALL---DRVGLKDRAnhypSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:cd03290 95 VEENITFGsPFnkqRYKAVTDACSLQPDIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190
....*....|....*....|....*....|....
gi 505397517 167 LDPELRHEVLK--VMRSLADEGMTMVIVTHEIGF 198
Cdd:cd03290 171 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-196 |
1.07e-17 |
|
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: 81.37 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 25 EAGEVVVIIGPSGSGKSTLLRcinkleaISSGTL---LvaGMHITDPHASECdIRREAGMVfqqfhLFPHLTALENvmfG 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-------ILSGELkpnL--GDYDEEPSWDEV-LKRFRGTE-----LQDYFKKLAN---G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 102 PIRV----------RKQ---------SKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:COG1245 159 EIKVahkpqyvdliPKVfkgtvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....
gi 505397517 163 PTSALDPELRHEVLKVMRSLADEGMTMVIVTHEI 196
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-217 |
2.04e-17 |
|
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: 80.61 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphasecDIRREA-----GMVFQQFHLFPHLTA 94
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-------ADNREAyrqlfSAVFSDFHLFDRLLG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENvmfgpirvrkqskAAAREQALALLDRVGLKDR---ANHYPS--ELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:COG4615 424 LDG-------------EADPARARELLERLELDHKvsvEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505397517 170 ELR----HEVLKVMRSladEGMTMVIVTHEIGFArDVASRLIFIDRGTIAED 217
Cdd:COG4615 491 EFRrvfyTELLPELKA---RGKTVIAISHDDRYF-DLADRVLKMDYGKLVEL 538
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-236 |
3.67e-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: 80.37 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLrcinkleaissgTLLVAGMHITDPHASecdIRREAGMVFQQFHLfPH 91
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL------------SALLAEMDKVEGHVH---MKGSVAYVPQQAWI-QN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFG----PIRVRKQSKAAAREQALALL---DRVGLKDRAnhypSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:TIGR00957 713 DSLRENILFGkalnEKYYQQVLEACALLPDLEILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 165 SALDPEL-RHEVLKVmrsLADEGM----TMVIVTHEIGFARDVaSRLIFIDRGTIAEDGSPDMLLnaSSNPRLKEFL 236
Cdd:TIGR00957 789 SAVDAHVgKHIFEHV---IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL--QRDGAFAEFL 859
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-196 |
1.33e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 78.23 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 5 SAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHItDPHASECDIRREAGMVFQ 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMFG--PIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 505397517 163 PTSAL-DPELRHeVLKVMRSLADEGMTMVIVTHEI 196
Cdd:PRK10982 161 PTSSLtEKEVNH-LFTIIRKLKERGCGIVYISHKM 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-212 |
2.07e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.23 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 27 GEVVVIIGPSGSGKSTLLRCINK---LEAISSGTLLVAGmhitdpHASECDIRREAGMVFQQ-FHLfPHLTALENVMFG- 101
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNG------RPLDSSFQRSIGYVQQQdLHL-PTSTVRESLRFSa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 102 ----PIRVRKQSKAAAREQALALLDRVGLKDRANHYPSE-LSGGQQQRVAIARALAVKPKMMLF-DEPTSALDPELRHEV 175
Cdd:TIGR00956 862 ylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSI 941
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505397517 176 LKVMRSLADEGMTMVIVTHE---IGFARdvASRLIFIDRG 212
Cdd:TIGR00956 942 CKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKG 979
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
5.64e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGttpvlhDINLKIEAG-----EVVVIIGPSGSGKSTLLRcinkleaissgtlLVAGmhITDPHASECD- 74
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVEGGeiyegEVIGIVGPNGIGKTTFAK-------------LLAG--VLKPDEGEVDp 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 ----------IRREAGMVFQQFhLFPHLTALENVMFGPirvrkqskaaareqalALLDRVGLKDRANHYPSELSGGQQQR 144
Cdd:PRK13409 399 elkisykpqyIKPDYDGTVEDL-LRSITDDLGSSYYKS----------------EIIKPLQLERLLDKNVKDLSGGELQR 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLI 207
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-194 |
1.53e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.52 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 10 SFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEA--ISSGTLLVAGMHITDphaSECDIRREAGmVFQQFH 87
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILD---LEPEERAHLG-IFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 LFPHLTALENVMFgpIRVRKQSKAAAREQ----ALAL-------LDRVGLKDR-ANHYPSE-LSGGQQQRVAIARALAVK 154
Cdd:CHL00131 92 YPIEIPGVSNADF--LRLAYNSKRKFQGLpeldPLEFleiinekLKLVGMDPSfLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505397517 155 PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-239 |
1.65e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.21 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAG-----EVVVIIGPSGSGKSTLLRcinkleaissgtlLVAGMhitdphasecdIRREAGMVfqqfhlfphLT 93
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIK-------------MLAGV-----------LKPDEGDI---------EI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFGPIRVRKQSKAAAREQALALLDRVGlkdRANHYPSE-----------------LSGGQQQRVAIARALAVKPK 156
Cdd:cd03237 59 ELDTVSYKPQYIKADYEGTVRDLLSSITKDFY---THPYFKTEiakplqieqildrevpeLSGGELQRVAIAACLSKDAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 157 MMLFDEPTSALDPELRHEVLKVMRSLADEG-MTMVIVTHEIGFARDVASRLIFIDrGTIAEDG--SPDMLLNASSNprlk 233
Cdd:cd03237 136 IYLLDEPSAYLDVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGvaNPPQSLRSGMN---- 210
|
....*.
gi 505397517 234 EFLQHV 239
Cdd:cd03237 211 RFLKNL 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-169 |
2.22e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECDIRREAGM 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 vfQQ---FHLFPHLTALENV-MFGpiRVRKQSKAAAREQALALLDRVGL---KDRanhyPS-ELSGGQQQRVAIARALAV 153
Cdd:NF033858 82 --PQglgKNLYPTLSVFENLdFFG--RLFGQDAAERRRRIDELLRATGLapfADR----PAgKLSGGMKQKLGLCCALIH 153
|
170
....*....|....*.
gi 505397517 154 KPKMMLFDEPTSALDP 169
Cdd:NF033858 154 DPDLLILDEPTTGVDP 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-226 |
2.59e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 18 HDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPHASecdIRreAGMVF-----QQFHLFP 90
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA---IR--AGIMLcpedrKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 HLTALENV---------MFGPIRVRKQSKAAAREQalalLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11288 345 VHSVADNInisarrhhlRAGCLINNRWEAENADRF----IRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIA-----EDGSPDMLLNA 226
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALSL 491
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-230 |
3.46e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.30 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 20 INLKIEAGEVVVIIGPSGSGKSTLLRCINkleAISSGTLLVAG--MHITD-------PHASECDIRREAGMVFQ--QFHL 88
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIC---GVTKDNWRVTAdrMRFDDidllrlsPRERRKLVGHNVSMIFQepQSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 89 FPHLTALENVMFG-PIRVRK----QSKAAAREQALALLDRVGLKDRAN---HYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK15093 103 DPSERVGRQLMQNiPGWTYKgrwwQRFGWRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 161 DEPTSALDPELRHEVLKVMRSL-ADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLNASSNP 230
Cdd:PRK15093 183 DEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHP 253
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-221 |
3.52e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 24 IEAGEVVVIIGPSGSGKSTLLRCINKLEAiSSGTLLVAGMHITDPHASECDIRReAGMVFQQ-----FHLFPHLTalenv 98
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR-AYLSQQQtppfaMPVFQYLT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 99 MFGPIRVRKQSKAAAREQalaLLDRVGLKDRANHYPSELSGGQQQRVAIARA-LAVKP------KMMLFDEPTSALDPEL 171
Cdd:PRK03695 92 LHQPDKTRTEAVASALNE---VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPD 221
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-196 |
3.80e-15 |
|
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: 72.40 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 27 GEVVVIIGPSGSGKSTLLRcinkleaISSGTLLVA-GMHITDPHASECdIRREAGMVFQQFhlfphLTALENVMFGPIR- 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALK-------ILAGKLKPNlGKFDDPPDWDEI-LDEFRGSELQNY-----FTKLLEGDVKVIVk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 105 ------VRKQSKAAARE---------QALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:cd03236 93 pqyvdlIPKAVKGKVGEllkkkdergKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 505397517 170 ELRHEVLKVMRSLADEGMTMVIVTHEI 196
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-207 |
5.43e-15 |
|
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: 73.67 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGttpvlhDINLKIEAG-----EVVVIIGPSGSGKSTLLRcinkleaissgtlLVAGmhITDPHASECD-- 74
Cdd:COG1245 342 VEYPDLTKSYG------GFSLEVEGGeiregEVLGIVGPNGIGKTTFAK-------------ILAG--VLKPDEGEVDed 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 ---------IRREAGMVFQQFhlfphltaLENVMFGPIrvrkQSKAAAREqalaLLDRVGLKDRANHYPSELSGGQQQRV 145
Cdd:COG1245 401 lkisykpqyISPDYDGTVEEF--------LRSANTDDF----GSSYYKTE----IIKPLGLEKLLDKNVKDLSGGELQRV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADE-GMTMVIVTHEIGFARDVASRLI 207
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-212 |
5.75e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTT-PVLHDINL------KIeaGevvvIIGPSGSGKSTLLRCINKLEAISSG-TLLVAGMHItdphasecdirre 78
Cdd:PRK11819 12 VSKVVPPKkQILKDISLsffpgaKI--G----VLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKV------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 aGMVFQQFHLFPHLTALENVMFGpirVRKQSKAAAREQAL------------ALLDRVG-LKDRANHY------------ 133
Cdd:PRK11819 73 -GYLPQEPQLDPEKTVRENVEEG---VAEVKAALDRFNEIyaayaepdadfdALAAEQGeLQEIIDAAdawdldsqleia 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 134 ------P------SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElrhEVLKVMRSLADEGMTMVIVTHEIGFARD 201
Cdd:PRK11819 149 mdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDN 225
|
250
....*....|.
gi 505397517 202 VASRLIFIDRG 212
Cdd:PRK11819 226 VAGWILELDRG 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-170 |
1.48e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 5 SAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLlvagmHITDPHASECDIRREAGMVFQ 84
Cdd:PRK13543 15 HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 85 QFHLFPHLTALENVMF-GPIRVRKQSKAAAreQALALldrVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:PRK13543 90 LPGLKADLSTLENLHFlCGLHGRRAKQMPG--SALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*..
gi 505397517 164 TSALDPE 170
Cdd:PRK13543 165 YANLDLE 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-194 |
1.49e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 27 GEVVVIIGPSGSGKSTLLRcinkleaISSGTL---LvaGMHITDPHASECdIRREAGMVFQQFhlfphltaLENVMFGPI 103
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVK-------ILSGELipnL--GDYEEEPSWDEV-LKRFRGTELQNY--------FKKLYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 104 RV----------RKQSKAAARE---------QALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK13409 161 KVvhkpqyvdliPKVFKGKVREllkkvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|
gi 505397517 165 SALDPELRHEVLKVMRSLAdEGMTMVIVTH 194
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELA-EGKYVLVVEH 269
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-226 |
4.68e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSfgTTPVLHDINLKIEAGEVVVIIGPSGSGKSTL-------------------------------------- 43
Cdd:PTZ00265 1171 VNFRYISRP--NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmtneqdyqgdeeq 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 44 ---LRCINKLEAI-------------SSGTLLVAGMHITDPHASecDIRREAGMVFQQFHLFpHLTALENVMFGPIR--- 104
Cdd:PTZ00265 1249 nvgMKNVNEFSLTkeggsgedstvfkNSGKILLDGVDICDYNLK--DLRNLFSIVSQEPMLF-NMSIYENIKFGKEDatr 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 105 --VRKQSKAAAREQALALLDRvGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSL 182
Cdd:PTZ00265 1326 edVKRACKFAAIDEFIESLPN-KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 505397517 183 ADEG-MTMVIVTHEIGFARDVASRLIF--IDR-GTIAE-DGSPDMLLNA 226
Cdd:PTZ00265 1405 KDKAdKTIITIAHRIASIKRSDKIVVFnnPDRtGSFVQaHGTHEELLSV 1453
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-213 |
5.47e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.20 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 13 TTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphASECDIRREAGMVfQQFHLFPHL 92
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYC-PQFDAIDDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 TALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:TIGR01257 2027 LTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505397517 173 HEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-225 |
7.50e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASecDIRREAGMVFQQFHLFPh 91
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT--DLRRVLSIIPQSPVLFS- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 ltalenvmfGPIRVRKQSKAAAREQAL-ALLDRVGLKDRANHYP-----------SELSGGQQQRVAIARALAVKPKMML 159
Cdd:PLN03232 1324 ---------GTVRFNIDPFSEHNDADLwEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 160 FDEPTSALDpeLRHEVLkVMRSLADE--GMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLN 225
Cdd:PLN03232 1395 LDEATASVD--VRTDSL-IQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-226 |
1.47e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHI-TDPHASecdIRREAGMVfQQFHLFPHLT 93
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsSLSHSV---LRQGVAMV-QQDPVVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFG-PIRVRKQSKAAAREQaLALLDRV---GLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:PRK10790 431 FLANVTLGrDISEEQVWQALETVQ-LAELARSlpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505397517 170 ELRHEVLKVMRsLADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA 226
Cdd:PRK10790 510 GTEQAIQQALA-AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-168 |
2.81e-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: 68.78 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCInkleaissgtllvagMHITDPhaSECDIRREAGMVFQ-QFHLFPHL 92
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI---------------MGELEP--SEGKIKHSGRISFSpQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 93 TALENVMFG----PIRVRKQSKAAAREQALALL---DRVGLKDRAnhypSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:TIGR01271 502 TIKDNIIFGlsydEYRYTSVIKACQLEEDIALFpekDKTVLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 505397517 166 ALD 168
Cdd:TIGR01271 578 HLD 580
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-217 |
3.45e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEAISSGTLLVAGmHITDPHASECDIRREAGMV---FQQFHLFPHLTA 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFING-KPVDIRNPAQAIRAGIAMVpedRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMFGPIR---VRKQSKAAAREQAL-ALLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:TIGR02633 357 GKNITLSVLKsfcFKMRIDAAAELQIIgSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505397517 170 ELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAED 217
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-196 |
5.11e-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: 66.80 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEaissgtllvagmhitdphASECDIRREAGMVF-QQFHLFPH 91
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELE------------------PSEGKIKHSGRISFsSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFG----PIRVRKQSKAAAREQalallDRVGLKDRANHYPSE----LSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:cd03291 112 GTIKENIIFGvsydEYRYKSVVKACQLEE-----DITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190
....*....|....*....|....*....|....*
gi 505397517 164 TSALDPELRHEVLK--VMRSLADEgmTMVIVTHEI 196
Cdd:cd03291 187 FGYLDVFTEKEIFEscVCKLMANK--TRILVTSKM 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-200 |
5.63e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGT---TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLvagmhITDPHASEcDI--- 75
Cdd:PTZ00265 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-----INDSHNLK-DInlk 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 --RREAGMVFQQFHLFPH---------------LTALENVM----------------------------------FGPIR 104
Cdd:PTZ00265 457 wwRSKIGVVSQDPLLFSNsiknnikyslyslkdLEALSNYYnedgndsqenknkrnscrakcagdlndmsnttdsNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 105 VRKQSKAAAREQALALLDRVGLKDRANHYP-----------SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:PTZ00265 537 MRKNYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|....*...
gi 505397517 174 EVLKVMRSL-ADEGMTMVIVTHEIGFAR 200
Cdd:PTZ00265 617 LVQKTINNLkGNENRITIIIAHRLSTIR 644
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-191 |
6.17e-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: 67.65 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVaGMHItdpHASECDIRREAgm 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---KLAYVDQSRDA-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 vfqqfhLFPHLTALENVMFGP--IRVRKqskaaaRE-QALALLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKM 157
Cdd:TIGR03719 397 ------LDPNKTVWEEISGGLdiIKLGK------REiPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 505397517 158 MLFDEPTSALDPElrhevlkVMRSLADE-----GMTMVI 191
Cdd:TIGR03719 465 LLLDEPTNDLDVE-------TLRALEEAllnfaGCAVVI 496
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-196 |
6.68e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.88 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAgmhitdphasecdirREAGMVFQQFHLFpHLTAL 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------------RSIAYVPQQAWIM-NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMF----GPIRVRKQSKAAAREQALALLDRvGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PTZ00243 739 GNILFfdeeDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180
....*....|....*....|....*
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEI 196
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQV 842
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-194 |
7.03e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 8 SKSFGT-TPVLHdINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGmHITDPHasECDIRREAGMVFQQF 86
Cdd:NF033858 273 TMRFGDfTAVDH-VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVDAG--DIATRRRVGYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 87 HLFPHLTALENVM-----FG-PirvrkQSKAAAREQALalLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:NF033858 349 SLYGELTVRQNLElharlFHlP-----AAEIAARVAEM--LERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190
....*....|....*....|....*....|....*
gi 505397517 161 DEPTSALDPELRHEVLKVMRSLA-DEGMTMVIVTH 194
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTH 456
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-194 |
2.40e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.93 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLlvagmhiTDPhaSECDIrreagmvfqqFHL--FPHLT 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-------TKP--AKGKL----------FYVpqRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 --ALENVMFGPIRVRKQSKAAAREQAL-ALLDRVGLK---------DRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:TIGR00954 528 lgTLRDQIIYPDSSEDMKRRGLSDKDLeQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|...
gi 505397517 162 EPTSALDPELRHevlKVMRSLADEGMTMVIVTH 194
Cdd:TIGR00954 608 ECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-240 |
3.32e-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: 64.49 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 12 GTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAIsSGTLLVAGMHITDPHASECdiRREAGMVFQQFHLFPh 91
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKW--RKAFGVIPQKVFIFS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 ltalenvmfGPIRVRKQSKAA-AREQALALLDRVGLKDRANHYPSE-----------LSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03289 91 ---------GTFRKNLDPYGKwSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 160 FDEPTSALDPeLRHEVLKVMRSLADEGMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLLNA--------SSNPR 231
Cdd:cd03289 162 LDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEkshfkqaiSPSDR 239
|
....*....
gi 505397517 232 LKEFLQHVS 240
Cdd:cd03289 240 LKLFPRRNS 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-228 |
3.60e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.57 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEcdIRREAGMVFQQFHLFPHlTAL 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE--LRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVmfGPIRvrkqskAAAREQALALLDRVGLKDRAnhyPSELSG--------------GQQQRVAIARALAVK-PKMMLF 160
Cdd:PTZ00243 1402 QNV--DPFL------EASSAEVWAALELVGLRERV---ASESEGidsrvleggsnysvGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 161 DEPTSALDPELRHEVLKVMRSlADEGMTMVIVTHEIgfaRDVAS--RLIFIDRGTIAEDGSP-DMLLNASS 228
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAQydKIIVMDHGAVAEMGSPrELVMNRQS 1537
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-224 |
6.46e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdpHASECDIRREAGMVFQQFHLFPhlta 94
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVLGIIPQAPVLFS---- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 lenvmfGPIRVR-----KQSKAAAREQalalLDRVGLKDRANHYPSEL-----------SGGQQQRVAIARALAVKPKMM 158
Cdd:PLN03130 1327 ------GTVRFNldpfnEHNDADLWES----LERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505397517 159 LFDEPTSALDpeLRHEVLkVMRSLADE--GMTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLL 224
Cdd:PLN03130 1397 VLDEATAAVD--VRTDAL-IQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-209 |
9.74e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.14 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRC-INKLEAiSSGTLLVA-----GMHITDpHASEcdi 75
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELEP-DSGTVKWSenaniGYYAQD-HAYD--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 76 rreagmvfqqfhlFPHLTALENVMfgpirvRKQSKAAAREQAL-ALLDRVGL-KDRANHYPSELSGGQQQRVAIARALAV 153
Cdd:PRK15064 395 -------------FENDLTLFDWM------SQWRQEGDDEQAVrGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 154 KPKMMLFDEPTSALDPElrhevlkVMRSLAD-----EGmTMVIVTHEIGFARDVASRLIFI 209
Cdd:PRK15064 456 KPNVLVMDEPTNHMDME-------SIESLNMalekyEG-TLIFVSHDREFVSSLATRIIEI 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-226 |
1.44e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAG--MHITDPH---------ASEcDIRREA---G 80
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQdglangivyISE-DRKRDGlvlG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHlfpHLTALENVMFGPIRVRKQSKAAAREQALALLD--------RVGLkdranhypseLSGGQQQRVAIARALA 152
Cdd:PRK10762 345 MSVKENM---SLTALRYFSRAGGSLKHADEQQAVSDFIRLFNiktpsmeqAIGL----------LSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 153 VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTI-----AEDGSPDMLLNA 226
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMAA 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-215 |
4.28e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 19 DINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITdphASECDIRREAGMVF-----QQFHLFPHLT 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEIN---ALSTAQRLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENV---MFG--PIRVRKQSKAAAREQALALLdrvGLK-DRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSAL 167
Cdd:PRK15439 358 LAWNVcalTHNrrGFWIKPARENAVLERYRRAL---NIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505397517 168 DPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIA 215
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-195 |
6.95e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI--NKLEAISSGTLLVAGMhitdPHASECdIRREAGMVFQQFHLFPHLT 93
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGF----PKKQET-FARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALENVMFG-----PIRVRKQSKAAAREQALALLDRVGLKDRANHYP--SELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:PLN03140 970 VRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*....
gi 505397517 167 LDPELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-213 |
8.82e-11 |
|
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: 58.87 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLrcinkleaissgtllvagmhitdphaSECDIRREAGMVFQQFHLFPHLTAle 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--------------------------NEGLYASGKARLISFLPKFSRNKL-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 97 nvmfgpIRVRKqskaaareqaLALLDRVGLKD-RANHYPSELSGGQQQRVAIARALAVKPK--MMLFDEPTSALDPELRH 173
Cdd:cd03238 63 ------IFIDQ----------LQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505397517 174 EVLKVMRSLADEGMTMVIVTHEIGFArDVASRLIFIDRGT 213
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFGPGS 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-217 |
1.02e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEAISSGTLLVAGMHITDPHASECdIRREAGMVFQ---QFHLFPH 91
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQA-IAQGIAMVPEdrkRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 92 LTALENVMFGPI-RVRKQS---KAAAREQALALLDRVGLKDRANHYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:PRK13549 356 MGVGKNITLAALdRFTGGSridDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505397517 167 LDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAED 217
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-238 |
1.03e-10 |
|
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: 61.08 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLeAISSGTLLVAGmhITDPHASECDIRREAGMVFQQFHLFPhltal 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFS----- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 envmfGPIRVRKQSKAAAREQAL-ALLDRVGLKDRANHYPSEL-----------SGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:TIGR01271 1306 -----GTFRKNLDPYEQWSDEEIwKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 164 TSALDPeLRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIfIDRGTIAEDGSPDMLLNASS--------NPRLKEF 235
Cdd:TIGR01271 1381 SAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLV-IEGSSVKQYDSIQKLLNETSlfkqamsaADRLKLF 1458
|
...
gi 505397517 236 LQH 238
Cdd:TIGR01271 1459 PLH 1461
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.06e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLE--AISSGTLLVAGMHITDPHASEcdirRE 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED----RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 79 AGMVFQQFHLFPHLTALENVMFGPIRVRKQSKaaAREQalALLDRVGLKD------RANHYPSEL---------SGGQQQ 143
Cdd:PRK09580 77 GEGIFMAFQYPVEIPGVSNQFFLQTALNAVRS--YRGQ--EPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505397517 144 RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-192 |
1.39e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 14 TPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRcinkleAISSGTLLVAGMHitdphasECDIRREAGMVFQQFHlfpHLT 93
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALAR------ALAGELPLLSGER-------QSQFSHITRLSFEQLQ---KLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 ALE-----NVMFGPIR----------VRKQSKAAAREQALALLDRVG-LKDRANHYpseLSGGQQQRVAIARALAVKPKM 157
Cdd:PRK10938 80 SDEwqrnnTDMLSPGEddtgrttaeiIQDEVKDPARCEQLAQQFGITaLLDRRFKY---LSTGETRKTLLCQALMSEPDL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 505397517 158 MLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIV 192
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-218 |
1.53e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.29 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLlrcinkleaissgTLLVAGmhITDPHASECDIRREAGMVFQQFHLFPHLTALE 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTL-------------SNLIAG--VTMPNKGTVDIKGSAALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 97 NV-----MFGpirvrkQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK13545 105 NIelkglMMG------LTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505397517 172 RHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDG 218
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-208 |
2.03e-10 |
|
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: 57.38 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 27 GEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMhitdphasecdirreagmvfqqfhlfphltalenvmfgpirvr 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 107 kqskaaarEQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEG 186
Cdd:smart00382 39 --------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170 180
....*....|....*....|....*...
gi 505397517 187 M------TMVIVTHEIGFARDVASRLIF 208
Cdd:smart00382 111 LkseknlTVILTTNDEKDLGPALLRRRF 138
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-193 |
2.45e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRcinkleAISSGT---LLVAGMHIT-DPHASECDIRREAGMVF----QQFH 87
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLK------TIASNTdgfHIGVEGVITyDGITPEEIKKHYRGDVVynaeTDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 88 lFPHLTALENVMF-----GP-IRVRKQSKAAAREQALALLDRV-GL---KDR--ANHYPSELSGGQQQRVAIARALAVKP 155
Cdd:TIGR00956 150 -FPHLTVGETLDFaarckTPqNRPDGVSREEYAKHIADVYMATyGLshtRNTkvGNDFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 505397517 156 KMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVT 193
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-215 |
5.53e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASEC---------DIRREAGMVFQQ 85
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvtEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 FHLFPHLTALENVMFGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSeLSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:PRK10982 342 DIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505397517 166 ALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIA 215
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
2-207 |
6.00e-10 |
|
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: 56.81 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINlKIEAGEVVVIIGPSGSGKSTLLRcinkleaissgtlLVAGMHITDPHASECDIRReagm 81
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVK-------------ILAGQLIPNGDNDEWDGIT---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 82 vfqqfhlfphltalenVMFGPIRVrkqskaaareqalalldrvglkdranhypsELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03222 63 ----------------PVYKPQYI------------------------------DLSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505397517 162 EPTSALDPELRHEVLKVMRSLADEGM-TMVIVTHEIGFARDVASRLI 207
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-195 |
1.06e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDphaSECDIRREAGMVFQQFHLFPHLTA 94
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK---DLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 95 LENVMFGpirVRKQSKAAAREQALALLDRVGLKDranhYPSEL-SGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:PRK13540 92 RENCLYD---IHFSPGAVGITELCRLFSLEHLID----YPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 505397517 174 EVLKVMRSLADEGMTMVIVTHE 195
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-191 |
4.54e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 2 VEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVaG--MHItdphaSECDIRREA 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetVKL-----AYVDQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 gmvfqqfhLFPHLTALENVMFGP--IRVRKQ---SKA-AAR------EQAlallDRVGlkdranhypsELSGGQQQRVAI 147
Cdd:PRK11819 399 --------LDPNKTVWEEISGGLdiIKVGNReipSRAyVGRfnfkggDQQ----KKVG----------VLSGGERNRLHL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505397517 148 ARALAVKPKMMLFDEPTSALDPElrhevlkVMRSLADE-----GMTMVI 191
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVE-------TLRALEEAllefpGCAVVI 498
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-237 |
7.73e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLlvagmhitDPHASECDIRREAGMVFQqfhlfphLTALE 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--------DRNGEVSVIAISAGLSGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 97 NVMFGPIRV---RKQSKAAAREqalaLLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRH 173
Cdd:PRK13546 105 NIEFKMLCMgfkRKEIKAMTPK----IIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 174 EVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGTIAEDGSPDMLLnassnPRLKEFLQ 237
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLN 239
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-194 |
8.71e-09 |
|
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: 53.13 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 26 AGEVVVIIGPSGSGKSTLLRCInkleaissgtLLVAGMHitdphasecdirreagmvfqqfhlFPHLTALENVMFGPIRv 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI----------GLALGGA------------------------QSATRRRSGVKAGCIV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 106 rkqskaAAREQALALLDrvglkdranhypSELSGGQQQRVAIARALA---VKPK-MMLFDEPTSALDPELRHEVLKVMRS 181
Cdd:cd03227 65 ------AAVSAELIFTR------------LQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILE 126
|
170
....*....|...
gi 505397517 182 LADEGMTMVIVTH 194
Cdd:cd03227 127 HLVKGAQVIVITH 139
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
81-229 |
1.35e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.83 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLF-----PHLTALENVMFGpirvrkqskaaaREQALALLDRVGLK----DRAnhyPSELSGGQQQRVAIARAL 151
Cdd:PRK00635 427 MSLQELFIFlsqlpSKSLSIEEVLQG------------LKSRLSILIDLGLPyltpERA---LATLSGGEQERTALAKHL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 152 AVKPK--MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHE---IGFAR---DVASRL-IFidRGTIAEDGSPDM 222
Cdd:PRK00635 492 GAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADriiDIGPGAgIF--GGEVLFNGSPRE 569
|
....*..
gi 505397517 223 LLNASSN 229
Cdd:PRK00635 570 FLAKSDS 576
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-224 |
2.36e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.99 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 15 PVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITD-PHASecdIRREAGMVFQQFHLFPhlt 93
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHT---LRSRLSIILQDPILFS--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 94 alenvmfGPIRVRKQSKAAAREQAL-ALLDRVGLKDRANHYPSEL-----------SGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03288 109 -------GSIRFNLDPECKCTDDRLwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 162 EPTSALDPELRHEVLK-VMRSLADEgmTMVIVTHEIGFARDvASRLIFIDRGTIAEDGSPDMLL 224
Cdd:cd03288 182 EATASIDMATENILQKvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-195 |
4.40e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.87 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTL----------LRCINKLEAISSGTL---------LVAGMHIT---DPHASECD 74
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLgqmdkpdvdSIEGLSPAiaiDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 75 IRREAGMVFQQFHLFPHLTALEnvmfgPIRVRkqskaaareqaLALLDRVGLK----DRANhypSELSGGQQQRVAIARA 150
Cdd:cd03270 91 PRSTVGTVTEIYDYLRLLFARV-----GIRER-----------LGFLVDVGLGyltlSRSA---PTLSGGEAQRIRLATQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505397517 151 LAVKPKMML--FDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-194 |
4.86e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 16 VLHDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLVAGMHITDPHASECdirreaGMVFQQFHLFPHLTAL 95
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC------TYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 96 ENVMFgpirvrkQSKA-AAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHE 174
Cdd:PRK13541 89 ENLKF-------WSEIyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 505397517 175 VLKVMRSLADEGMTMVIVTH 194
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSH 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-211 |
1.11e-07 |
|
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: 50.68 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 29 VVVIIGPSGSGKSTLLRCINkleAISSGTL---LVAGMHITDPhASECDIRREAGMVFQ-----QFHLFPHLTALENVMF 100
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK---YALTGELppnSKGGAHDPKL-IREGEVRAQVKLAFEnangkKYTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 101 GPirvrkqskaaaREQALALLDRvgLKDRanhypseLSGGQQQ------RVAIARALAVKPKMMLFDEPTSALDPE-LRH 173
Cdd:cd03240 100 CH-----------QGESNWPLLD--MRGR-------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 505397517 174 EVLKVMRS-LADEGMTMVIVTHEIGFaRDVASRLIFIDR 211
Cdd:cd03240 160 SLAEIIEErKSQKNFQLIVITHDEEL-VDAADHIYRVEK 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-168 |
4.24e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVL-HDINLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTLLvagmhitdphasecdirREA 79
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------------RSA 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 80 GM---VFQQFHLfphlTALEnVMFGPIRVRKQSKAAAREQAL-ALLDRVGLKDRANHYPS-ELSGGQQQRVAIARALAVK 154
Cdd:PLN03073 571 KVrmaVFSQHHV----DGLD-LSSNPLLYMMRCFPGVPEQKLrAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKK 645
|
170
....*....|....
gi 505397517 155 PKMMLFDEPTSALD 168
Cdd:PLN03073 646 PHILLLDEPSNHLD 659
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
29-196 |
4.54e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 29 VVVIIGPSGSGKSTLLRCINKL---EAISSGTLLVAGMHITDPHAS-----ECD-----IRREAGMVFQQFHLFP----- 90
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYAlygKARSRSKLRSDLINVGSEEASvelefEHGgkryrIERRQGEFAEFLEAKPserke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 91 ------HLTALENVM--FGPIRVRKQSKAAAREQALALLDRVGLKDRANHYPSELSGGQQQRVAIARALAvkpkmMLFDe 162
Cdd:COG0419 105 alkrllGLEIYEELKerLKELEEALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLLS-----LILD- 178
|
170 180 190
....*....|....*....|....*....|....
gi 505397517 163 pTSALDPELRHEVLKVMRSLAdegmtmvIVTHEI 196
Cdd:COG0419 179 -FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-216 |
1.08e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 3 EFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRC-INKLEAIS----SGTLL-VAGMhitDPHASECDIR 76
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSgrihCGTKLeVAYF---DQHRAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 77 R----------EAGMVF-QQFHLfphLTALENVMFGPIRVRKQSKAaareqalalldrvglkdranhypseLSGGQQQRV 145
Cdd:PRK11147 398 KtvmdnlaegkQEVMVNgRPRHV---LGYLQDFLFHPKRAMTPVKA-------------------------LSGGERNRL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 146 AIARaLAVKP-KMMLFDEPTSALDPELRhEVLKVMrsLADEGMTMVIVTHEIGFARD-VASRLIFIDRGTIAE 216
Cdd:PRK11147 450 LLAR-LFLKPsNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKIGR 518
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
135-195 |
1.43e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 1.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505397517 135 SELSGGQQQRVAIARALAVK---PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-194 |
2.02e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 135 SELSGGQQQRVAIARAL---AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
138-207 |
2.16e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 138 SGGQQQRVAIARALAVKPKMMLFDEPTSALDpelRHEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLI 207
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-195 |
2.27e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 7 VSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRCI-NKLEAISSGTLLVAGMHITdphasecdirreagmVFQQ 85
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIGLAKGIKLG---------------YFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 86 fHLFPHLTALENvmfgPIRvrKQSKAAAREQALALLDRVG----LKDRANHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:PRK10636 383 -HQLEFLRADES----PLQ--HLARLAPQELEQKLRDYLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....
gi 505397517 162 EPTSALDPELRHEVLKvmrSLADEGMTMVIVTHE 195
Cdd:PRK10636 456 EPTNHLDLDMRQALTE---ALIDFEGALVVVSHD 486
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-194 |
3.64e-06 |
|
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: 47.32 E-value: 3.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 137 LSGGQQQRVAIARALAVK---PKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-216 |
4.81e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 1 MVEFSAVSKSFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLrcinkleAISSGTLLVAGMHITDPHasecdiRREAG 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLL-------ALLKNEISADGGSYTFPG------NWQLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 81 MVFQQFHLFPhLTALENVMFGPIRVRK--QSKAAAREQ------------------------ALALLDRVGLKDRANHYP 134
Cdd:PRK10636 68 WVNQETPALP-QPALEYVIDGDREYRQleAQLHDANERndghaiatihgkldaidawtirsrAASLLHGLGFSNEQLERP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 135 -SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElrhEVLKVMRSLADEGMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:PRK10636 147 vSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQS 223
|
...
gi 505397517 214 IAE 216
Cdd:PRK10636 224 LFE 226
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-194 |
8.49e-06 |
|
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: 45.84 E-value: 8.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 127 KDRANHYPSELSGGQQQ---RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:pfam13304 227 GGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-232 |
1.00e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 135 SELSGGQQQRVAIARALAVKPK---MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDvASRLIFIDR 211
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
90 100
....*....|....*....|.
gi 505397517 212 GTIAEDGSpdmLLNASSNPRL 232
Cdd:PRK00635 1777 GSGKTGGK---ILFSGPPKDI 1794
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-239 |
1.71e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.99 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 17 LHDINLKIEAGeVVVIIGPSGSGKSTLLRCINKL------EAISS------------------------GTLLVAGMHIT 66
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLlgpsssRKFDEedfylgddpdlpeieieltfgsllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 67 DPHASECDIRREAGMVFQQFH-LFPHLTALENVMFGPIRVRKQSKAAAREQALALLdRVGLKDRANHYPSELSGGQQQRV 145
Cdd:COG3593 93 DKEELEEALEELNEELKEALKaLNELLSEYLKELLDGLDLELELSLDELEDLLKSL-SLRIEDGKELPLDRLGSGFQRLI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 146 AIA--RALA-----VKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHEIGFARDV-ASRLIFIDRGtiaED 217
Cdd:COG3593 172 LLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRD---SG 248
|
250 260
....*....|....*....|..
gi 505397517 218 GSPDMLLNASSNPRLKEFLQHV 239
Cdd:COG3593 249 GTTSTKLIDLDDEDLRKLLRYL 270
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
118-194 |
2.33e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 118 LALLDRVGLkdranHY-----PS-ELSGGQQQRVAIARALAVKPK---MMLFDEPTSALDPELRHEVLKVMRSLADEGMT 188
Cdd:COG0178 807 LQTLQDVGL-----GYiklgqPAtTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNT 881
|
....*.
gi 505397517 189 MVIVTH 194
Cdd:COG0178 882 VVVIEH 887
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-195 |
2.59e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505397517 137 LSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTHE 195
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSE 463
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-193 |
1.02e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 42.25 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505397517 136 ELSGGQQQRVAIARALAVK-----PkMMLFDEPTSALDPELRHEVLKVMRSLADEgmTMVIVT 193
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALDAQYRTAVANMIKELSDG--AQFITT 217
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
1.15e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.15e-04
10 20
....*....|....*....|....*..
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTL 43
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-214 |
1.77e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 11 FGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLRcinkleaISSGTLL-VAGMHITDPHASECDIRREagmvfqQFhLF 89
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMK-------ILGGDLEpSAGNVSLDPNERLGKLRQD------QF-AF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 90 PHLTALENVMFGPI---RVRKQS---------------KAAAREQALALLDRVGLKDRA------------NHYP--SEL 137
Cdd:PRK15064 77 EEFTVLDTVIMGHTelwEVKQERdriyalpemseedgmKVADLEVKFAEMDGYTAEARAgelllgvgipeeQHYGlmSEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 138 SGGQQQRVAIARALAVKPKMMLFDEPTSALDpelrhevLKVMRSLADE----GMTMVIVTHEIGFARDVASRLIFIDRGT 213
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnerNSTMIIISHDRHFLNSVCTHMADLDYGE 229
|
.
gi 505397517 214 I 214
Cdd:PRK15064 230 L 230
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-58 |
3.56e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|....*...
gi 505397517 21 NLKIEAGEVVVIIGPSGSGKSTLLRCINKLEAISSGTL 58
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-44 |
4.15e-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: 4.15e-04
10 20
....*....|....*....|....*...
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLL 44
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-44 |
7.08e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 7.08e-04
10 20
....*....|....*....|....*...
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTLL 44
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-195 |
1.01e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505397517 118 LALLDRVGLK----DRAnhyPSELSGGQQQRVAIARAL--AVKPKMMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVI 191
Cdd:TIGR00630 469 LGFLIDVGLDylslSRA---AGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV 545
|
....
gi 505397517 192 VTHE 195
Cdd:TIGR00630 546 VEHD 549
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-194 |
1.49e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505397517 137 LSGGQQQRVAIARALAVKPK---MMLFDEPTSALDPELRHEVLKVMRSLADEGMTMVIVTH 194
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEH 891
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
24-88 |
1.70e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.62 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505397517 24 IEAGE-VVVIIGPSGSGKSTLLRCInkLEAISSGTLLVagmHITDPHASECDIRReagMVFQQFHL 88
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRL--LERLPDDVKVA---YIPNPQLSPAELLR---AIADELGL 96
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-62 |
1.77e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 1.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 505397517 18 HDINLKIEAGEVVVIIGPSGSGKSTLlrcinkLEAISsgTLLVAG 62
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTL------LDAIQ--TLLVPA 49
|
|
| HprK |
COG1493 |
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ... |
27-61 |
1.83e-03 |
|
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms];
Pssm-ID: 441102 [Multi-domain] Cd Length: 142 Bit Score: 37.47 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|....*
gi 505397517 27 GEVVVIIGPSGSGKSTLLrcinkLEAISSGTLLVA 61
Cdd:COG1493 11 GRGVLITGPSGSGKSELA-----LELIKRGHRLVA 40
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
1.88e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.88e-03
10 20
....*....|....*....|....*..
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTL 43
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-43 |
2.11e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.11e-03
10 20
....*....|....*....|....*..
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTL 43
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
18-48 |
2.65e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 2.65e-03
10 20 30
....*....|....*....|....*....|.
gi 505397517 18 HDINLKIEAGeVVVIIGPSGSGKSTLLRCIN 48
Cdd:COG3950 17 LEIDFDNPPR-LTVLVGENGSGKTTLLEAIA 46
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
29-49 |
2.77e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 36.74 E-value: 2.77e-03
|
| AAA_23 |
pfam13476 |
AAA domain; |
17-47 |
2.87e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 2.87e-03
10 20 30
....*....|....*....|....*....|.
gi 505397517 17 LHDINLKIEAGeVVVIIGPSGSGKSTLLRCI 47
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
27-45 |
3.77e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.73 E-value: 3.77e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-47 |
4.74e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 4.74e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-43 |
5.24e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 5.24e-03
10 20
....*....|....*....|....*..
gi 505397517 17 LHDINLKIEAGEVVVIIGPSGSGKSTL 43
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-50 |
6.13e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.61 E-value: 6.13e-03
10 20
....*....|....*....|....*
gi 505397517 26 AGEVVVIIGPSGSGKSTLlrcINKL 50
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNAL 105
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-66 |
6.54e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.11 E-value: 6.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505397517 26 AGEVVVIIGPSGSGKSTLlrcINKLE--------AISsgTLLVAGMHIT 66
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTL---LNALApdlelktgEIS--EALGRGKHTT 206
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
10-48 |
9.24e-03 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 36.25 E-value: 9.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 505397517 10 SFGTTPVLHDINLKIEAGEVVVIIGPSGSGKSTLLR--CIN 48
Cdd:cd03286 13 STASSFVPNDVDLGATSPRILVLTGPNMGGKSTLLRtvCLA 53
|
|
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