|
Name |
Accession |
Description |
Interval |
E-value |
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-242 |
0e+00 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 545.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDKAIREL 80
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEP 160
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQTDAFKNYL 240
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEAFKNYL 240
|
..
gi 504696061 241 SH 242
Cdd:PRK11124 241 SH 242
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-242 |
0e+00 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 517.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDKAIREL 80
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEP 160
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQTDAFKNYL 240
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQTEAFAHYL 240
|
..
gi 504696061 241 SH 242
Cdd:COG4161 241 SH 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-242 |
3.73e-122 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 346.60 E-value: 3.73e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfakTPSDKAIRELRQ 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL----TDSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQTDAFKNYLS 241
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEeFFENPQHERTRAFLS 237
|
.
gi 504696061 242 H 242
Cdd:COG1126 238 K 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-219 |
3.48e-104 |
|
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: 300.22 E-value: 3.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdFAKTPSDKAIRELRQ 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDG----LKLTDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-242 |
7.14e-100 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 291.32 E-value: 7.14e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKT------PSD-KAIRELRQNV 84
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvPADrRQLQRIRTRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLL 164
Cdd:COG4598 98 GMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 165 FDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYLSH 242
Cdd:COG4598 178 FDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPpAEVFGNPKSERLRQFLSS 256
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-241 |
7.86e-88 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 260.45 E-value: 7.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGaHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDK--AIRELRQNVGMVF 88
Cdd:PRK11264 13 FHG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQkgLIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK11264 92 QNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 169 TAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTDAFKNYLS 241
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAkALFADPQQPRTRQFLE 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-242 |
3.38e-86 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 255.79 E-value: 3.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfAKTPSDKaIRELRQNVGMVFQQY 91
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK---VNDPKVD-ERLIRQEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:PRK09493 87 YLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 172 LDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYLSH 242
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDpQVLIKNPPSQRLQEFLQH 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-242 |
5.49e-84 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 253.46 E-value: 5.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY----GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTpSDKAIR 78
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG--VDLTAL-SERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAEN-VALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAF 236
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPvLDVFANPQSELT 237
|
....*.
gi 504696061 237 KNYLSH 242
Cdd:COG1135 238 RRFLPT 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-219 |
7.98e-81 |
|
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: 241.24 E-value: 7.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGA----HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPSDKAIR 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG--TDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:cd03255 79 FRRRHIGFVFQSFNLLPDLTALEN-VELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKtASRVVYMENGYI 219
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-232 |
1.88e-79 |
|
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: 238.25 E-value: 1.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAH----QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTpSDKAIR 78
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG--TDLTLL-SGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFEN-VALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQ 232
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEeVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-222 |
5.62e-78 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.55 E-value: 5.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYG----AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIR 78
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQ--DISSL-SERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELR-QNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALM 157
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPELTALEN-VALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKtASRVVYMENGYIVEQ 222
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-241 |
2.06e-76 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 231.78 E-value: 2.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFA-------KTPSDKAIRELRQNV 84
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYS-DRYPLHLSGGQQQRVAIARALMMEPAVL 163
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 164 LFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYLS 241
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGApEQLFGNPQSPRLQQFLK 253
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-223 |
1.35e-73 |
|
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: 222.78 E-value: 1.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDkairelRQ 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--DVTGVPPE------RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAEN-IAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-225 |
2.79e-73 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 226.90 E-value: 2.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelR 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR--DVTGLPPEK-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 qNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:COG3842 78 -NVGMVFQDYALFPHLTVAEN-VAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA 225
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-224 |
7.19e-71 |
|
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: 216.43 E-value: 7.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELR 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG------KDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQynlwP-----HLTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARAL 156
Cdd:COG1122 75 RKVGLVFQN----PddqlfAPTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-217 |
1.69e-69 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 211.28 E-value: 1.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfakTPSDKAIRELRQ 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL----TDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIEApcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-233 |
2.13e-69 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 216.55 E-value: 2.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDKairel 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRER----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 rqNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEP 160
Cdd:COG1118 76 --RVGFVFQHYALFPHMTVAEN-IAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQT 233
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDeVYDRPAT 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-221 |
6.74e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.06 E-value: 6.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsDKAIRELR 81
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG--QDLSRLK-RREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYEN-VALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVE 221
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
12-241 |
8.85e-69 |
|
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: 212.00 E-value: 8.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGN---HFDFAKTP----SDKAIRELRQNV 84
Cdd:TIGR03005 10 FGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEqlyHMPGRNGPlvpaDEKHLRQMRNKI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLL 164
Cdd:TIGR03005 90 GMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVML 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 165 FDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTDAFKNYLS 241
Cdd:TIGR03005 170 FDEVTSALDPELVGEVLNVIRRLAsEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPdEIFRQPKEERTREFLS 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-233 |
9.18e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 214.94 E-value: 9.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDfaktPSDkair 78
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLP----PKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 elRqNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:COG3839 75 --R-NIAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHE-VEvARKTASRVVYMENGYIVEQGD-ASCFANPQT 233
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDqVE-AMTLADRIAVMNDGRIQQVGTpEELYDRPAN 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-224 |
1.52e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 207.99 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaiRELRQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG--EDVARDP-----AEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIEApCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:COG1131 74 RIGYVPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-237 |
8.98e-67 |
|
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: 206.58 E-value: 8.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGA----HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIR 78
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG------RPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQY--NLWPHLTVLQNLIEaPCRVLGLSKDQAigRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARA 155
Cdd:COG1124 76 AFRRRVQMVFQDPyaSLHPRHTVDRILAE-PLRIHGLPDREE--RIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQT 233
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAdLLAGPKH 232
|
....
gi 504696061 234 DAFK 237
Cdd:COG1124 233 PYTR 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-220 |
9.93e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.45 E-value: 9.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINC-FYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTpsdKAIRELR 81
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG---RALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNL-------IEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIAR 154
Cdd:COG3638 80 RRIGMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-224 |
2.61e-66 |
|
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: 204.72 E-value: 2.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEM-----PRSGTLAIAG-NHFDfaktpSDKA 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkDIYD-----LDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 IRELRQNVGMVFQQYNLWPhLTVLQNlIEAPCRVLGLSKDQAI-GRAEKLLERLRLKPY-SDR-YPLHLSGGQQQRVAIA 153
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDN-VAYGLRLHGIKLKEELdERVEEALRKAALWDEvKDRlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 154 RALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-232 |
2.91e-66 |
|
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: 213.23 E-value: 2.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIRELRQNVGMVFQ--- 89
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGK--DLTKL-SRRSLRELRRRVQMVFQdpy 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 -QYNlwPHLTVLQNLIEaPCRVLG-LSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:COG1123 353 sSLN--PRMTVGDIIAE-PLRLHGlLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 167 EPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASC-FANPQ 232
Cdd:COG1123 430 EPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEvFANPQ 497
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-234 |
4.06e-66 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 208.12 E-value: 4.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY----GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIR 78
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ--DLTAL-SEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSRTVFDN-VALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQTD 234
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSeVFSHPKHP 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-224 |
5.02e-66 |
|
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: 204.44 E-value: 5.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIRELRQ 82
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ--DITGL-SEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLG-LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFEN-VAFPLREHTdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-228 |
1.51e-65 |
|
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: 203.18 E-value: 1.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGA-HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTpsdKAIRELR 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG---KALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNLIEA------PCRVL-GLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIAR 154
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGrlgrrsTWRSLfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCF 228
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-222 |
5.30e-64 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 199.49 E-value: 5.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIREl 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG------EDATDVPVQE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 rQNVGMVFQQYNLWPHLTVLQNL---IEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALM 157
Cdd:cd03296 74 -RNVGFVFQHYALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIvEQ 222
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRI-EQ 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-217 |
6.10e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 199.93 E-value: 6.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY----GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIR 78
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-----------KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:COG1116 77 GPGPDRGVVFQEPALLPWLTVLDN-VALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 159 EPAVLLFDEPTAALDpEITAQIVS--IIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:COG1116 156 DPEVLLMDEPFGALD-ALTRERLQdeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-217 |
1.38e-63 |
|
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: 197.30 E-value: 1.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFY--GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELR 81
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG------KDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQynlwP-----HLTVLQNLIEAPCRvLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARAL 156
Cdd:cd03225 75 RKVGLVFQN----PddqffGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-226 |
2.20e-63 |
|
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: 197.91 E-value: 2.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYG-AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlAIAGNHFDFAKTpSDKAIRELR 81
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSG--SILLEGTDITKL-RGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNLIEApcRV---------LGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAI 152
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHG--RLgykptwrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-241 |
8.14e-63 |
|
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: 196.36 E-value: 8.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 9 NCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlAIAGN-HFDFAKTPSDKA-IRELRQNVGM 86
Cdd:TIGR00972 8 NLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGV-RIEGKvLFDGQDIYDKKIdVVELRRRVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 87 VFQQYNLWPhLTVLQNLIEAPcRVLGL-SKDQAIGRAEKLLERLRL----KPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:TIGR00972 87 VFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYL 240
Cdd:TIGR00972 165 VLLLDEPTSALDPIATGKIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPtEQIFTNPKEKRTEDYI 243
|
.
gi 504696061 241 S 241
Cdd:TIGR00972 244 S 244
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-241 |
3.51e-60 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 190.25 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLN-LLEMPR----SGTLAIAG-NHFDfaktpSDKA 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDLIPgarvEGEILLDGeDIYD-----PDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 IRELRQNVGMVFQQYNLWPHlTVLQNlIEAPCRVLGL-SKDQAIGRAEKLLERL--------RLKpysdRYPLHLSGGQQ 147
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPK-SIYDN-VAYGLRLHGIkSKSELDEIVEESLRKAalwdevkdRLK----KSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS- 226
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEq 239
|
250
....*....|....*
gi 504696061 227 CFANPQTDAFKNYLS 241
Cdd:COG1117 240 IFTNPKDKRTEDYIT 254
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-234 |
9.83e-60 |
|
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: 188.66 E-value: 9.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGA-HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIRE-- 79
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG-----------EDIREqd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 ---LRQNVGMVFQQYNLWPHLTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKP--YSDRYPLHLSGGQQQRVAIAR 154
Cdd:cd03295 70 pveLRRKIGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 155 ALMMEPAVLLFDEPTAALDP----EITAQIVSIIRELAEtniTQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFA 229
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQELGK---TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTpDEILR 225
|
....*
gi 504696061 230 NPQTD 234
Cdd:cd03295 226 SPAND 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-223 |
1.66e-59 |
|
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: 187.71 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIRELRQ 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE--DISGL-SEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLG-LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFEN-VAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-216 |
3.57e-59 |
|
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: 186.14 E-value: 3.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYG----AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIR 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----------EPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:cd03293 70 GPGPDRGYVFQQDALLPWLTVLDN-VALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 159 EPAVLLFDEPTAALDP----EITAQIVSIIRelaETNITQVIVTHEVEVARKTASRVVYMEN 216
Cdd:cd03293 149 DPDVLLLDEPFSALDAltreQLQEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-223 |
6.24e-59 |
|
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: 185.79 E-value: 6.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfaKTPSDKAIRELRQN-VGMVFQQY 91
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKD----LLKLSRRLRKIRRKeIQMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 --NLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAE-KLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:cd03257 92 msSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 168 PTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-223 |
2.44e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 186.83 E-value: 2.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPsdkaIRELR 81
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGE--DIRDLD----PVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKP--YSDRYPLHLSGGQQQRVAIARALMME 159
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAEN-IATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 160 PAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYD 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-226 |
9.61e-58 |
|
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: 183.52 E-value: 9.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIRELRQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-------EDVRKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:COG4555 75 QIGVLPDERGLYDRLTVREN-IRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-225 |
1.38e-57 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 183.08 E-value: 1.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDkairelRQ 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ--DATRVHAR------DR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:TIGR00968 73 KIGFVFQHYALFKHLTVRDN-IAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA 225
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLhDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSP 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-223 |
3.85e-57 |
|
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: 181.67 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelrQ 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK--DITNLPPHK------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFEN-IAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-223 |
2.62e-56 |
|
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: 180.73 E-value: 2.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGA-----HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdFAKTPSDK-A 76
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDG----RDITAKKKkK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 IRELRQNVGMVFQ--QYNLWpHLTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIA 153
Cdd:TIGR04521 77 LKDLRKKVGLVFQfpEHQLF-EETVYKDIAFGP-KNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 154 RALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-240 |
3.30e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 179.18 E-value: 3.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGaHQAL-FDITLncPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKaiRElr 81
Cdd:COG3840 2 LRLDDLTYRYG-DFPLrFDLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ--DLTALPPAE--RP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 qnVGMVFQQYNLWPHLTVLQNLieapcrVLGLSKDQAIGRAEK-----LLERLRLKPYSDRYPLHLSGGQQQRVAIARAL 156
Cdd:COG3840 73 --VSMLFQENNLFPHLTVAQNI------GLGLRPGLKLTAEQRaqveqALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTD 234
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPtAALLDGEPPP 224
|
....*.
gi 504696061 235 AFKNYL 240
Cdd:COG3840 225 ALAAYL 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-232 |
1.32e-55 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 185.49 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLeMPRSGTlaIAGNHFDFAKTPSDKAIRELRQNVGMVFQ--Q 90
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGR--ISGEVLLDGRDLLELSEALRGRRIGMVFQdpM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNLWPhLTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:COG1123 94 TQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 171 ALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQ 232
Cdd:COG1123 172 ALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPeEILAAPQ 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-222 |
2.23e-55 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 180.66 E-value: 2.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIREl 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG------TDVSRLHARD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 rQNVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSK--DQAIGRAE--KLLERLRLKPYSDRYPLHLSGGQQQRVAIARAL 156
Cdd:PRK10851 74 -RKVGFVFQHYALFRHMTVFDN-IAFGLTVLPRRErpNAAAIKAKvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIvEQ 222
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI-EQ 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-223 |
2.76e-55 |
|
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: 176.29 E-value: 2.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelrQ 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPKD------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03301 73 DIAMVFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-234 |
4.02e-54 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 175.14 E-value: 4.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIRELRQN-VGMVFQQYNLWP 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ--DIAAM-SRKELRELRRKkISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE 175
Cdd:cd03294 116 HRTVLEN-VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 176 ITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTD 234
Cdd:cd03294 195 IRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPeEILTNPAND 255
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-223 |
1.74e-53 |
|
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: 176.00 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelrQ 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR--DITRLPPQK------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADN-IAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:TIGR03265 156 LLLDEPLSALDARVREHLRTEIRQLqRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-217 |
2.21e-53 |
|
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: 171.28 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPsDKAIRELRQNVGMVFQQYN 92
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGE--DVNRLR-GRQLPLLRRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:TIGR02673 90 LLPDRTVYEN-VALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504696061 173 DPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:TIGR02673 169 DPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-217 |
7.54e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.61 E-value: 7.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQ 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG------KPLSAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHlTVLQNLiEAPCRVLGLSKDQAigRAEKLLERLRLKPYS-DRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:COG4619 75 QVAYVPQEPALWGG-TVRDNL-PFPFQLRERKFDRE--RALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-232 |
1.25e-52 |
|
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: 172.55 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLEMPR--SGTLAIAGNhfDFAKTpSDKAIRELRQN-VGMVF 88
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPGitSGEILFDGE--DLLKL-SEKELRKIRGReIQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQ-YN-LWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKP---YSDRYPLHLSGGQQQRVAIARALMMEPAVL 163
Cdd:COG0444 93 QDpMTsLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 164 LFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQ 232
Cdd:COG0444 173 IADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVeELFENPR 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-226 |
5.65e-52 |
|
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: 168.00 E-value: 5.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRElrq 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR--DITGLPPHERARA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLiEAPCRVLGLSKDQAigRAEKLLERL-RLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENL-LLGAYARRRAKRKA--RLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-226 |
6.03e-52 |
|
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: 168.38 E-value: 6.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRELRQNVGMVFQQYNLWPHL 97
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ--DLFALDEDARARLRARHVGFVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNlIEAPCRVLGlsKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEIT 177
Cdd:COG4181 106 TALEN-VMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATG 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504696061 178 AQIVSIIREL-AETNITQVIVTHEVEVARKtASRVVYMENGYIVEQGDAS 226
Cdd:COG4181 183 EQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-226 |
9.64e-52 |
|
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: 167.85 E-value: 9.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLAIAGNhfDFAKTPSDKAIRelrQ 82
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLLP-PRSGSIRFDGE--DITGLPPHRIAR---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLieapcrVLGLSKDQAIGRAEKLLERL-----RLKPYSDRYPLHLSGGQQQRVAIARALM 157
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENL------LLGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-232 |
1.57e-50 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 167.60 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKtPSDKAIRELRQNVGMVFQ--QYNL 93
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ--DITG-LSGRELRPLRRRMQMVFQdpYASL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQnLIEAPCRVLGL-SKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:COG4608 109 NPRMTVGD-IIAEPLRIHGLaSKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 172 LDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQ 232
Cdd:COG4608 188 LDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRdELYARPL 250
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-170 |
1.73e-50 |
|
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: 161.66 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQYNLWPHL 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL------TDDERKSLRKEIGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 98 TVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDR----YPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:pfam00005 75 TVRENLRLGL-LLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-223 |
2.48e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 168.74 E-value: 2.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIRELRQN-VGMVFQQYNLWP 95
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGE--DITKL-SKKELRELRRKkMSMVFQHFALLP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPe 175
Cdd:COG4175 119 HRTVLEN-VAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP- 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 176 itaqivsIIR-----EL----AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:COG4175 197 -------LIRremqdELlelqAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIG 246
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-223 |
3.69e-50 |
|
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: 166.03 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaiRELRQNVGMVFQQY 91
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG--YDVVREP-----RKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:TIGR01188 76 SVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504696061 172 LDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-217 |
3.98e-50 |
|
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: 161.41 E-value: 3.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaiRELRQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--KDIKKEP-----EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLieapcrvlglskdqaigraekllerlrlkpysdryplHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03230 74 RIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-226 |
2.86e-49 |
|
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: 162.14 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSdkaiRELRQ 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR--DLASLSR----RELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVL----------QNLIEAPCRvlglsKDQAIgrAEKLLERLRLKPYSDRYPLHLSGGQQQRVAI 152
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRelvalgryphLGLFGRPSA-----EDREA--VEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-219 |
3.02e-49 |
|
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: 160.65 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPsDKAIRELRQNVGMVFQQYNLWPH 96
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ--DVSDLR-GRAIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEI 176
Cdd:cd03292 93 RNVYEN-VAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504696061 177 TAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:cd03292 172 TWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-223 |
2.22e-48 |
|
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: 158.43 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLncPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtPSDKAirelrq 82
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-PADRP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 nVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAiGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03298 72 -VSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDR-QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-223 |
3.23e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 162.81 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelrQ 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAEN------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFEN-VAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-234 |
4.84e-48 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 165.63 E-value: 4.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLemPRSGTLAIAGNHFDfakTPSDKAIRELRQNVGMVFQQ- 90
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRLI--PSEGEIRFDGQDLD---GLSRRALRPLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YN-LWPHLTVLQnLIEAPCRVL--GLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:COG4172 372 FGsLSPRMTVGQ-IIAEGLRVHgpGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 167 EPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTD 234
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTeQVFDAPQHP 520
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-223 |
9.03e-48 |
|
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: 161.56 E-value: 9.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRELRQNVGMVFQQYN 92
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGE--NIMKQSPVELREVRRKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:TIGR01186 82 LFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504696061 173 DPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVG 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-223 |
1.52e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 157.98 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY--GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaKTPSDKAIREL 80
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL-----DTLDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQqyNlwPH-----LTV-------LQNLieapcrvlGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQ 148
Cdd:TIGR04520 76 RKKVGMVFQ--N--PDnqfvgATVeddvafgLENL--------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 149 RVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEG 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-233 |
1.94e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.17 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRV-LNLLEmPRSGTLAIAGnhfdfaktpsdKAIRELR 81
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAiLGLLP-PTSGTVRLFG-----------KPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNL---WPhLTVLQnLIEAPC----RVLGLSKDQAIGRAEKLLERLRLKPYSDRyPL-HLSGGQQQRVAIA 153
Cdd:COG1121 75 RRIGYVPQRAEVdwdFP-ITVRD-VVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 154 RALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMeNGYIVEQGDASCFANPQT 233
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPEN 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-225 |
8.13e-47 |
|
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: 158.73 E-value: 8.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 19 FDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNH-FDfaktpSDKAIR---ELRQnVGMVFQQYNLW 94
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQD-----SARGIFlppHRRR-IGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHLTVLQNLiEAPCRVLGLSKDQAigRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:COG4148 90 PHLSVRGNL-LYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504696061 175 EITAQIVSIIRELA-ETNITQVIVTHEV-EVARkTASRVVYMENGYIVEQGDA 225
Cdd:COG4148 167 ARKAEILPYLERLRdELDIPILYVSHSLdEVAR-LADHVVLLEQGRVVASGPL 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-232 |
1.39e-46 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 157.43 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKtPSDKAIRELRQNVGMVFQQ-Y-NL 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--DLLK-ADPEAQKLLRQKIQIVFQNpYgSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQNLiEAPCRV-LGLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:PRK11308 106 NPRKKVGQIL-EEPLLInTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 172 LDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQ 232
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTkEQIFNNPR 247
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
16-219 |
2.65e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 153.34 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDKAIRelRQNVGMVFQQYNLWP 95
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILR--RELIGYIFQSFNLIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE 175
Cdd:NF038007 97 HLSIFDN-VALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504696061 176 ITAQIVSIIRELAETNITQVIVTHEVEvARKTASRVVYMENGYI 219
Cdd:NF038007 176 NARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-217 |
4.33e-46 |
|
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: 150.86 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQN 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG------KDIAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 84 VGMVFQqynlwphltvlqnlieapcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALMMEPAVL 163
Cdd:cd00267 75 IGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504696061 164 LFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-232 |
5.83e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 154.79 E-value: 5.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIaGNHFDFAKTpSDKAIRELRQNVGMVFQ--QYNLW 94
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGK-KNKKLKPLRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHlTVLQNLIEAPCRvLGLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALD 173
Cdd:PRK13634 100 EE-TVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 174 PEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQ 232
Cdd:PRK13634 178 PKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPrEIFADPD 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-223 |
1.24e-45 |
|
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: 151.75 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaiRELRQNVGMVFQQY 91
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREP-----REVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNL-IEApcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:cd03265 83 SVDDELTGWENLyIHA--RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504696061 171 ALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-226 |
1.26e-45 |
|
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: 152.21 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRelrQ 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE--DITGLPPHEIAR---L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLS---------KDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIA 153
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 154 RALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-223 |
1.47e-45 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 151.29 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCP---EGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGN-HFDFAK---TPSDkairelRQNVGMV 87
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvLFDSRKkinLPPQ------QRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 88 FQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAigRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:cd03297 81 FQQYALFPHLNVREN-LAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 168 PTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-220 |
3.18e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 159.89 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRELRQNVGMVFQQYNLWPHL 97
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ--DVATLDADALAQLRREHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEIT 177
Cdd:PRK10535 102 TAAQN-VEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504696061 178 AQIVSIIRELAETNITQVIVTHEVEVARKtASRVVYMENGYIV 220
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-204 |
3.41e-45 |
|
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: 149.50 E-value: 3.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtpsdKAIRELRQNVGMVFQ- 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR----KGLLERRQRVGLVFQd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 --QYNLWPhlTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:TIGR01166 77 pdDQLFAA--DVDQDVAFGP-LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 504696061 168 PTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVA 204
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-214 |
4.00e-45 |
|
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: 150.07 E-value: 4.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdFAKTPSDKAIRELRQN- 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ---ETPPLNSKKASKFRREk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 84 VGMVFQQYNLWPHLTVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVL 163
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENL-DLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 164 LFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKtASRVVYM 214
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-222 |
4.77e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 154.23 E-value: 4.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDfaktPSDKAIrelrqnvGMVFQ 89
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNELE----PADRDI-------AMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLWPHLTVLQNLiEAPCRVLGLSK---DQAIGRAEKLLErlrLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK11650 84 NYALYPHMSVRENM-AYGLKIRGMPKaeiEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 167 EPTAALDPEITAQIVSIIREL-AETNITQVIVTH-EVEvARKTASRVVYMeNGYIVEQ 222
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLhRRLKTTSLYVTHdQVE-AMTLADRVVVM-NGGVAEQ 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-225 |
1.11e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 152.95 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRElrQNV 84
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV------THRSIQQ--RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLL 164
Cdd:PRK11432 81 CMVFQSYALFPHMSLGEN-VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 165 FDEPTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA 225
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-223 |
1.34e-44 |
|
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: 149.85 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSG-TLAIAGNhfDFAKTPsdkaIRELR 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE--RRGGED----VWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMV--FQQYNLWPHLTVLQNLIEAPCRVLGLSK---DQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARAL 156
Cdd:COG1119 78 KRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVI-VTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-241 |
1.79e-44 |
|
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: 149.02 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelrQNVGMVFQQYNLWPHL 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--DITNLPPEK------RDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEIT 177
Cdd:cd03299 87 TVYKN-IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 178 AQIVSIIRELAETNITQVI-VTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYLS 241
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKpEEVFKKPKNEFVAEFLG 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-233 |
3.71e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 149.46 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtpsdKAIRELRQNVGMVFQQYN--- 92
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK----KSLLEVRKTVGIVFQNPDdql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPhlTVLQNLIEAPCRvLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:PRK13639 92 FAP--TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 173 DPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQT 233
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKeVFSDIET 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.45e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 149.08 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAH-----QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSD- 74
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 75 -----------------KAIRELRQNVGMVFQ--QYNLWPHlTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRL-KPY 134
Cdd:PRK13651 81 ekvleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGP-VSMGVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 135 SDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYM 214
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|
gi 504696061 215 ENGYIVEQGD 224
Cdd:PRK13651 239 KDGKIIKDGD 248
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-232 |
1.49e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 147.96 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQynlwP 95
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG------REVNAENEKWVRSKVGLVFQD----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 H-----LTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:PRK13647 89 DdqvfsSTVWDDVAFGP-VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 171 ALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQ 232
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-223 |
1.64e-43 |
|
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: 146.36 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaiRELRQNVGMVFQQYNLWP 95
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEP-----AEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE 175
Cdd:cd03266 92 RLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504696061 176 ITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-235 |
5.69e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 145.11 E-value: 5.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYgAHQAL-FDITLNcpEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDkairelR 81
Cdd:PRK10771 2 LKLTDITWLY-HHLPMrFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPS------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKDQAIgRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:PRK10771 71 RPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQRE-KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQTDA 235
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-223 |
8.27e-43 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 144.21 E-value: 8.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLAIAGNHfdfaktpsdkaIRELRQNVGMVFQQ 90
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLK-PTSGSIRVFGKP-----------LEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNL-W--PhLTVLQNL---IEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRyPL-HLSGGQQQRVAIARALMMEPAVL 163
Cdd:cd03235 77 RSIdRdfP-ISVRDVVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-QIgELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 164 LFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMeNGYIVEQG 223
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-224 |
1.28e-42 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 146.87 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 33 LLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSdkairELRqNVGMVFQQYNLWPHLTVLQNlIEAPCRVLG 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE--DVTNVPP-----HLR-HINMVFQSYALFPHMTVEEN-VAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 113 LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQ----IVSIIRELA 188
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQmqleLKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 504696061 189 etnITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:TIGR01187 152 ---ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-232 |
1.47e-42 |
|
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: 150.99 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKS-SLLRVLNLLemPRSGtlAIAGNHFDFAKTP----SDKAIRELRQN-VGM 86
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPA--AHPSGSILFDGQDllglSERELRRIRGNrIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 87 VFQQ--YNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLK-PYS--DRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:COG4172 97 IFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPERrlDAYPHQLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQ 232
Cdd:COG4172 177 LLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPtAELFAAPQ 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-223 |
2.19e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.19 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYG-----AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDfaktPSDK 75
Cdd:PRK13637 1 MSIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VD----ITDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 76 AI--RELRQNVGMVFQ--QYNLWPHlTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLK--PYSDRYPLHLSGGQQQR 149
Cdd:PRK13637 75 KVklSDIRKKVGLVFQypEYQLFEE-TIEKDIAFGP-INLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 150 VAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-223 |
2.70e-42 |
|
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: 142.72 E-value: 2.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGeTLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSdkairELRQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQ-----KLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03264 73 RIGYLPQEFGVYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITqVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDRIV-ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-241 |
8.17e-42 |
|
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: 142.28 E-value: 8.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRElrqN 83
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE--DITKLPPHERARA---G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 84 VGMVFQQYNLWPHLTVLQNLIeapcrvLGLskdQAIGRAEK-LLERLR-----LKPYSDRYPLHLSGGQQQRVAIARALM 157
Cdd:TIGR03410 77 IAYVPQGREIFPRLTVEENLL------TGL---AALPRRSRkIPDEIYelfpvLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAscfANPQTDAF 236
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAG---DELDEDKV 224
|
....*
gi 504696061 237 KNYLS 241
Cdd:TIGR03410 225 RRYLA 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-224 |
9.80e-42 |
|
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: 142.87 E-value: 9.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRelrqn 83
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR--DITGLPPHRIAR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 84 VGMV--FQQYNLWPHLTVLQNLIEAPCRVLGLS--------------KDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQ 147
Cdd:COG0411 79 LGIArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-220 |
1.79e-41 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 140.47 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktpsDKAIRELRQNVGMVFQ- 89
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---------PIKAKERRKSIGYVMQd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 -QYNLWPHlTVLQNLIeapcrvLGL-SKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:cd03226 80 vDYQLFTD-SVREELL------LGLkELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504696061 168 PTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-223 |
2.63e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY--GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIREL 80
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG------MVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQY-NLWPHLTV-------LQNLieapcrvlGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAI 152
Cdd:PRK13635 80 RRQVGMVFQNPdNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-217 |
7.22e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 137.90 E-value: 7.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYG--AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIREL 80
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL------RDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQynlwPHL---TVLQNLieapcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALM 157
Cdd:cd03228 75 RKNIAYVPQD----PFLfsgTIRENI--------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENG 217
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-223 |
8.13e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 137.95 E-value: 8.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQN 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG------KDLASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 84 VGMVFQqynlwphltvlqnlieapcrvlglskdqaigraekLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVL 163
Cdd:cd03214 75 IAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 164 LFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
1.55e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 141.53 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQ-----ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAI----AGNHFDFAK-- 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHEli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 71 -TPSDKAIR---ELRQNVGMVFQ--QYNLWPHlTVLQNLIEAPCrVLGLSKDQAIGRAEKLLERLRLK-PYSDRYPLHLS 143
Cdd:PRK13631 101 tNPYSKKIKnfkELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 144 GGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
.
gi 504696061 224 D 224
Cdd:PRK13631 259 T 259
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
1.58e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 139.59 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLN-LLEMPRS----GTLAIAGNHFdfaKTPSDKA 76
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEarveGEVRLFGRNI---YSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 IrELRQNVGMVFQQYNLWPHLTVLQNL-IEAPCRVLGLSKDQAIGRAEKLLERLRL-KPYSDR---YPLHLSGGQQQRVA 151
Cdd:PRK14267 81 I-EVRREVGMVFQYPNPFPHLTIYDNVaIGVKLNGLVKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 152 IARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELaETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFAN 230
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTrKVFEN 238
|
250
....*....|.
gi 504696061 231 PQTDAFKNYLS 241
Cdd:PRK14267 239 PEHELTEKYVT 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-223 |
1.90e-40 |
|
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: 138.18 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtpsdkairelRQ 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----------RN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIEApCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03269 71 RIGYLPEERGLYPKMKVIDQLVYL-AQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-241 |
2.70e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 138.89 E-value: 2.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLN-LLEM---PR-SGTLAIAGNhfDFAKTPsdkaI 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIELypeARvSGEVYLDGQ--DIFKMD----V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 78 RELRQNVGMVFQQYNLWPHLTVLQNLieapcrVLGLSKDQAIGRAEKLLERLR-----------LKPYSDRYPLHLSGGQ 146
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENV------ALGLKLNRLVKSKKELQERVRwalekaqlwdeVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 147 QQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELaETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA- 225
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTr 230
|
250
....*....|....*.
gi 504696061 226 SCFANPQTDAFKNYLS 241
Cdd:PRK14247 231 EVFTNPRHELTEKYVT 246
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
2.95e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 139.60 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY--GAHqALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaktpSDKAIREL 80
Cdd:PRK13636 6 LKVEELNYNYsdGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY----SRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQY-NLWPHLTVLQNLIEAPCRvLGLSKDQAIGRAEKLLERLRLKPYSDRyPLH-LSGGQQQRVAIARALMM 158
Cdd:PRK13636 81 RESVGMVFQDPdNQLFSASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDK-PTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-223 |
3.14e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 139.49 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGA-----HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPSDK 75
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD--TLITSTSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 76 AIRELRQNVGMVFQ--QYNLWPHlTVLQNLIEAPcRVLGLSKDQAIGRAEkllERLRLKPYS----DRYPLHLSGGQQQR 149
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGP-QNFGVSQEEAEALAR---EKLALVGISeslfEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 150 VAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
3-224 |
3.88e-40 |
|
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: 137.30 E-value: 3.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYgaHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG-NHFDFAktPSdkairelR 81
Cdd:TIGR01277 1 LALDKVRYEY--EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqSHTGLA--PY-------Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNL---IEAPCRVLGLSKDQAIGRAEKLlerlRLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:TIGR01277 70 RPVSMLFQENNLFAHLTVRQNIglgLHPGLKLNAEQQEKVVDAAQQV----GIADYLDRLPEQLSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:TIGR01277 146 PNPILLLDEPFSALDPLLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
3.98e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 138.84 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MS-IKLNGINCFYG----AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaKTPSdk 75
Cdd:COG4525 1 MSmLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV---TGPG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 76 AIRelrqnvGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARA 155
Cdd:COG4525 76 ADR------GVVFQKDALLPWLNVLDN-VAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMEN--GYIVEQ 222
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-217 |
7.38e-40 |
|
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: 136.87 E-value: 7.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktpSDKA-IRELRQNVGMVFQQY 91
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--------SIRTdRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:cd03263 85 ALFDELTVREHL-RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504696061 172 LDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:cd03263 164 LDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-224 |
1.65e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.97 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGAHqALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSdkaireLRQNVGMVFQQ 90
Cdd:PRK11607 29 FDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLSHVPP------YQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:PRK11607 100 YALFPHMTVEQN-IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 171 ALDPEITAQI-VSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:PRK11607 179 ALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
3.82e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 134.53 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIREL 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-------EPIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNLWPHLTVLQNLiEAPCRVLGLSKDQAigRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEP 160
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENL-RFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
4.11e-39 |
|
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: 143.44 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQ--ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDfaktpsdka 76
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQID--------- 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 IRELRQNVGMVFQQYNLWpHLTVLQNL------------IEApCRVLGLskDQAIGRAEK-----LLERLRLkpysdryp 139
Cdd:COG2274 544 PASLRRQIGVVLQDVFLF-SGTIRENItlgdpdatdeeiIEA-ARLAGL--HDFIEALPMgydtvVGEGGSN-------- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 140 lhLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYI 219
Cdd:COG2274 612 --LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
....
gi 504696061 220 VEQG 223
Cdd:COG2274 688 VEDG 691
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-238 |
4.35e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 136.36 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpSDKAIRELRQNVGMVFQQ-- 90
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE--PLAKL-NRAQRKAFRRDIQMVFQDsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 --YNlwPHLTVlQNLIEAPCR-VLGLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK10419 100 saVN--PRKTV-REIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 167 EPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQ---GDASCFANPQTDAFKN 238
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKLTFSSPAGRVLQN 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
6.29e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 6.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaKTPSDkAireLRQ 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF-RSPRD-A---QAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQN--LIEAPCRVLGLSKDQAIGRAEKLLERLRLK-----PYSDryplhLSGGQQQRVAIARA 155
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENifLGREPRRGGLIDWRAMRRRARELLARLGLDidpdtPVGD-----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTH---EVevaRKTASRVVYMENGYIVEQGDAS 226
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHrldEV---FEIADRVTVLRDGRLVGTGPVA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-223 |
8.54e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 135.70 E-value: 8.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQ 90
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI------TKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YN---LWPhlTVLQNLIEAPCRvLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:PRK13652 87 PDdqiFSP--TVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 168 PTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
1.63e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 134.76 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnllemprSGTLA---IAGNHFDFAKTPSDKA--- 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITgdkSAGSHIELLGRTVQREgrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 ---IRELRQNVGMVFQQYNLWPHLTVLQN-LIEApcrvLG-----------LSKDQAiGRAEKLLERLRLKPYSDRYPLH 141
Cdd:PRK09984 78 ardIRKSRANTGYIFQQFNLVNRLSVLENvLIGA----LGstpfwrtcfswFTREQK-QRALQALTRVGMVHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 142 LSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETN-ITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
250
....*....|....
gi 504696061 221 EQGDASCFANPQTD 234
Cdd:PRK09984 233 YDGSSQQFDNERFD 246
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-223 |
1.95e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 137.08 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfAKTPSDKairelr 81
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAER------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 qNVGMVFQQYNLWPHLTVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:PRK11000 76 -GVGMVFQSYALYPHLSVAENM-SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 162 VLLFDEPTAALDPEITAQI-VSIIRELAETNITQVIVTH-EVEvARKTASRVVYMENGYIVEQG 223
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHdQVE-AMTLADKIVVLDAGRVAQVG 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-223 |
2.48e-38 |
|
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: 136.40 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQalFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNH-FDFAK---TPSDKairelrQNVGMV 87
Cdd:TIGR02142 9 LGDFS--LDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlFDSRKgifLPPEK------RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 88 FQQYNLWPHLTVLQNLIEAPCRVLGlskDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRARP---SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 168 PTAALDPEITAQIVSIIREL-AETNITQVIVTHEV-EVARkTASRVVYMENGYIVEQG 223
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLhAEFGIPILYVSHSLqEVLR-LADRVVVLEDGRVAAAG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-241 |
2.90e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 133.75 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLAIAGNHFDFAKTPSdkai 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDT---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 78 RELRQNVGMVFQQYNLWPhLTVLQNLIEApCRVLGLsKDQAIgrAEKLLERlRLKPYS------DRypLH-----LSGGQ 146
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGI-KDKQV--LDEAVEK-SLKGASiwdevkDR--LHdsalgLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 147 QQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA- 225
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTk 232
|
250
....*....|....*.
gi 504696061 226 SCFANPQTDAFKNYLS 241
Cdd:PRK14239 233 QMFMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-226 |
1.38e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 132.94 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYG-----AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAgnHFDFAKTPSDKAI 77
Cdd:PRK13643 2 IKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 78 RELRQNVGMVFQ--QYNLWPHlTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRL-KPYSDRYPLHLSGGQQQRVAIAR 154
Cdd:PRK13643 80 KPVRKKVGVVFQfpESQLFEE-TVLKDVAFGP-QNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-223 |
1.54e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.52 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDfakTPSDKAIRELRQNVGMVFQQynlwPH 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LD---TSDEENLWDIRNKAGMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNLIE-----APcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:PRK13633 96 NQIVATIVEedvafGP-ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504696061 172 LDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:PRK13633 175 LDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-241 |
2.48e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 131.44 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLN----LLEMPR-SGTLAIAG-NHFDFAKTPSdka 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlndLIPGFRvEGKVTFHGkNLYAPDVDPV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 irELRQNVGMVFQQYNLWPHlTVLQNLIEAPcRVLGLSkdqaiGRAEKLLER-LR-------LKPYSDRYPLHLSGGQQQ 148
Cdd:PRK14243 88 --EVRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGYK-----GDMDELVERsLRqaalwdeVKDKLKQSGLSLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 149 RVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYM---------ENGYI 219
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYL 237
|
250 260
....*....|....*....|...
gi 504696061 220 VE-QGDASCFANPQTDAFKNYLS 241
Cdd:PRK14243 238 VEfDRTEKIFNSPQQQATRDYVS 260
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-240 |
5.26e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 130.55 E-value: 5.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDKAIRELRQNVGMVFQQYNLWPHL 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNlIEAPCRVLGLSKDQAIGR-AEKLLERLRL-KPYSDRY---PLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:PRK14246 106 SIYDN-IAYPLKSHGIKEKREIKKiVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 173 DPEITAQIVSIIRELaETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS-CFANPQTDAFKNYL 240
Cdd:PRK14246 185 DIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNeIFTSPKNELTEKYV 252
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
9.68e-37 |
|
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: 135.66 E-value: 9.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIREL 80
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING------VDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQynlwPHL---TVLQNL----IEAPcrvlglskDQAIGRAeklLERLRLKPYSDRYP--LH---------L 142
Cdd:COG4988 410 RRQIAWVPQN----PYLfagTIRENLrlgrPDAS--------DEELEAA---LEAAGLDEFVAALPdgLDtplgeggrgL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 143 SGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITqVIVTHEVEVARKtASRVVYMENGYIVEQ 222
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV-ILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
..
gi 504696061 223 GD 224
Cdd:COG4988 553 GT 554
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-221 |
1.07e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 130.72 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGA-----HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfAKTpSDK 75
Cdd:PRK13641 1 MSIKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT-PET-GNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 76 AIRELRQNVGMVFQ--QYNLWPHlTVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAI 152
Cdd:PRK13641 79 NLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGP-KNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVE 221
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-217 |
1.23e-36 |
|
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: 128.71 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVL--NLLemPRSGTLAI--AGNHFDFAkTPSDKAIRELRQN-VGMVFQQ 90
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhDGGWVDLA-QASPREILALRRRtIGYVSQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNLWPHLTVLQnLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPysdR----YPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:COG4778 102 LRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPE---RlwdlPPATFSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 167 EPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-234 |
1.74e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 129.57 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaktpSDKAIRElrQNVGMVFQQYN--L 93
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY----GDYKYRC--KHIRMIFQDPNtsL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQNLiEAPcrvLGLSKD-QAIGRAEKLLERLR----LKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:COG4167 101 NPRLNIGQIL-EEP---LRLNTDlTAEEREERIFATLRlvglLPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 169 TAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTD 234
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKtAEVFANPQHE 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-220 |
2.38e-36 |
|
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: 126.00 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAkTPSDKaireLRQ 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-SPRDA----RRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQqynlwphltvlqnlieapcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03216 76 GIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
2.43e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 134.51 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFY--GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDFAktpsdka 76
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDED------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 irELRQNVGMVFQQynlwPHL---TVLQNL-IEAPcrvlGLSKDQAIgraeKLLERLRLKPYSDRYP--LH--------- 141
Cdd:COG4987 406 --DLRRRIAVVPQR----PHLfdtTLRENLrLARP----DATDEELW----AALERVGLGDWLAALPdgLDtwlgeggrr 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 142 LSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVE 221
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVE 549
|
...
gi 504696061 222 QGD 224
Cdd:COG4987 550 QGT 552
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-223 |
3.55e-36 |
|
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: 126.95 E-value: 3.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPsdkairelRQ 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--------LR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLiEAPCRVLGLSKDqaigRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03268 73 RIGALIEAPGFYPNLTARENL-RLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTH---EVEvarKTASRVVYMENGYIVEQG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHllsEIQ---KVADRIGIINKGKLIEEG 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-240 |
6.28e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.31 E-value: 6.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTpSDKAIRELR-QNVGMVFQQYNLWPHLT 98
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKI-SDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 99 VLQNLIEApcrvLGLSKDQAIGRAEKLLERLR---LKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE 175
Cdd:PRK10070 123 VLDNTAFG----MELAGINAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 176 ITAQIV-SIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTDAFKNYL 240
Cdd:PRK10070 199 IRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPdEILNNPANDYVRTFF 265
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
8.82e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.80 E-value: 8.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQ--ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagnhfdFAKTPSDKAIREL 80
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI------DGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQY-NLWPHLTV-------LQNLIEAPcrvlglSKDQAIgrAEKLLERLRLKPYSDRYPLHLSGGQQQRVAI 152
Cdd:PRK13632 82 RKKIGIIFQNPdNQFIGATVeddiafgLENKKVPP------KKMKDI--IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVI-VTHEVEVARKtASRVVYMENGYIVEQGD 224
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGK 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-223 |
1.13e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.97 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGA-----HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagNHFDFAKTPSDK 75
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 76 AIRELRQNVGMVFQqynlWPHLTVLQNLIE-----APcRVLGLSKDQAIGRAEKLLERLRL-KPYSDRYPLHLSGGQQQR 149
Cdd:PRK13646 79 YIRPVRKRIGMVFQ----FPESQLFEDTVEreiifGP-KNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 150 VAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-240 |
1.75e-35 |
|
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: 125.73 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairelRQ 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ--DITKLPMHK-----RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVF--QQYNLWPHLTVLQNLIeAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEP 160
Cdd:cd03218 74 RLGIGYlpQEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQtDAFKNYL 240
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE-LVRKVYL 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-232 |
2.61e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 127.90 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLEMpRSGTLAIAGNhfDFAKTpSDKAIRELRQNVGMVFQQ--YN 92
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKA-TDGEVAWLGK--DLLGM-KDDEWRAVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTVlQNLIEAPCRVL--GLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:PRK15079 111 LNPRMTI-GEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 170 AALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG-DASCFANPQ 232
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGtYDEVYHNPL 254
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-219 |
5.98e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 125.18 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLaIAGNhfdfakTPSDKAIRELRqnv 84
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT------APLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 gMVFQQYNLWPHLTVLQNLieapcrVLGLSKDQAiGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLL 164
Cdd:PRK11247 85 -LMFQDARLLPWKKVIDNV------GLGLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 165 FDEPTAALDP----EITAQIVSIIRelaETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:PRK11247 157 LDEPLGALDAltriEMQDLIESLWQ---QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-220 |
8.00e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.83 E-value: 8.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtpsDKAIRELRQNVGMVFQQ 90
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLK---NREVPFLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:PRK10908 88 HHLLMDRTVYDN-VAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504696061 171 ALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-204 |
9.69e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.38 E-value: 9.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaKTPSDkAIRelrQ 82
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI-RSPRD-AIA---L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLI--EAPCRVLGLSKDQAIGRAEKLLER--LRLKPysDRYPLHLSGGQQQRVAIARALMM 158
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDRKAARARIRELSERygLDVDP--DAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTH---EV-EVA 204
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHklrEVmAIA 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-223 |
1.92e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.51 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDfaktpsdkaIRELRQNVGMVFQ 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLT---------LESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLWpHLTVLQNL----IEAPcrvlglskDQAIGRAeklLERLRLKPYSDRYP-----------LHLSGGQQQRVAIAR 154
Cdd:COG1132 422 DTFLF-SGTIRENIrygrPDAT--------DEEVEEA---AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-232 |
3.33e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 128.28 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKS-SLLRVLNLLEMP----RSGTLAIAGNHFDFAktpSDKAIRELRQN-VGMVF 88
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHA---SEQTLRGVRGNkIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQ--YNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDR---YPLHLSGGQQQRVAIARALMMEPAVL 163
Cdd:PRK15134 99 QEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 164 LFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASC-FANPQ 232
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATlFSAPT 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-216 |
4.46e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.43 E-value: 4.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnllemprSGTLAiAGNHFDFAKTPSDKAIREL- 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAI-------AGTLS-PAFSASGEVLLNGRRLTALp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 --RQNVGMVFQQYNLWPHLTVLQNLIEA-PCRVlglSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALM 157
Cdd:COG4136 73 aeQRRIGILFQDDLLFPHLSVGENLAFAlPPTI---GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRE-LAETNITQVIVTHEVEVARKtASRVVYMEN 216
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-224 |
5.17e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.68 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtpsdkairelR 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGmvfqqY-----NLWPHLTVLQNLIE-ApcRVLGLSKDQAIGRAEKLLERLRLKPYSDRyPLH-LSGGQQQRVAIAR 154
Cdd:COG4152 71 RRIG-----YlpeerGLYPKMKVGEQLVYlA--RLKGLSKAEAKRRADEWLERLGLGDRANK-KVEeLSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
5.48e-34 |
|
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: 127.61 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEM--PRSGTL--------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 60 --AIAGNHF-----DFAKtPSDKAIRELRQNVGMVFQQ-YNLWPHLTVLQNLIEApCRVLGLSKDQAIGRAEKLLERLRL 131
Cdd:TIGR03269 81 pcPVCGGTLepeevDFWN-LSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 132 KPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEiTAQIV-SIIRELA-ETNITQVIVTHEVEVARKTAS 209
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ-TAKLVhNALEEAVkASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*..
gi 504696061 210 RVVYMENGYIVEQGDAS 226
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPD 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-232 |
1.20e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 127.66 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfakTPSDKAIRELRQNVGMVFQQ--YNLWPHLTVLQNLIE 105
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID---TLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 106 aPCRVLGL-SKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSI 183
Cdd:PRK10261 427 -PLRVHGLlPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 184 IRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQ 232
Cdd:PRK10261 506 LLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPrRAVFENPQ 556
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-217 |
1.35e-33 |
|
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: 121.03 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIRELRQNVGMVFQQYNLWPHL 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-----------KQITEPGPDRMVVFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNLIEAPCRVL-GLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP-- 174
Cdd:TIGR01184 70 TVRENIALAVDRVLpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAlt 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504696061 175 --EITAQIVSIIRelaETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:TIGR01184 150 rgNLQEELMQIWE---EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-223 |
2.53e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 122.22 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktPSDKAIRELRQ 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE-------PVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIeAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-217 |
3.07e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.26 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfakTPSdkAIRelrq 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE---GPG--AER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 nvGMVFQQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAV 162
Cdd:PRK11248 73 --GVVFQNEGLLPWRNVQDN-VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-234 |
3.12e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.89 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSS----LLRVLNllemprsgtlaiAGNHFDFAKTP----SDKAIRELRQNV 84
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN------------SQGEIWFDGQPlhnlNRRQLLPVRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYN--LWPHLTVLQnLIEAPCRV--LGLSKDQAIGRAEKLLERLRLKPYS-DRYPLHLSGGQQQRVAIARALMME 159
Cdd:PRK15134 365 QVVFQDPNssLNPRLNVLQ-IIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 160 PAVLLFDEPTAALDPEITAQIVSIIRELAETN-ITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTD 234
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHqLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCeRVFAAPQQE 520
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-222 |
7.42e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.45 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfakTPSDKAIRELR-QNVGMVFQQYNLWPH 96
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS---KLSSAAKAELRnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEi 176
Cdd:PRK11629 102 FTALEN-VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504696061 177 TAQivSIIRELAETNITQ----VIVTHEVEVARKTaSRVVYMENGYIVEQ 222
Cdd:PRK11629 180 NAD--SIFQLLGELNRLQgtafLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-223 |
1.18e-31 |
|
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: 114.96 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLN--LLEMPRSGTLAIAGnhfdfakTPSDKaiRELRQNVGMVFQQYNLWP 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING-------RPLDK--RSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNL-IEAPCRVlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:cd03213 96 TLTVRETLmFAAKLRG-------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504696061 175 EITAQIVSIIRELAETNITQVIVTHEVEVAR-KTASRVVYMENGYIVEQG 223
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-224 |
1.35e-31 |
|
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: 121.06 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAI-AGNHF-DFAKTPSDKAIReLRQNVGMVFQQ 90
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWvDMTKPGPDGRGR-AKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNLWPHLTVLQNLIEAPCrvLGLSKDQAIGRAEKLL-----ERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLF 165
Cdd:TIGR03269 374 YDLYPHRTVLDNLTEAIG--LELPDELARMKAVITLkmvgfDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 166 DEPTAALDPeITAQIV--SIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:TIGR03269 452 DEPTGTMDP-ITKVDVthSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
2.57e-31 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 114.61 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQ--ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPSdkaiRE 79
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIRQLDP----AD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQynlwPHL---TVLQNLieapcrVLG--LSKDQAIGRAeklLERLRLKPYSDRYPL-----------HLS 143
Cdd:cd03245 76 LRRNIGYVPQD----VTLfygTLRDNI------TLGapLADDERILRA---AELAGVTDFVNKHPNgldlqigergrGLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 144 GGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETnITQVIVTHEVeVARKTASRVVYMENGYIVEQG 223
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-211 |
9.93e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 113.34 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQ--ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfakTPSDKAIR-ELR-QNVGMVF 88
Cdd:PRK10584 19 GEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----HQMDEEARaKLRaKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQYNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK10584 95 QSFMLIPTLNALEN-VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504696061 169 TAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRV 211
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRL 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-224 |
1.31e-30 |
|
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: 113.40 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQy 91
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDI------RDLNLRWLRSQIGLVSQE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 nlwPHL---TVLQNL-----------IEAPCRVLGlskdqaigrAEKLLERLrlkPysDRYPLH-------LSGGQQQRV 150
Cdd:cd03249 86 ---PVLfdgTIAENIrygkpdatdeeVEEAAKKAN---------IHDFIMSL---P--DGYDTLvgergsqLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 151 AIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQGD 224
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-205 |
2.00e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.56 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnHFDFAKTPSDKAIRE-----LRQNVGM 86
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-GARVAYVPQRSEVPDslpltVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 87 vfqqyNLWPHLtvlqnlieAPCRVLGLSKDQAIGRAeklLERLRLKPYSDRyPLH-LSGGQQQRVAIARALMMEPAVLLF 165
Cdd:NF040873 81 -----GRWARR--------GLWRRLTRDDRAAVDDA---LERVGLADLAGR-QLGeLSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504696061 166 DEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVAR 205
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-217 |
2.03e-30 |
|
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: 111.15 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDK-AIRELRQNVGMVFQQYNLWPH 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG-------ADISQwDPNELGDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 lTVLQNLieapcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEI 176
Cdd:cd03246 91 -SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504696061 177 TAQIVSIIRELAETNITQVIVTHEVEVARkTASRVVYMENG 217
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDG 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-223 |
4.02e-30 |
|
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: 111.94 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAH-QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIRE-----LRQNVG 85
Cdd:cd03253 10 YDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG-----------QDIREvtldsLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 86 MVFQQYNLWpHLTVLQNLIEAPcrvLGLSKDQAIGRAEKLLERLRLKPYSDRYP-------LHLSGGQQQRVAIARALMM 158
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGR---PDATDEEVIEAAKAAQIHDKIMRFPDGYDtivgergLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELAeTNITQVIVTHEVEVArKTASRVVYMENGYIVEQG 223
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-224 |
1.04e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.00 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGIN-CFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG-NHFDFAKTPsdkairEL 80
Cdd:PRK13644 2 IRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQ------GI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQynlwPHL-----TVLQNLIEAPcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARA 155
Cdd:PRK13644 76 RKLVGIVFQN----PETqfvgrTVEEDLAFGP-ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEvARKTASRVVYMENGYIVEQGD 224
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGE 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-223 |
1.06e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnllemprSGTLAIAGNHFDFAKTP-SDKAIRE 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-------SGELSPDSGEVRLNGRPlADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQynlwPHLTvlqnlieAPCRV-----LGLS-------KDQAIgrAEKLLERLRLKPYSDRYPLHLSGGQQ 147
Cdd:PRK13548 74 LARRRAVLPQH----SSLS-------FPFTVeevvaMGRAphglsraEDDAL--VAAALAQVDLAHLAGRDYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 148 QRVAIARALM------MEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVI-VTHEVEVARKTASRVVYMENGYIV 220
Cdd:PRK13548 141 QRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIvVLHDLNLAARYADRIVLLHQGRLV 220
|
...
gi 504696061 221 EQG 223
Cdd:PRK13548 221 ADG 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
1.11e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.36 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfAKTPSDKAIRE--L 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELARRRavL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFqqynlwpHLTVLQnLIE---APCRVLGLSKDQAIGRAeklLERLRLKPYSDRYPLHLSGGQQQRVAIARAL- 156
Cdd:COG4559 81 PQHSSLAF-------PFTVEE-VVAlgrAPHGSSAAQDRQIVREA---LALVGLAHLAGRSYQTLSGGEQQRVQLARVLa 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 157 ------MMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:COG4559 150 qlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-241 |
5.91e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.19 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLE-----MPRSGTLAIAGNH-FDFaktpsdKAIRELRQNVG 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSiFNY------RDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 86 MVFQQYNLWPhLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRL-KPYSDRY---PLHLSGGQQQRVAIARALMMEPA 161
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQTDAFKNYL 240
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTeQLFSSPKHAETARYV 262
|
.
gi 504696061 241 S 241
Cdd:PRK14271 263 A 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-223 |
8.30e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.02 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPSDK-----AI 77
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG--LDVATTPSRElakrlAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 78 reLRQNVGMVfqqynlwPHLTVLQnLIEapcrvLG--------LSKD--QAIGRAeklLERLRLKPYSDRYPLHLSGGQQ 147
Cdd:COG4604 80 --LRQENHIN-------SRLTVRE-LVA-----FGrfpyskgrLTAEdrEIIDEA---IAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-219 |
1.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.44 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQY-NLWPH 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL------TEENVWDIRHKIGMVFQNPdNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTV-------LQNLieapcrvlGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:PRK13650 97 ATVeddvafgLENK--------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504696061 170 AALDPEITAQIVSIIRELAETNITQVI-VTHEV-EVArkTASRVVYMENGYI 219
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMTVIsITHDLdEVA--LSDRVLVMKNGQV 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-224 |
1.14e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.09 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLrvlNLLemPR-----SGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQY 91
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLV---NLI--PRfydvdSGRILIDGHDV------RDYTLASLRRQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWpHLTVLQNLIEApcrVLGLSKDQAI--GRAEKLLERLRLKPysDRYP-------LHLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03251 86 FLF-NDTVAENIAYG---RPGATREEVEeaARAANAHEFIMELP--EGYDtvigergVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQGD 224
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
3.06e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.54 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIREL 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-------VPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNLWPHLTVLQNLIeAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEP 160
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-223 |
3.61e-28 |
|
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: 105.47 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYG--AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIREL 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-------VPVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQynlwPHL---TVLQNLieapcrvlglskdqaiGRaekllerlrlkpysdryplHLSGGQQQRVAIARALM 157
Cdd:cd03247 74 SSLISVLNQR----PYLfdtTLRNNL----------------GR-------------------RFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVeVARKTASRVVYMENGYIVEQG 223
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-232 |
3.64e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.87 E-value: 3.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKS-SLLRVLNLLEMP----RSGTLAIAGNHFDFAK--TPSDKAIRELR-QNVGMV 87
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQVIElsEQSAAQMRHVRgADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 88 FQQ--YNLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLkPYSD----RYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQtilsRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANPQ 232
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVeQIFHAPQ 261
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-224 |
4.04e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 109.19 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQalFDITLNCP-EGETLVLlGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNH-FDFAKT---PSDKairelrQNVGMV 87
Cdd:PRK11144 11 GDLC--LTVNLTLPaQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGiclPPEK------RRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 88 FQQYNLWPHLTVLQNLieapcrVLGLSKDQAiGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:PRK11144 82 FQDARLFPHYKVRGNL------RYGMAKSMV-AQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 168 PTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-236 |
4.15e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.32 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFD----------FAK 70
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaraasrrVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 71 TPSDKAIR---ELRQNVGMvfqqyNLWPHLTVLQNLIEAPCRVLglskDQAIGRAEkllerlrLKPYSDRYPLHLSGGQQ 147
Cdd:PRK09536 82 VPQDTSLSfefDVRQVVEM-----GRTPHRSRFDTWTETDRAAV----ERAMERTG-------VAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASC 227
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
250
....*....|.
gi 504696061 228 FANPQT--DAF 236
Cdd:PRK09536 226 VLTADTlrAAF 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-223 |
7.00e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIREL 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD------KPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYnLWPHLTVLQNLIE---APCRVL--GLS-KDQAigRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIAR 154
Cdd:PRK11231 75 ARRLALLPQHH-LTPEGITVRELVAygrSPWLSLwgRLSaEDNA--RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-223 |
8.17e-28 |
|
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: 105.88 E-value: 8.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfakTPSDKAIRELRQnVGMVFQQYN-LWP 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL------VPWKRRKKFLRR-IGVVFGQKTqLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQ--NLIEapcRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALD 173
Cdd:cd03267 109 DLPVIDsfYLLA---AIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 174 PEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03267 186 VVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-223 |
1.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.02 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlAIAGNHFDFAKTPSDKAIRELRQNVGMVFQqynlWP 95
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAIPANLKKIKEVKRLRKEIGLVFQ----FP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNLIE-----APCRvLGLSKDQAIGRAEKLLERLRL-KPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:PRK13645 100 EYQLFQETIEkdiafGPVN-LGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 170 AALDPEITAQIVSIIRELAETNITQVI-VTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIImVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-199 |
1.25e-27 |
|
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: 110.14 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfaktPSDKAIRELRQNVGMVFQQyn 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP------VSSLDQDEVRRRVSVCAQD-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 lwPHL---TVLQNLIEAPcrvlGLSKDQAIGRAeklLERLRLKPYSDRYP--LH---------LSGGQQQRVAIARALMM 158
Cdd:TIGR02868 418 --AHLfdtTVRENLRLAR----PDATDEELWAA---LERVGLADWLRALPdgLDtvlgeggarLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRElAETNITQVIVTH 199
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-223 |
1.38e-27 |
|
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: 105.68 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIA---GNHFDFAKTPSDKAIRE 79
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQY--NLWPHLTVLQNLIEapcRVLGLSkDQAIGR----AEKLLERLRLKP-YSDRYPLHLSGGQQQRVAI 152
Cdd:TIGR02323 84 MRTEWGFVHQNPrdGLRMRVSAGANIGE---RLMAIG-ARHYGNiratAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-223 |
2.62e-27 |
|
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: 104.15 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktpsDKAIREL 80
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 rqNVGMVfqqynlwPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRyPL-HLSGGQQQRVAIARALMME 159
Cdd:cd03220 92 --GGGFN-------PELTGREN-IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL-PVkTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 160 PAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-230 |
3.37e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.58 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRElrq 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTAKIMRE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLieapcrVLG---LSKDQAIGRAEKLLERL-RLKPYSDRYPLHLSGGQQQRVAIARALMM 158
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENL------AMGgffAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIV-EQGDASCFAN 230
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVlEDTGDALLAN 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-223 |
5.32e-27 |
|
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: 103.50 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnlleMPRSGTLAIAGNHFDFAKTPSDKAirELRQNVGMVFQQYNLWP 95
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAI----SGRVEGGGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNLIEAPCRVLGLSKDQAIGRAE---KLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 173 DPEITAQIVSIIRELAETNITqVIVTheVEVAR----KTASRVVYMENGYIVEQG 223
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRI-VILT--IHQPRsdlfRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-223 |
6.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRS---GTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQY-N 92
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG------ITLTAKTVWDIREKVGIVFQNPdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTV-------LQNLieapcrvlGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLF 165
Cdd:PRK13640 96 QFVGATVgddvafgLENR--------AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 166 DEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVArKTASRVVYMENGYIVEQG 223
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-241 |
1.11e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.72 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAktpsDKAIRElrQNVGMVFQ--QYNL 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG----DYSYRS--QRIRMIFQdpSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQnLIEAPCRvlgLSKD-QAIGRAEKLLERLR----LKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK15112 101 NPRQRISQ-ILDFPLR---LNTDlEPEQREKQIIETLRqvglLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 169 TAALDPEITAQIVSIIRELAETN-ITQVIVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYLS 241
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHISDQVLVMHQGEVVERGStADVLASPLHELTKRLIA 251
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-223 |
1.50e-26 |
|
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: 107.35 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQYNLWP 95
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDG------QDLAGLDVQAVRRQLGVVLQNGRLMS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HlTVLQNLIEAPcrvlGLSKDQAIGRAEK--LLERLRLKPYSdrypLH---------LSGGQQQRVAIARALMMEPAVLL 164
Cdd:TIGR03797 541 G-SIFENIAGGA----PLTLDEAWEAARMagLAEDIRAMPMG----MHtvisegggtLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 165 FDEPTAALDpEITAQIVSiiRELAETNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:TIGR03797 612 FDEATSALD-NRTQAIVS--ESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-224 |
1.79e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.55 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKtpsdKAIRELRQNVGMVFQQY 91
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK----RGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLL-----ERLRLKPYSdryplHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALtlvdaQHFRHQPIQ-----CLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 167 EPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-223 |
2.27e-26 |
|
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: 101.92 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELR 81
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI------RDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQynlwPHL---TVLQNL-----------IEAPCRVLGLskDQAIGRAEKLLERLrLKPYSDRyplhLSGGQQ 147
Cdd:cd03254 77 SMIGVVLQD----TFLfsgTIMENIrlgrpnatdeeVIEAAKEAGA--HDFIMKLPNGYDTV-LGENGGN----LSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-240 |
2.30e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.81 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEmPRSGTLAIAGNHFDFAKTPSDKA--IRE 79
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRVEFFNQNIYERRvnLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQYNLWPhLTVLQNlIEAPCRVLG----LSKDQAIGRAEK---LLERLRLKPYsdRYPLHLSGGQQQRVAI 152
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDN-VAYGVKIVGwrpkLEIDDIVESALKdadLWDEIKHKIH--KSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEV-EVARKTASRVVYMEN----GYIVEQGDAS 226
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLhQVSRLSDFTAFFKGNenriGQLVEFGLTK 241
|
250
....*....|....*
gi 504696061 227 -CFANPQTDAFKNYL 240
Cdd:PRK14258 242 kIFNSPHDSRTREYV 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-226 |
2.68e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfAKTPSDKAirELrq 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-KLDHKLAA--QL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLI--EAPCR-VLGLS----KDQAIgRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARA 155
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYigRHLTKkVCGVNiidwREMRV-RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-220 |
3.11e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIRelrqNVGMVFQ--QYN 92
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLPEYKRAK----YIGRVFQdpMMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTVLQNLIEAPCR------VLGLSKDQaigRAE--KLLERL------RLKpysDRYPLhLSGGQQQRVAIARALMM 158
Cdd:COG1101 93 TAPSMTIEENLALAYRRgkrrglRRGLTKKR---RELfrELLATLglglenRLD---TKVGL-LSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-202 |
6.71e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.99 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTpsdkaiRE-LRQN 83
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST------TAaLAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 84 VGMVFQQYNLWPHLTVLQNLI--EAPCRVLGLSKDQAIGRAEKLLERLRLKpYSDRYPL-HLSGGQQQRVAIARALMMEP 160
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYlgQLPHKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLkYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVE 202
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME 201
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-223 |
8.99e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 8.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 6 NGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNH---FDFAKTPSDKAIRELRQ 82
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlRDLYALSEAERRRLLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQ--QYNLWPHLTVLQNLIEapcRVLGLSkDQAIGR----AEKLLERLRLKPYS-DRYPLHLSGGQQQRVAIARA 155
Cdd:PRK11701 90 EWGFVHQhpRDGLRMQVSAGGNIGE---RLMAVG-ARHYGDiratAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-223 |
1.17e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.66 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 11 FYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQ 90
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI------RTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 91 YNLWPHlTVLQNLieapcrvlglskdqAIGRAEKLLERLRL-------------KPysDRYPLH-------LSGGQQQRV 150
Cdd:PRK13657 418 AGLFNR-SIEDNI--------------RVGRPDATDEEMRAaaeraqahdfierKP--DGYDTVvgergrqLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 151 AIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.43e-25 |
|
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: 104.29 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSdkaireL 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS------W 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQynlwPHL---TVLQNLIEAPCRVLGLSKDQAIGRAEkLLERLRLKPYSDRYPL-----HLSGGQQQRVAI 152
Cdd:TIGR02857 395 RDQIAWVPQH----PFLfagTIAENIRLARPDASDAEIREALERAG-LDEFVAALPQGLDTPIgeggaGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYM 214
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-223 |
3.06e-25 |
|
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: 99.10 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQ--ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTpsDKAirEL 80
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH--DLALA--DPA--WL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQyNLWPHLTVLQNLIEApcrvlglskDQAIGRaEKLLERLRLKPYSD---RYPL-----------HLSGGQ 146
Cdd:cd03252 75 RRQVGVVLQE-NVLFNRSIRDNIALA---------DPGMSM-ERVIEAAKLAGAHDfisELPEgydtivgeqgaGLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 147 QQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARkTASRVVYMENGYIVEQG 223
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQG 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-223 |
3.73e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfAKTPSDKAIRElrq 82
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQIARM--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 nvGMV--FQQYNLWPHLTVLQNLIEAPCRVL------GL--------SKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQ 146
Cdd:PRK11300 81 --GVVrtFQHVRLFREMTVIENLLVAQHQQLktglfsGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 147 QQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-231 |
4.47e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.95 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnlleMprsGTLA----IAGN-HFDFAK--TPSDKAIRELR-QNVGMVF 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFAL----M---GLLAangrIGGSaTFNGREilNLPEKELNKLRaEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQ--YNLWPHLTVLQNLIEapcrVL----GLSKDQAIGRAEKLLERLRLKPYSDR---YPLHLSGGQQQRVAIARALMME 159
Cdd:PRK09473 104 QDpmTSLNPYMRVGEQLME----VLmlhkGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 160 PAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA-SCFANP 231
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNArDVFYQP 253
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-226 |
5.72e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 100.59 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 21 ITLNCPEGETLVLLGPSGAGKS-SLLRVLNLLEMP-RSGTLAIAGNHFDFAKTPSdkaiRELRQNVG----MVFQQ--YN 92
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgRVMAEKLEFNGQDLQRISE----KERRNLVGaevaMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRL-KPYS--DRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 170 AALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-223 |
5.78e-25 |
|
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: 102.90 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYG-AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagNHFDFaktpSDKAIREL 80
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL--NGFSL----KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQynlwPHL---TVLQNLIEAPCRvlGLSKD---QAIGRAE--KLLERLRLKpYSDRYPLH---LSGGQQQR 149
Cdd:TIGR01193 547 RQFINYLPQE----PYIfsgSILENLLLGAKE--NVSQDeiwAACEIAEikDDIENMPLG-YQTELSEEgssISGGQKQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 150 VAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNItqVIVTHEVEVARKTaSRVVYMENGYIVEQG 223
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTI--IFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-223 |
6.86e-25 |
|
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: 102.64 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDfaktPSDkaireLRQNVGMVFQQYNL 93
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdiRQID----PAD-----LRRNIGYVPQDPRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WpHLTVLQNL-IEAPcrvlgLSKDQAIGRAEK---LLERLRLKPYSDRYPLH-----LSGGQQQRVAIARALMMEPAVLL 164
Cdd:TIGR03375 551 F-YGTLRDNIaLGAP-----YADDEEILRAAElagVTEFVRRHPDGLDMQIGergrsLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 165 FDEPTAALDPEITAQIVSIIRELAETNiTQVIVTHEVEVArKTASRVVYMENGYIVEQG 223
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVADG 681
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-242 |
1.02e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.85 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 21 ITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQYNLwPHLTVL 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNAL-LGFLPYQGSLKINGIEL------RELDPESWRKHLSWVGQNPQL-PHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 101 QNLieapcrVLGLSK--DQAIgraEKLLERLRLKPYSDRYPLHL-----------SGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:PRK11174 441 DNV------LLGNPDasDEQL---QQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 168 PTAALDPEITAQIVSIIRELAETNiTQVIVTHEVEvARKTASRVVYMENGYIVEQGDASCFANpQTDAFKNYLSH 242
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQ-TTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQ-AGGLFATLLAH 583
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-240 |
1.61e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MSIKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKairel 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE--DITHLPMHK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGM--------VFQQynlwphLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAI 152
Cdd:COG1137 75 RARLGIgylpqeasIFRK------LTVEDN-ILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVevaRKTAS---RVVYMENGYIVEQGDASCFA 229
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNV---RETLGicdRAYIISEGKVLAEGTPEEIL 224
|
250
....*....|.
gi 504696061 230 NPQtDAFKNYL 240
Cdd:COG1137 225 NNP-LVRKVYL 234
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-223 |
1.77e-24 |
|
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: 101.36 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQA--LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTpsDKAirE 79
Cdd:TIGR01846 455 AITFENIRFRYAPDSPevLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDG--VDLAIA--DPA--W 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQyNLWPHLTVLQNLieAPCRVlGLSKDQAI-----GRAEKLLERLRlKPYS---DRYPLHLSGGQQQRVA 151
Cdd:TIGR01846 529 LRRQMGVVLQE-NVLFSRSIRDNI--ALCNP-GAPFEHVIhaaklAGAHDFISELP-QGYNtevGEKGANLSGGQRQRIA 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 152 IARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-223 |
1.94e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.90 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAkTPSdKAirelrQ 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPA-KA-----H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVG--MVFQQYNLWPHLTVLQNLIeapcrvLGLSKDQaigRAEKLLERLrLKPYSDRYPLHLSGG-----QQQRVAIARA 155
Cdd:PRK15439 85 QLGiyLVPQEPLLFPNLSVKENIL------FGLPKRQ---ASMQKMKQL-LAALGCQLDLDSSAGslevaDRQIVEILRG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-223 |
2.19e-24 |
|
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: 100.95 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQYNLWPH 96
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL------ADYTLASLRRQVALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 lTVLQNLieapcrvlGLSKDQAIGRA--EKLLERLRLKPYSDRYPL-----------HLSGGQQQRVAIARALMMEPAVL 163
Cdd:TIGR02203 421 -TIANNI--------AYGRTEQADRAeiERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 164 LFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-233 |
2.24e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAiagnhfdFAKTP-SDKAIRELRQNVGMVFQQ-YNLW 94
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF-------YNNQAiTDDNFEKLRKHIGIVFQNpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHLTV-------LQNLIeapcrvlgLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:PRK13648 97 VGSIVkydvafgLENHA--------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 168 PTAALDPEITAQIVSIIREL-AETNITQVIVTHEVEVARKtASRVVYMENGYIVEQGdascfaNPQT 233
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG------TPTE 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-223 |
8.61e-24 |
|
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: 94.87 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQ--ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaIRE 79
Cdd:cd03244 2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--VDISKIG----LHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQynlwPHL---TVLQNLieAPcrvLGLSKDQAIGRAeklLERLRLKPYSDRYP-----------LHLSGG 145
Cdd:cd03244 76 LRSRISIIPQD----PVLfsgTIRSNL--DP---FGEYSDEELWQA---LERVGLKEFVESLPggldtvveeggENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 146 QQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRElAETNITQVIVTHEVEvARKTASRVVYMENGYIVEQG 223
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFD 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-242 |
8.95e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 8.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfaktpsdKAIRELrqnvGMVFQqy 91
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---------SALLEL----GAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 nlwPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRyPL-HLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:COG1134 101 ---PELTGREN-IYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 171 ALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAScfanpqtDAFKNYLSH 242
Cdd:COG1134 176 VGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE-------EVIAAYEAL 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-199 |
9.12e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.92 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaKTPsdKAIRElrQ 82
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF-NGP--KSSQE--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNLIeapcrvLGLSKDQAIGR---------AEKLLERLRLKPYSDRYPLHLSGGQQQRVAIA 153
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIF------LGREFVNRFGRidwkkmyaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504696061 154 RALMMEPAVLLFDEPTAAL-DPEiTAQIVSIIRELAETNITQVIVTH 199
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtDTE-TESLFRVIRELKSQGRGIVYISH 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-217 |
9.62e-24 |
|
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: 94.46 E-value: 9.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLAIAGNhfdFAKTPSDKAIRE--LRQNV--GMVFQQY 91
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGELEKlSGSVSVPGS---IAYVSQEPWIQNgtIRENIlfGKPFDEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 nlWphltvLQNLIEAPCrvlgLSKDqaigraeklLERLrlkPYSDRYPLH-----LSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:cd03250 96 --R-----YEKVIKACA----LEPD---------LEIL---PDGDLTEIGekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504696061 167 EPTAALDPEITAQIV-SIIRELAETNITQVIVTHEVEVARKtASRVVYMENG 217
Cdd:cd03250 153 DPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-225 |
1.21e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.60 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAiagnhFDFAKTP--SDKAIREL 80
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIL-----FDGENIPamSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNLWPHLTVLQN----------LIEAPCRVLGLSKDQAIGraekllerlrLKPYSDRYPLHLSGGQQQRV 150
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNvayplrehtqLPAPLLHSTVMMKLEAVG----------LRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 151 AIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAET-NITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA 225
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-217 |
7.87e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktpsdkaireLRqnV 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------------LR--I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYNLWPHLTVLQNLIEAPCRVLGLSKD-------------------------QAIG------RAEKLLERLRLKP 133
Cdd:COG0488 64 GYLPQEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefEALGgweaeaRAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 134 -YSDRyPL-HLSGGQQQRVAIARALMMEPAVLLFDEPTAALDpeitaqIVSII---RELAETNITQVIVTHEVEVARKTA 208
Cdd:COG0488 144 eDLDR-PVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEwleEFLKNYPGTVLVVSHDRYFLDRVA 216
|
....*....
gi 504696061 209 SRVVYMENG 217
Cdd:COG0488 217 TRILELDRG 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-220 |
9.05e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 9.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaKTPSDkAIRElrqnvGMVF-----QQYNLW 94
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI-RSPRD-AIRA-----GIAYvpedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHLTVLQNLIEAPCRVLG----LSKDQAIGRAEKLLERLRLKPYSDRYPL-HLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:COG1129 343 LDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504696061 170 AALDPEITAQIVSIIRELAETNITQVIVTHEV-EVARkTASRVVYMENGYIV 220
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAEGKAVIVISSELpELLG-LSDRILVMREGRIV 473
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
1.28e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.05 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFY--GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIRE 79
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-----------QPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 -----LRQNVGMVFQQynlwPHL---TVLQNLI--------EAPCRVL---GLskdqaigraEKLLErlrlkpysDRYPL 140
Cdd:PRK11160 407 yseaaLRQAISVVSQR----VHLfsaTLRDNLLlaapnasdEALIEVLqqvGL---------EKLLE--------DDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 141 ---------HLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAEtNITQVIVTHevevaRKTA--- 208
Cdd:PRK11160 466 nawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH-----RLTGleq 539
|
250
....*....|....*..
gi 504696061 209 -SRVVYMENGYIVEQGD 224
Cdd:PRK11160 540 fDRICVMDNGQIIEQGT 556
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-241 |
2.27e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.07 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSslLRVLNLLEMPRSGTLAIAGN-HFD-FAKTPSD---KAIRELRQNVGMVFQqynlw 94
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRvLLDgKPVAPCAlrgRKIATIMQNPRSAFN----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHLTVLQNLIEApCRVLGLSKDQA----IGRAEKLLERLRLkpySDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTA 170
Cdd:PRK10418 94 PLHTMHTHARET-CLALGKPADDAtltaALEAVGLENAARV---LKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 171 ALDPEITAQIVSIIRELAETNITQV-IVTHEVEVARKTASRVVYMENGYIVEQGD-ASCFANPQTDAFKNYLS 241
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMlLVTHDMGVVARLADDVAVMSHGRIVEQGDvETLFNAPKHAVTRSLVS 242
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-232 |
2.40e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagNHFDFAKTPSDKairELRQNVGMVFQQY 91
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII--DDEDISLLPLHA---RARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 172 LDPEITAQIVSIIRELAETNITQVIVTHEVevaRKTasrVVYMENGYIVEQGDASCFANPQ 232
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNV---RET---LAVCERAYIVSQGHLIAHGTPT 222
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-223 |
2.47e-22 |
|
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: 91.31 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfaktpsdkaiRELRQNVGMVFQQY 91
Cdd:TIGR03740 10 FGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT----------RKDLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVLQNLiEAPCRVLGLSKDqaigRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:TIGR03740 80 PLYENLTARENL-KVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 172 LDPEITAQIVSIIRELAETNITQVIVTH---EVEVarkTASRVVYMENGYIVEQG 223
Cdd:TIGR03740 155 LDPIGIQELRELIRSFPEQGITVILSSHilsEVQQ---LADHIGIISEGVLGYQG 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-226 |
3.28e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.08 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 21 ITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQYNLWPHLTVL 100
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL------TAENVWNLRRKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 101 QNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQI 180
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504696061 181 VSIIRELAET-NITQVIVTHEVEVArKTASRVVYMENGYIVEQGDAS 226
Cdd:PRK13642 180 MRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPS 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-199 |
4.13e-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: 90.11 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIRELRQNVGMVFQQYNLWPHLTVLQNLiEAP 107
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG-------TPLAEQRDEPHENILYLGHLPGLKPELSALENL-HFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 108 CRVLGlSKDQAIgraEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL 187
Cdd:TIGR01189 98 AAIHG-GAQRTI---EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|..
gi 504696061 188 AETNITQVIVTH 199
Cdd:TIGR01189 174 LARGGIVLLTTH 185
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-219 |
5.91e-22 |
|
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: 93.95 E-value: 5.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG---NHFDFaktpsdkaiRELRQNVGMVFQ 89
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlKQWDR---------ETFGKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLWPHlTVLQNLieapCRVLGLSKDQAIGRAEKLLER----LRLKPYSDRY----PLHLSGGQQQRVAIARALMMEPA 161
Cdd:TIGR01842 400 DVELFPG-TVAENI----ARFGENADPEKIIEAAKLAGVheliLRLPDGYDTVigpgGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVArKTASRVVYMENGYI 219
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLL-GCVDKILVLQDGRI 531
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-199 |
7.40e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGmvfQQYNLWPHLTVLQNLiEAP 107
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYLG---HRNAMKPALTVAENL-EFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 108 CRVLGlskdQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIREL 187
Cdd:PRK13539 98 AAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|..
gi 504696061 188 AETNITQVIVTH 199
Cdd:PRK13539 174 LAQGGIVIAATH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
1.07e-21 |
|
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: 88.26 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDKAIR-------ELRQNVGMVfqqyn 92
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK--PVTRRSPRDAIRagiayvpEDRKREGLV----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 lwPHLTVLQNLIeapcrvlglskdqaIGRaekllerlrlkpysdryplHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:cd03215 91 --LDLSVAENIA--------------LSS-------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504696061 173 DPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-224 |
1.93e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAiRELRQNVGMVFQQYN-LW 94
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG------YVPFKRR-KEFARRIGVVFGQRSqLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHLTVLQNLieapcRVL----GLSKDQAIGRAEKLLERLRLKPYSDRyPL-HLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:COG4586 109 WDLPAIDSF-----RLLkaiyRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 170 AALDPEITAQIVSIIREL-AETNITQVIVTH---EVEvarKTASRVVYMENGYIVEQGD 224
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnRERGTTILLTSHdmdDIE---ALCDRVIVIDHGRIIYDGS 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-200 |
4.39e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLNLLEMP---RSGTLAIAGnhfdfakTPSDKaiRELRQNVGMVFQQYNLWPHLTVLQNL 103
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG-------MPIDA--KEMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 104 I-EAPCRvLG--LSKDQAIGRAEKLLERLRLKPYSD------RYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:TIGR00955 121 MfQAHLR-MPrrVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180
....*....|....*....|....*.
gi 504696061 175 EITAQIVSIIRELAETNITQVIVTHE 200
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQ 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-223 |
1.15e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.08 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQYNLW 94
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL------RDYTLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 pHLTVLQNLIEApcRVLGLSKDQaIGRAEKL------LERLR--LKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK11176 430 -NDTIANNIAYA--RTEQYSREQ-IEEAARMayamdfINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 167 EPTAALDPEITAQIVSIIRELaETNITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:PRK11176 506 EATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-225 |
1.15e-20 |
|
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: 90.19 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfaktPSDKaiRELRQNVGMVFQQYNLWPHl 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDR--EELGRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNlIeapCRvLGLSKDQAIGRAEKL------LERLRlkpysDRY-------PLHLSGGQQQRVAIARALMMEPAVLL 164
Cdd:COG4618 421 TIAEN-I---AR-FGDADPEKVVAAAKLagvhemILRLP-----DGYdtrigegGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 165 FDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARkTASRVVYMENGYIVEQGDA 225
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPR 550
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-223 |
1.31e-20 |
|
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: 90.26 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIRE-----LRQNVGMV 87
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG-----------QDIRDvtqasLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 88 FQ---------QYNLW---PHLTvlQNLIEAPCR-------VLGLSK--DQAIGraekllERlRLKpysdryplhLSGGQ 146
Cdd:COG5265 438 PQdtvlfndtiAYNIAygrPDAS--EEEVEAAARaaqihdfIESLPDgyDTRVG------ER-GLK---------LSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 147 QQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVI------VTHevevarktASRVVYMENGYIV 220
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADEILVLEAGRIV 571
|
...
gi 504696061 221 EQG 223
Cdd:COG5265 572 ERG 574
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-205 |
1.37e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLeMPR---SGTLAIAGNHFDFaktpsdKAIRE 79
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQA------SNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 L-RQNVGMVFQQYNLWPHLTVLQNLIeapcrvLG--------LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRV 150
Cdd:PRK13549 79 TeRAGIAIIHQELALVKELSVLENIF------LGneitpggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 151 AIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEV-EVAR 205
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLnEVKA 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-232 |
2.67e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.11 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagnHFDFAKTPSdKAIREL-R 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEI---YWSGSPLKA-SNIRDTeR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 QNVGMVFQQYNLWPHLTVLQNLI---EAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPL-HLSGGQQQRVAIARALM 157
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 158 MEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQ 232
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-226 |
5.09e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLL-RVLNLLemPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQYNLWPH 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNG------RPLSDWSAAELARHRAYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNLieAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMM-------EPAVLLFDEPT 169
Cdd:COG4138 84 MPVFQYL--ALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 170 AALDpeITAQIV--SIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDAS 226
Cdd:COG4138 162 NSLD--VAQQAAldRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-223 |
1.26e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 12 YGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQY 91
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI------QHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWPHLTVlQNLI------EAPCRVLGLSKDQ-AIGRAeklLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLL 164
Cdd:PRK10253 91 TTPGDITV-QELVargrypHQPLFTRWRKEDEeAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 165 FDEPTAALDpeITAQIvSIIRELAETNITQ----VIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK10253 167 LDEPTTWLD--ISHQI-DLLELLSELNREKgytlAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-205 |
1.65e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.09 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagnhfdfaktPSDKairelrqnvGMVF--QQynlwPHL 97
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR----------PAGA---------RVLFlpQR----PYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 tVLQNLIEA---PCRVLGLSkDQAIgraEKLLERLRLKPYSDRypLH--------LSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:COG4178 438 -PLGTLREAllyPATAEAFS-DAEL---REALEAVGLGHLAER--LDeeadwdqvLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504696061 167 EPTAALDPEITAQIVSIIR-ELAETNItqVIVTHEVEVAR 205
Cdd:COG4178 511 EATSALDEENEAALYQLLReELPGTTV--ISVGHRSTLAA 548
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-200 |
2.48e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfDFAKTPSDkairELRQNV 84
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE--DISTLKPE----IYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 85 GMVFQQYNLWPHlTVLQNLIeAPCRVLGLSKDQAIGRAEklLERLRL------KPYSDryplhLSGGQQQRVAIARALMM 158
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLI-FPWQIRNQQPDPAIFLDD--LERFALpdtiltKNIAE-----LSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHE 200
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-214 |
2.62e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 83.39 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 25 CPeGETLVLLGPSGAGKSSLLRVLnllemprSGTlaIAGNHFDFAKTPSD-KAIRELRQNVGMVFQQYNLWPHLTVLQNL 103
Cdd:PLN03211 92 SP-GEILAVLGPSGSGKSTLLNAL-------AGR--IQGNNFTGTILANNrKPTKQILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 104 IEapCRVL----GLSKDQAIGRAEKLLERLRLKP-----YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:PLN03211 162 VF--CSLLrlpkSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504696061 175 EITAQIVSIIRELAETNITQVIVTHEvevarkTASRVVYM 214
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQ------PSSRVYQM 273
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-199 |
2.72e-18 |
|
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: 79.84 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALF---DITLNcpEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIRELRQNVGMVFQQYNL 93
Cdd:cd03231 14 ALFsglSFTLA--AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-------GPLDFQRDSIARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQNLieapcrvLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALD 173
Cdd:cd03231 85 KTTLSVLENL-------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 504696061 174 PEITAQIVSIIRELAETNITQVIVTH 199
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-216 |
3.51e-18 |
|
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: 78.73 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLaiagnhfdfaktpsdkaIRELRQNVGMVFQQynlwPHL 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------------GMPEGEDLLFLPQR----PYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TvlqnlieapcrvLGLSKDQAIgraekllerlrlkpysdrYPLH--LSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE 175
Cdd:cd03223 76 P------------LGTLREQLI------------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504696061 176 ITAQIVSIIRELAETNITqviVTHEVEVaRKTASRVVYMEN 216
Cdd:cd03223 126 SEDRLYQLLKELGITVIS---VGHRPSL-WKFHDRVLDLDG 162
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-219 |
3.76e-18 |
|
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: 80.21 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 14 AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQYNL 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG------KPISQYEHKYLHSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHltVLQNLIE---APCRVLGLSKDQAIGRAEKLLERLRLKPYSD--RYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:cd03248 100 FAR--SLQDNIAyglQSCSFECVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 169 TAALDPEITAQIVSIIRElAETNITQVIVTHEVEVARKtASRVVYMENGYI 219
Cdd:cd03248 178 TSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-223 |
8.17e-18 |
|
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: 78.46 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLempRSGTLAIAGN-HFDfaKTPSDKAIRELRQNVGMVFQQYNLWPHLT 98
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYN--GIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 99 VLQnLIEAPCRVLGlskdqaigraekllerlrlkpysDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITA 178
Cdd:cd03233 100 VRE-TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504696061 179 QIVSIIRELA-ETNITQVI-VTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:cd03233 156 EILKCIRTMAdVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-226 |
1.30e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVL------------------NLLEMPrsgtlaiagnhfdfaktPSDKAire 79
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtsgsilldgeDILELS-----------------PDERA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 lRQNVGMVFQQYNLWPHLTVLQNLIEA--PCRVLGLSKDQAIGRAEKLLERLRLKP-YSDRYpLH--LSGGQQQRVAIAR 154
Cdd:COG0396 76 -RAGIFLAFQYPVEIPGVSVSNFLRTAlnARRGEELSAREFLKLLKEKMKELGLDEdFLDRY-VNegFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 155 ALMMEPAVLLFDEPTAALDpeITA-QIVS-IIRELAETNITQVIVTH------EVEvarktASRVVYMENGYIVEQGDAS 226
Cdd:COG0396 154 MLLLEPKLAILDETDSGLD--IDAlRIVAeGVNKLRSPDRGILIITHyqrildYIK-----PDFVHVLVDGRIVKSGGKE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-199 |
1.62e-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: 80.98 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLnllemprSGTLaiAGNHFDFAKTPS-DKAIRELRqnvGMVFQQYnlwphltvLQNLIE 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIL-------SGEL--KPNLGDYDEEPSwDEVLKRFR---GTELQDY--------FKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 106 --------------APCRVLG-----LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:COG1245 158 geikvahkpqyvdlIPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 504696061 167 EPTAALDpeITAQI--VSIIRELAETNITQVIVTH 199
Cdd:COG1245 238 EPSSYLD--IYQRLnvARLIRELAEEGKYVLVVEH 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-220 |
1.63e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 21 ITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFaKTPSDkAIR-------ELRQNVGMVfqqynl 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-RSPRD-AIRagimlcpEDRKAEGII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 wPHLTVLQNL-IEA-----PCRVLgLSKDQAIGRAEKLLERLRLKPYSDRYPL-HLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK11288 344 -PVHSVADNInISArrhhlRAGCL-INNRWEAENADRFIRSLNIKTPSREQLImNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504696061 167 EPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-223 |
1.80e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAG------NHfdfaktpsdkaiRELRQNVGMVFQ 89
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqyDH------------HYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLWPHlTVLQNLieapcrVLGLS---KDQAIGRAEKLLERLRLKPYSDRYPLH-------LSGGQQQRVAIARALMME 159
Cdd:TIGR00958 563 EPVLFSG-SVRENI------AYGLTdtpDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 160 PAVLLFDEPTAALDPEITaQIVSIIRELAEtnITQVIVTHEVEVARKtASRVVYMENGYIVEQG 223
Cdd:TIGR00958 636 PRVLILDEATSALDAECE-QLLQESRSRAS--RTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-231 |
2.85e-17 |
|
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: 80.83 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfaktpsdKAIRELRQNVGMVFQQYNLWPHLTVLQNLIEA 106
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-------TNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 107 pCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRE 186
Cdd:TIGR01257 1028 -AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504696061 187 LaETNITQVIVTHEVEVARKTASRVVymengyIVEQGDASCFANP 231
Cdd:TIGR01257 1107 Y-RSGRTIIMSTHHMDEADLLGDRIA------IISQGRLYCSGTP 1144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-199 |
3.54e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFY-GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAireL 80
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-------QPTRQA---L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQN-VGMVFQQYNLWPHLTVLQNLIEAPCRV--LGL-----SKDQAIgrAEKLLERLRLKPYSDRYPLHLSGGQQQRVAI 152
Cdd:PRK15056 76 QKNlVAYVPQSEEVDWSFPVLVEDVVMMGRYghMGWlrrakKRDRQI--VTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTH 199
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-199 |
3.83e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.77 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFD-ITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdKAIRELRQnvgmVFQQYNLW-- 94
Cdd:PRK13538 16 LFSgLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-----------EPIRRQRD----EYHQDLLYlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 ------PHLTVLQNLIEApCRVLGLSKDQAIGRAeklLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK13538 81 hqpgikTELTALENLRFY-QRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|.
gi 504696061 169 TAALDPEITAQIVSIIRELAETNITQVIVTH 199
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-203 |
3.87e-17 |
|
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: 77.79 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLnllemprSGTLAiaGNHFDFAKTPS-DKAIRELRqnvGMVFQQYnlwphLTVL----- 100
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGKLK--PNLGKFDDPPDwDEILDEFR---GSELQNY-----FTKLlegdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 101 ------QNLIEAPCRVLG-----LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:cd03236 88 kvivkpQYVDLIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|....
gi 504696061 170 AALDPEITAQIVSIIRELAETNITQVIVTHEVEV 203
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-226 |
4.31e-17 |
|
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: 76.80 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLnlleMPRSGTLAIAGN-HFD----FAKTPSDKAirelRQNVGMVFQqyn 92
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTI----MGHPKYEVTEGEiLFKgediTDLPPEERA----RLGIFLAFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 lwphltvlqnlieAPCRVLGLskdqaigraeKLLERLRLKPYSdryplhLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:cd03217 85 -------------YPPEIPGV----------KNADFLRYVNEG------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 173 DPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVY-MENGYIVEQGDAS 226
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHvLYDGRIVKSGDKE 190
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-221 |
4.87e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.69 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRvlnllemprsgtlAIAGNHFDFAKTPSDK-----------AIRELR 81
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAK-------------AICGVTKDNWRVTADRmrfddidllrlSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 Q----NVGMVFQ--QYNLWPHLTVLQNLIEA-PC--------RVLGLSKDQAIgraeKLLERLRLKPYSD---RYPLHLS 143
Cdd:PRK15093 85 KlvghNVSMIFQepQSCLDPSERVGRQLMQNiPGwtykgrwwQRFGWRKRRAI----ELLHRVGIKDHKDamrSFPYELT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 144 GGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQV-IVTHEVEVARKTASRVVYMENGYIVE 221
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLSQWADKINVLYCGQTVE 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-207 |
5.16e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLaiagnhfdfaktpsdkaIRELRQ 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPH--LTVLQNLIEAPcrvlGLSKDQ---AIGR--AEKLLErlrlkpysdrYPLH-LSGGQQQRVAIAR 154
Cdd:PRK09544 68 RIGYVPQKLYLDTTlpLTVNRFLRLRP----GTKKEDilpALKRvqAGHLID----------APMQkLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIREL-AETNITQVIVTHEVE-VARKT 207
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHlVMAKT 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-223 |
5.91e-17 |
|
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: 76.30 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAH--QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTPsdkaIRE 79
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTIP----LED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQQynlwPHL---TVLQNLieapcRVLGLSKDqaigraEKLLERLRLKPYSdrypLHLSGGQQQRVAIARAL 156
Cdd:cd03369 80 LRSSLTIIPQD----PTLfsgTIRSNL-----DPFDEYSD------EEIYGALRVSEGG----LNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIRELAeTNITQVIVTHEVevaRKTA--SRVVYMENGYIVEQG 223
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYD 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-203 |
6.37e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVL--NLLEMPRSGTLAIAGNHFdfaktPSDKAIRElrqnvgmvfqqyNLWPHL 97
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQF-----GREASLID------------AIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNlIEAPCRVlGLSKDQaigraekllerLRLKPYSdryplHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEiT 177
Cdd:COG2401 111 DFKDA-VELLNAV-GLSDAV-----------LWLRRFK-----ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ-T 171
|
170 180
....*....|....*....|....*...
gi 504696061 178 AQIVS-IIRELA-ETNITQVIVTHEVEV 203
Cdd:COG2401 172 AKRVArNLQKLArRAGITLVVATHHYDV 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
1.27e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGN----HFDfaktpsdkair 78
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvkigYFD----------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 elrQNvgmvfqQYNLWPHLTVLQNLIE-APcrvlGLSKDQAIGRAEKLL---ERLRlKPYSDryplhLSGGQQQRVAIAR 154
Cdd:COG0488 385 ---QH------QEELDPDKTVLDELRDgAP----GGTEQEVRGYLGRFLfsgDDAF-KPVGV-----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 155 ALMMEPAVLLFDEPTAALDPE-ITAqivsIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVE 221
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIEtLEA----LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-217 |
1.62e-16 |
|
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: 73.64 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktpsdkairelrQ 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGmVFQQynlwphltvlqnlieapcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARALMMEPAV 162
Cdd:cd03221 64 KIG-YFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 163 LLFDEPTAALDPEitaQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:cd03221 92 LLLDEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-220 |
5.18e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 1 MS-IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLN-------------------LLEM--PRsgt 58
Cdd:PRK11147 1 MSlISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivaRLQQdpPR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 59 lAIAGNHFDF----------------------AKTPSDKAIRELRQnVGMVFQQYNLWPhltvLQNLIEAPCRVLGLSKD 116
Cdd:PRK11147 78 -NVEGTVYDFvaegieeqaeylkryhdishlvETDPSEKNLNELAK-LQEQLDHHNLWQ----LENRINEVLAQLGLDPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 117 qaigraekllerlrlKPYSDryplhLSGGQQQRVAIARALMMEPAVLLFDEPTAALDpeITAqIVSIIRELAETNITQVI 196
Cdd:PRK11147 152 ---------------AALSS-----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--IET-IEWLEGFLKTFQGSIIF 208
|
250 260
....*....|....*....|....
gi 504696061 197 VTHEVEVARKTASRVVYMENGYIV 220
Cdd:PRK11147 209 ISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-223 |
9.95e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.94 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 19 FDITLNcpEGETLVLLGPSGAGKSSLLRVL--------------------NLLEMprsgtlaiagnhfdfaktpSDKAIR 78
Cdd:COG4170 26 VSLTLN--EGEIRGLVGESGSGKSLIAKAIcgitkdnwhvtadrfrwngiDLLKL-------------------SPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 EL-RQNVGMVFQ--QYNLWPHLTVLQNLIEA-PCRVLGLS----KDQAIGRAEKLLERLRLKPYSD---RYPLHLSGGQQ 147
Cdd:COG4170 85 KIiGREIAMIFQepSSCLDPSAKIGDQLIEAiPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGEC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQV-IVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIlLISHDLESISQWADTITVLYCGQTVESG 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-199 |
1.11e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLnllemprSGTLaiAGNHFDFAKTPS-DKAIRELRqnvGMVFQQYnlwphltvLQNLIE 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKIL-------SGEL--IPNLGDYEEEPSwDEVLKRFR---GTELQNY--------FKKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 106 --------------APCRVLG-----LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK13409 158 geikvvhkpqyvdlIPKVFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|...
gi 504696061 167 EPTAALDPEITAQIVSIIRELAEtNITQVIVTH 199
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-174 |
1.22e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLL------RVLnllempRSGTLAIAGNhfDFAktpsDKA 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEVLGG--DMA----DAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 77 IREL---R-----QNVGMvfqqyNLWPHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQ 148
Cdd:NF033858 70 HRRAvcpRiaympQGLGK-----NLYPTLSVFEN-LDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180
....*....|....*....|....*.
gi 504696061 149 RVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-223 |
1.28e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 75.75 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLAIAGNhfdFAKTPSDKAIRE--LRQNVgmvfqqynLW 94
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVHMKGS---VAYVPQQAWIQNdsLRENI--------LF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHltvlqnlieapcrVLGLSKDQAIGRAEKLLERLRLKPYSDRYPL-----HLSGGQQQRVAIARALMMEPAVLLFDEPT 169
Cdd:TIGR00957 722 GK-------------ALNEKYYQQVLEACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 170 AALDPEITAQIVS--IIRELAETNITQVIVTHEVEVARKTaSRVVYMENGYIVEQG 223
Cdd:TIGR00957 789 SAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
109-223 |
3.74e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.62 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 109 RVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA 188
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110
....*....|....*....|....*....|....*
gi 504696061 189 ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:NF000106 192 RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-221 |
5.96e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 17 ALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnllemprSGTLAiAGN-----HFDfAKTPSDKAIRElRQNVGMVF--Q 89
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYP-HGSyegeiLFD-GEVCRFKDIRD-SEALGIVIihQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLWPHLTVLQNLIeapcrvLG--------LSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPA 161
Cdd:NF040905 86 ELALIPYLSIAENIF------LGnerakrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVE 221
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-200 |
1.54e-14 |
|
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: 72.28 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVlnllemprsgtlaIAGNHFDFaktpSDKAIRELRQNVGMVFQQYNLWPHL 97
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------------MAGVDKDF----NGEARPQPGIKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNLIEAPCRVLGLSK----------------DQAIGRAEKL-----------LER--------LRLKPYsDRYPLHL 142
Cdd:TIGR03719 84 TVRENVEEGVAEIKDALDrfneisakyaepdadfDKLAAEQAELqeiidaadawdLDSqleiamdaLRCPPW-DADVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 143 SGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVsiiRELAETNITQVIVTHE 200
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPGTVVAVTHD 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-220 |
1.75e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfAKTPsdKAIREL--------RQNVGM 86
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT-GLSP--RERRRLgvayipedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 87 VfqqynlwPHLTVLQNLI------EAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPL-HLSGGQQQRVAIARALMME 159
Cdd:COG3845 348 V-------PDMSVAENLIlgryrrPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 160 PAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIV 220
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-174 |
3.77e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 19 FDItlncPEGETLVLLGPSGAGKSSLLRVLN-LLEmPRSGTLAIAGNHFDfaktPSDkaiRELRQNVGMVFQQYNLWPHL 97
Cdd:NF033858 287 FRI----RRGEIFGFLGSNGCGKSTTMKMLTgLLP-ASEGEAWLFGQPVD----AGD---IATRRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 98 TVLQNLiEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:NF033858 355 TVRQNL-ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-217 |
4.62e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.01 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLAIAGNHFDFaKTPSDKaireLRQNVGMV---FQQYNLWP 95
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDI-RNPAQA----IRAGIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNLIEAPC-------RVLGLSKDQAIGRAeklLERLRLKPYSDRYPL-HLSGGQQQRVAIARALMMEPAVLLFDE 167
Cdd:TIGR02633 353 ILGVGKNITLSVLksfcfkmRIDAAAELQIIGSA---IQRLKVKTASPFLPIgRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504696061 168 PTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-219 |
7.30e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAiagnhFDFAKTPSDKAIRELRQnvGMVF-----QQYNLW 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM-----LNGKEINALSTAQRLAR--GLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 phltvlqnlIEAPCR--VLGLSKD-----QAIGRAEKLLERLR----LKPYSDRYPLH-LSGGQQQRVAIARALMMEPAV 162
Cdd:PRK15439 354 ---------LDAPLAwnVCALTHNrrgfwIKPARENAVLERYRralnIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 163 LLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-233 |
7.99e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfakTPSDKAireLRQNVGMVFQQYNLWPHL 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE---SWSSKA---FARKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQnlIEAPCR-----VLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:PRK10575 101 TVRE--LVAIGRypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 173 DPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQT 233
Cdd:PRK10575 179 DIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-221 |
9.62e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfAKTPSDKA------IRELRQNVGMvFQQYNL 93
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVkkgmayITESRRDNGF-FPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQNLIEAPCR-VLGL---SKDQAIgrAEKLLERLRLKPYS-DRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK09700 359 AQNMAISRSLKDGGYKgAMGLfheVDEQRT--AENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504696061 169 TAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVE 221
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-224 |
1.00e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.13 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKSSLLrvlnllemprsgtlAIAGNHFD-------FAKTP-SDKAIRELRQNVGM 86
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLL--------------SLIQRHFDvsegdirFHDIPlTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 87 VFQQynlwPHL---TVLQNLieapcrvlglskdqAIGR----AEKLLERLRLKPYSD---RYP-----------LHLSGG 145
Cdd:PRK10789 394 VSQT----PFLfsdTVANNI--------------ALGRpdatQQEIEHVARLASVHDdilRLPqgydtevgergVMLSGG 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 146 QQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNiTQVIVTHEVEvARKTASRVVYMENGYIVEQGD 224
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR-TVIISAHRLS-ALTEASEILVMQHGHIAQRGN 532
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-217 |
1.29e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLAIAGNHFDFAKTPSDKAIRElRQNVGMVFQQYNLWpHL 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTLEGKVHWSNKNESEPSFEATRSRN-RYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNLI-EAPcrvLGLSKDQAIGRAEKLLERLRLKPYSDRYPL-----HLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:cd03290 94 TVEENITfGSP---FNKQRYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504696061 172 LDPEITAQIVS--IIRELAETNITQVIVTHEVEVARKtASRVVYMENG 217
Cdd:cd03290 171 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-231 |
3.20e-13 |
|
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: 67.05 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDF------AKTPSdkAIRELRQNVGMVFQQYNLWphltvl 100
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYkpqyikADYEG--TVRDLLSSITKDFYTHPYF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 101 QNLIEAPcrvlglskdqaigraekllerLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQI 180
Cdd:cd03237 96 KTEIAKP---------------------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504696061 181 VSIIRELAE-TNITQVIVTHEVEVARKTASRVvymengyIVEQGDAS--CFANP 231
Cdd:cd03237 155 SKVIRRFAEnNEKTAFVVEHDIIMIDYLADRL-------IVFEGEPSvnGVANP 201
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-215 |
5.52e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfaKTPSDKAirelrQNVGMVFQQYNLWPHLTVLQNLiEAP 107
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT----ATRGDRS-----RFMAYLGHLPGLKADLSTLENL-HFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 108 CRVLGLSKDQAIGRAeklLERLRLKPYSDRYPLHLSGGQQQRVAIARaLMMEPAVL-LFDEPTAALDPEITAQIVSIIRE 186
Cdd:PRK13543 107 CGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEGITLVNRMISA 182
|
170 180
....*....|....*....|....*....
gi 504696061 187 LAETNITQVIVTHEVEVARKTASRVVYME 215
Cdd:PRK13543 183 HLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-226 |
7.76e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNC----PEGETLVLLGPSGAGKSSLLRvlnllemprsgtlAIAGN--HFDFAKT--------PSDKAIREL 80
Cdd:TIGR00956 70 DTKTFDILKPMdgliKPGELTVVLGRPGSGCSTLLK-------------TIASNtdGFHIGVEgvitydgiTPEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNLWPHLTVLQNL-IEAPC-----RVLGLSKDQaigRAEKL---------LERLRLKPYSDRYPLHLSGG 145
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLdFAARCktpqnRPDGVSREE---YAKHIadvymatygLSHTRNTKVGNDFVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 146 QQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEV-EVARKTASRVVYMENGYIVEQG 223
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAnILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQIYFG 293
|
...
gi 504696061 224 DAS 226
Cdd:TIGR00956 294 PAD 296
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-217 |
1.55e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfaktpsdKAIRELRQNVGMVfQQYNLWPHLTVLQNLIEAP 107
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-------TNISDVHQNMGYC-PQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 108 CRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE----ITAQIVSI 183
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQarrmLWNTIVSI 2116
|
170 180 190
....*....|....*....|....*....|....
gi 504696061 184 IRElaetNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:TIGR01257 2117 IRE----GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-223 |
2.09e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 14 AHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVL--NLLEMPRSGTLAIAGN---------HFDFAKTPSDKAIRELRQ 82
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVTGDvtlngeplaAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNL-----WPHltvlqnlieapCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARAL- 156
Cdd:PRK13547 93 QPAFAFSAREIvllgrYPH-----------ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 157 --------MMEPAVLLFDEPTAALDPEITAQIVSIIRELA-ETNITQVIVTHEVEVARKTASRVVYMENGYIVEQG 223
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-197 |
2.49e-12 |
|
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: 65.96 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLaiagnhfDFAKTPSDKAirelrqnvgmvfqQYnLWP--HLTVLQNLI 104
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------DEDLKISYKP-------------QY-ISPdyDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 105 EAPCRVLGLSKDQaigraEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSII 184
Cdd:COG1245 424 SANTDDFGSSYYK-----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170
....*....|...
gi 504696061 185 RELAETNITQVIV 197
Cdd:COG1245 499 RRFAENRGKTAMV 511
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-202 |
9.62e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFakTPSDKAireLRQNVGMVFQQYNLWP 95
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEA---LENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQN--LIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALD 173
Cdd:PRK10982 87 QRSVMDNmwLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180
....*....|....*....|....*....
gi 504696061 174 PEITAQIVSIIRELAETNITQVIVTHEVE 202
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYISHKME 195
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-225 |
1.52e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLL-RVLNLLemPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQYNLWPH 96
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAG------QPLEAWSAAELARHRAYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNLieAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARA-LMMEPAV------LLFDEPT 169
Cdd:PRK03695 84 MPVFQYL--TLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 170 AALDpeiTAQIV---SIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDA 225
Cdd:PRK03695 162 NSLD---VAQQAaldRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-186 |
3.85e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 5 LNGINCFYGAHQALF--DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDfaktpsdKAIRELRQ 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLlqQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-------KDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 NVGMVFQQYNLWPHLTVLQNlieapCRVLGLSKDQAIGRAEkLLERLRLKPYSDrYPLHL-SGGQQQRVAIARALMMEPA 161
Cdd:PRK13540 75 QLCFVGHRSGINPYLTLREN-----CLYDIHFSPGAVGITE-LCRLFSLEHLID-YPCGLlSSGQKRQVALLRLWMSKAK 147
|
170 180
....*....|....*....|....*
gi 504696061 162 VLLFDEPTAALDPEITAQIVSIIRE 186
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQE 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-219 |
3.99e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLAIAGNHFDfAKTPSDKA------IRELRQNVGMVFQ--- 89
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVL-YGALPRtSGYVTLDGHEVV-TRSPQDGLangivyISEDRKRDGLVLGmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLwpHLTVLQNLIEAPCRVLGLSKDQAIGRAEKLLErlrLK-PYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK10762 348 KENM--SLTALRYFSRAGGSLKHADEQQAVSDFIRLFN---IKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 169 TAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-201 |
6.04e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLaiagnhfDFAKTPSDKAirelrqnvgmvfqQYnLWP--HLTVLQNLI 104
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------DPELKISYKP-------------QY-IKPdyDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 105 EAPCRVlglskDQAIGRAEkLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSII 184
Cdd:PRK13409 423 SITDDL-----GSSYYKSE-IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170
....*....|....*...
gi 504696061 185 RELAETN-ITQVIVTHEV 201
Cdd:PRK13409 497 RRIAEEReATALVVDHDI 514
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-223 |
6.34e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVfQQYNLWPHL 97
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG------RPLSSLSHSVLRQGVAMV-QQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNLIeapcrvlgLSKDQAIGRAEKLLERLRLKPYSDRYP--LH---------LSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PRK10790 430 TFLANVT--------LGRDISEEQVWQALETVQLAELARSLPdgLYtplgeqgnnLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696061 167 EPTAALDP---EITAQIVSIIRElaetNITQVIVTHE----VEvarktASRVVYMENGYIVEQG 223
Cdd:PRK10790 502 EATANIDSgteQAIQQALAAVRE----HTTLVVIAHRlstiVE-----ADTILVLHRGQAVEQG 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-240 |
6.71e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 138 YPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE----ITAQIVSIIRELAETNITqviVTHEVEVARKTASRVVY 213
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIIT---IAHRIASIKRSDKIVVF 1431
|
90 100 110
....*....|....*....|....*....|.
gi 504696061 214 M---ENGYIVE-QGDASCFANPQTDAFKNYL 240
Cdd:PTZ00265 1432 NnpdRTGSFVQaHGTHEELLSVQDGVYKKYV 1462
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-200 |
7.87e-11 |
|
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: 59.18 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMP--RSGTLAIAGNhfdfaktPSDKairELRQNVGMVFQQYNL 93
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGR-------PLDK---NFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 94 WPHLTVLQNL-IEAPCRVLGLSkdqaigraekllerlrlkpysdryplhlsggQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:cd03232 91 SPNLTVREALrFSALLRGLSVE-------------------------------QRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180
....*....|....*....|....*...
gi 504696061 173 DPEITAQIVSIIRELAETNITQVIVTHE 200
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-199 |
8.12e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 59.64 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFYGAHQALFDITLNcpegetlVLLGPSGAGKSSLLRVLnllemprsgTLAIAGNHFDFAKTPSDKAIRELR 81
Cdd:COG0419 4 RLRLENFRSYRDTETIDFDDGLN-------LIVGPNGAGKSTILEAI---------RYALYGKARSRSKLRSDLINVGSE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 Q-NVGMVF----QQYNL-WPHLTVLQNLIEAPC-------RVLGLSK-DQAIGRAEKL----------------LERLRL 131
Cdd:COG0419 68 EaSVELEFehggKRYRIeRRQGEFAEFLEAKPSerkealkRLLGLEIyEELKERLKELeealesaleelaelqkLKQEIL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 132 KPYSDRYPLH-LSGGQQQRVAIARALMmepavLLFDepTAALDPEITAQIVSIIRELAetnitqvIVTH 199
Cdd:COG0419 148 AQLSGLDPIEtLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-199 |
9.50e-11 |
|
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: 61.30 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIagnhfdfaktPSDKAIRELRQNvgmvfqqynlwPHLTV 99
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----------PAKGKLFYVPQR-----------PYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 100 --LQNLIEAPCRVLGLsKDQAIGRA--EKLLERLRLKPYSDR---------YPLHLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:TIGR00954 529 gtLRDQIIYPDSSEDM-KRRGLSDKdlEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|...
gi 504696061 167 EPTAALDPEITAQIVSIIRELaetNITQVIVTH 199
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-229 |
9.87e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLEMPRSGTLAiagnHFDFAKTPSDKAIRE--LRQNVgMVFQQYN-- 92
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEISEGRVWA----ERSIAYVPQQAWIMNatVRGNI-LFFDEEDaa 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 -LWPHLTVLQnlIEAPCRVLGLSKDQAIGraEKllerlrlkpysdryPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:PTZ00243 751 rLADAVRVSQ--LEADLAQLGGGLETEIG--EK--------------GVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 172 LDPEITAQIVS--IIRELAETniTQVIVTHEVEVARKtASRVVYMENGYIVEQGDASCFA 229
Cdd:PTZ00243 813 LDAHVGERVVEecFLGALAGK--TRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFM 869
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-205 |
1.03e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfakTPSDKAIRELRQNVGMVFQ---------- 89
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH-----NLKDINLKWWRSKIGVVSQdpllfsnsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 ---QYNLWP--HLTVLQN--------------------------------------LIEAPCRVLGLSKDQAIGRAEKLL 126
Cdd:PTZ00265 478 nniKYSLYSlkDLEALSNyynedgndsqenknkrnscrakcagdlndmsnttdsneLIEMRKNYQTIKDSEVVDVSKKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 127 ERLRLKPYSDRYPL-------HLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELA--ETNITqVIV 197
Cdd:PTZ00265 558 IHDFVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRIT-III 636
|
....*...
gi 504696061 198 THEVEVAR 205
Cdd:PTZ00265 637 AHRLSTIR 644
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-219 |
1.09e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 27 EGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLAIAGNHFDFaKTPSDkAIRelrQNVGMVFQ---QYNLWPHLTVLQN 102
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKI-RNPQQ-AIA---QGIAMVPEdrkRDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 103 LIEAP----CRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPL-HLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEIT 177
Cdd:PRK13549 362 ITLAAldrfTGGSRIDDAAELKTILESIQRLKVKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504696061 178 AQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYI 219
Cdd:PRK13549 442 YEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-199 |
1.78e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHfdfaktpsdkairelrqNVGMVFQQYNLWP 95
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI-----------------KVGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 96 HLTVLQNLIEAPCRVLGLSK----------------DQAIGRAEKL---------------LER----LRLKPySDRYPL 140
Cdd:PRK11819 84 EKTVRENVEEGVAEVKAALDrfneiyaayaepdadfDALAAEQGELqeiidaadawdldsqLEIamdaLRCPP-WDAKVT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 141 HLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEitaqivSII---RELAETNITQVIVTH 199
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE------SVAwleQFLHDYPGTVVAVTH 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-223 |
1.91e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPRSGT--LAIAGNhfdFAKTPSDKAI--RELRQNV--GMVFQQY 91
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETssVVIRGS---VAYVPQVSWIfnATVRENIlfGSDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 NLWphltvlqnlieapcrvlglskdQAIGrAEKLLERLRLKPYSDRYPL-----HLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PLN03232 709 RYW----------------------RAID-VTALQHDLDLLPGRDLTEIgergvNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 167 EPTAALDPEITAQIV-SIIRELAETNiTQVIVTHEVEVArKTASRVVYMENGYIVEQG 223
Cdd:PLN03232 766 DPLSALDAHVAHQVFdSCMKDELKGK-TRVLVTNQLHFL-PLMDRIILVSEGMIKEEG 821
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-234 |
5.79e-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: 59.15 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLnllemprSGTLaiagnhfdfakTPSDKAIRElRQNVGMVFQQYNLWPHl 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI-------MGEL-----------EPSEGKIKH-SGRISFSPQTSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNLIeapcrvLGLSKDQ----AIGRAEKLLERLRLKPYSDRYPL-----HLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:TIGR01271 502 TIKDNII------FGLSYDEyrytSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 169 TAALDPEITAQIV-SIIRELAeTNITQVIVTHEVEVARKtASRVVYMENGYIVEQGDASCFANPQTD 234
Cdd:TIGR01271 576 FTHLDVVTEKEIFeSCLCKLM-SNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRPD 640
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
3-223 |
6.26e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCfygahQALFDITLNCPEGETLVLLGPSGAGKSSLlrVLNLLEmpRSGTLAIAgnhfDFAKTPSDKAIRELRQ 82
Cdd:cd03238 1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI----SFLPKFSRNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 nvgmvfqqynlwphltvLQNLIEapcrvLGLskdqaigraekllERLRLkpysDRYPLHLSGGQQQRVAIARALMMEP-- 160
Cdd:cd03238 68 -----------------LQFLID-----VGL-------------GYLTL----GQKLSTLSGGELQRVKLASELFSEPpg 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 161 AVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVArKTASRVVYM------ENGYIVEQG 223
Cdd:cd03238 109 TLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-223 |
6.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMP-RSGTLAIagnhfdfaktpsdkaireLRQNVGMVFQQYNLWpH 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPpRSDASVV------------------IRGTVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNLIeapcrvLGLSKD-----QAIgRAEKLLERLRLKPYSDRYPL-----HLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:PLN03130 693 ATVRDNIL------FGSPFDperyeRAI-DVTALQHDLDLLPGGDLTEIgergvNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 167 EPTAALDPEITAQIVS--IIRELAETniTQVIVTHEVEVARKTaSRVVYMENGYIVEQG 223
Cdd:PLN03130 766 DPLSALDAHVGRQVFDkcIKDELRGK--TRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-206 |
1.02e-09 |
|
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: 56.46 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDitlncpEGETLvLLGPSGAGKSSLLRVLNLL---EMPRSGTlaiaGNHFDfaktPSDKAIRE 79
Cdd:cd03240 4 LSIRNIRSFHERSEIEFF------SPLTL-IVGQNGAGKTTIIEALKYAltgELPPNSK----GGAHD----PKLIREGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 80 LRQNVGMVFQ-----QYNLWPHLTVLQNLIEapCRvlglskdQaiGRAEKLLERLRlkpysDRyplhLSGGQQQ------ 148
Cdd:cd03240 69 VRAQVKLAFEnangkKYTITRSLAILENVIF--CH-------Q--GESNWPLLDMR-----GR----CSGGEKVlaslii 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 149 RVAIARALMMEPAVLLFDEPTAALDPE-ITAQIVSIIRELAETNITQVIV-THEVEVARK 206
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQLIViTHDEELVDA 188
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-239 |
1.21e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaktpsdkairelrqNVGMVFQQYNLW 94
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------------------SAALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 95 PHLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDP 174
Cdd:PRK13545 98 GQLTGIEN-IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 175 EITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGDASCFANPQTDAFKNY 239
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-242 |
1.33e-09 |
|
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: 56.79 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSL----LRVLNLlemprSGTLAIAGNHFDfaKTPsdkaIRELRQNVGMVF 88
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNT-----EGDIQIDGVSWN--SVP----LQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQYNLWPHlTVLQNLieapcRVLGLSKDQAIGraeKLLERLRLKPYSDRYPLHL-----------SGGQQQRVAIARALM 157
Cdd:cd03289 84 QKVFIFSG-TFRKNL-----DPYGKWSDEEIW---KVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 158 MEPAVLLFDEPTAALDPeITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGyiVEQGDASCFANPQTDAFK 237
Cdd:cd03289 155 SKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENK--VRQYDSIQKLLNEKSHFK 231
|
....*
gi 504696061 238 NYLSH 242
Cdd:cd03289 232 QAISP 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-221 |
1.49e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 29 ETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhFDFAKTpsdkAIRELRQNVGMVFQQYNLWPHlTVLQNLieAPc 108
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKF----GLMDLRKVLGIIPQAPVLFSG-TVRFNL--DP- 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 109 rvLGLSKDQAIGRAeklLERLRLKPYSDRYPLHL-----------SGGQQQRVAIARALMMEPAVLLFDEPTAALDPEIT 177
Cdd:PLN03130 1336 --FNEHNDADLWES---LERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504696061 178 AQIVSIIRELAETnITQVIVTHEVEVARKtASRVVYMENGYIVE 221
Cdd:PLN03130 1411 ALIQKTIREEFKS-CTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-217 |
1.51e-09 |
|
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: 56.79 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 10 CFYGAhQALFDITLNCPEGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLAIAGnhfdfaktpsdkairelrqNVGMVF 88
Cdd:cd03291 46 CLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELE-PSEGKIKHSG-------------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQYNLWPHlTVLQNLIeapcrvLGLSKDQ----AIGRAEKLLERLRLKPYSDRYPL-----HLSGGQQQRVAIARALMME 159
Cdd:cd03291 105 QFSWIMPG-TIKENII------FGVSYDEyrykSVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 160 PAVLLFDEPTAALDPEITAQIV-SIIRELAeTNITQVIVTHEVEVARKtASRVVYMENG 217
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIFeSCVCKLM-ANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-242 |
1.74e-09 |
|
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: 57.61 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 13 GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLAIAGNHFDfaktpsDKAIRELRQNVGMVFQQY- 91
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQIDGVSWN------SVTLQTWRKAFGVIPQKVf 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 92 --------NLWPHLTVlqnlieapcrvlglsKDQAIGraeKLLERLRLKPYSDRYP-----------LHLSGGQQQRVAI 152
Cdd:TIGR01271 1303 ifsgtfrkNLDPYEQW---------------SDEEIW---KVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 153 ARALMMEPAVLLFDEPTAALDPeITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGyiVEQGDASCFANPQ 232
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSS--VKQYDSIQKLLNE 1441
|
250
....*....|
gi 504696061 233 TDAFKNYLSH 242
Cdd:TIGR01271 1442 TSLFKQAMSA 1451
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-197 |
2.83e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 15 HQALFDI----TLNCPE-----GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAiagNHFDfakTPSDKAIRELRQNVG 85
Cdd:PRK10938 7 SQGTFRLsdtkTLQLPSltlnaGDSWAFVGANGSGKSALARALAGELPLLSGERQ---SQFS---HITRLSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 86 MVFQQYN---LWPH-----LT---VLQNLIEAPCRVLGLSKDQAIgraEKLLERlRLKpysdryplHLSGGQQQRVAIAR 154
Cdd:PRK10938 81 DEWQRNNtdmLSPGeddtgRTtaeIIQDEVKDPARCEQLAQQFGI---TALLDR-RFK--------YLSTGETRKTLLCQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504696061 155 ALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIV 197
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-217 |
4.01e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 4.01e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 142 LSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENG 217
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-217 |
4.05e-09 |
|
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: 55.78 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNCPEGETlVLLGPSGAGKSSLLRVLNLLeMPRSGTLAIAGNHFDFAKTPSDK------------------------ 75
Cdd:COG3593 16 DLSIELSDDLT-VLVGENNSGKSSILEALRLL-LGPSSSRKFDEEDFYLGDDPDLPeieieltfgsllsrllrlllkeed 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 76 ------AIRELRQNVGMVFQQYNlwphlTVLQNLIEAPCRVLGLSKDQAIGRAEKLLERLRLK-PYSDRYPLHLSG-GQQ 147
Cdd:COG3593 94 keeleeALEELNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRiEDGKELPLDRLGsGFQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 148 QRVAIA--RALMM-----EPAVLLFDEPTAALDPEITAQIVSIIRELAETNiTQVIV-THEVEVARKT-ASRVVYMENG 217
Cdd:COG3593 169 RLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKP-NQVIItTHSPHLLSEVpLENIRRLRRD 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-215 |
4.44e-09 |
|
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: 54.12 E-value: 4.44e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 142 LSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNI-TQVIVTHEVEVARKTASRVVYME 215
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-236 |
5.75e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 2 SIKLNGINCFY--GAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVL-NLLEMPRsGTLAIAGnhFDFAKTpsdkAIR 78
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfRIVELEK-GRIMIDD--CDVAKF----GLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 79 ELRQNVGMVFQQYNLWPHlTVLQNLieapcRVLGLSKDQAIGRAeklLERLRLKPYSDRYPLHL-----------SGGQQ 147
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSG-TVRFNI-----DPFSEHNDADLWEA---LERAHIKDVIDRNPFGLdaevseggenfSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETnITQVIVTHEVEVARKtASRVVYMENGYIVEQGDASC 227
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
....*....
gi 504696061 228 FANPQTDAF 236
Cdd:PLN03232 1456 LLSRDTSAF 1464
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-226 |
1.39e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFdfaktpSDKAIRELRQNVGMVFQQYNLWPHl 97
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI------AKIGLHDLRFKITIIPQDPVLFSG- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 TVLQNLieAPcrvLGLSKDQAIGRAeklLERLRLKPYSDRYPL-----------HLSGGQQQRVAIARALMMEPAVLLFD 166
Cdd:TIGR00957 1375 SLRMNL--DP---FSQYSDEEVWWA---LELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 167 EPTAALDPEITAQIVSIIRELAETnITQVIVTHEVEVARKTaSRVVYMENGYIVEQGDAS 226
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPS 1504
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-224 |
1.88e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 9 NCFYgahqALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNhfdfaktPSDKAIrelrqNVGMVF 88
Cdd:PRK13546 35 KTFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------VSVIAI-----SAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QqynlwphLTVLQNlIEAPCRVLGLSKDQAIGRAEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEP 168
Cdd:PRK13546 99 Q-------LTGIEN-IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 169 TAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGYIVEQGD 224
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
19-221 |
2.27e-08 |
|
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: 54.03 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 19 FDITLNcpEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfakTPSDKAIRE-LRQNVGMVFQQYNLWPHL 97
Cdd:COG4615 351 IDLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-------QPVTADNREaYRQLFSAVFSDFHLFDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 tvlqnlieapcrvLGLSKDQAIGRAEKLLERLRLK---PYSDRY--PLHLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:COG4615 422 -------------LGLDGEADPARARELLERLELDhkvSVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQ 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 173 DP--------EitaqivsIIRELAETNITQVIVTH-----EVevarktASRVVYMENGYIVE 221
Cdd:COG4615 489 DPefrrvfytE-------LLPELKARGKTVIAISHddryfDL------ADRVLKMDYGKLVE 537
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-204 |
2.76e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVlnllemprsgtlaIAGNHFD--------FAKTP-S 73
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-------------ITGDHPQgysndltlFGRRRgS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 74 DKAIRELRQNVGMVFQQYnlwpHL------TVLQNLIEAPCRVLGLSK---DQAIGRAEKLLERLRLKPYSDRYPLH-LS 143
Cdd:PRK10938 328 GETIWDIKKHIGYVSSSL----HLdyrvstSVRNVILSGFFDSIGIYQavsDRQQKLAQQWLDILGIDKRTADAPFHsLS 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504696061 144 GGQQQRVAIARALMMEPAVLLFDEPTAALDPeITAQIV-SIIRELAETNITQVI-VTHEVEVA 204
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDP-LNRQLVrRFVDVLISEGETQLLfVSHHAEDA 465
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-217 |
4.99e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLR-VLNLLEMPRSGTLAIAGNHFdfaktpsdkairelrqnvgmvfqqynlwphltvlqnliea 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDI---------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 107 pcrvlglskdqaigraEKLLERLRLKPYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIR- 185
Cdd:smart00382 42 ----------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEl 105
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504696061 186 -----ELAETNITQVIVTHEVEVARK-----TASRVVYMENG 217
Cdd:smart00382 106 rllllLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-174 |
8.56e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLNcpEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGnhfdfaKTPSDKAIRELRQNVGMVFQQYNLWPHLTV 99
Cdd:PRK10522 343 NLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG------KPVTAEQPEDYRKLFSAVFTDFHLFDQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 100 LQnlieapcrvlGLSKDQAIgrAEKLLERLRLK--------PYSDrypLHLSGGQQQRVAIARALMMEPAVLLFDEPTAA 171
Cdd:PRK10522 415 PE----------GKPANPAL--VEKWLERLKMAhkleledgRISN---LKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
...
gi 504696061 172 LDP 174
Cdd:PRK10522 480 QDP 482
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-199 |
3.39e-07 |
|
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: 50.08 E-value: 3.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696061 129 LRLKPYSDRYPL---HLSGGQQQ---RVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNItQVIV-TH 199
Cdd:pfam13304 221 LILLENGGGGELpafELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGA-QLILtTH 297
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
122-189 |
5.49e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 5.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696061 122 AEKLLERLRLK-PYSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAE 189
Cdd:NF040905 384 AEEYRKKMNIKtPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAA 452
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-223 |
5.58e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSL----------LRVLNLL---------EMPR---------SGTLAIAGNHFdfA 69
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLsayarqflgQMDKpdvdsieglSPAIAIDQKTT--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 70 KTPsdkairelRQNVGMVFQQYNLWphltvlqnlieapcRVLgLSKDQAIGRAEKL----LERLRLkpysDRYPLHLSGG 145
Cdd:cd03270 89 RNP--------RSTVGTVTEIYDYL--------------RLL-FARVGIRERLGFLvdvgLGYLTL----SRSAPTLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 146 QQQRVAIARALMMEPAVLL--FDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARkTASRVVYM------ENG 217
Cdd:cd03270 142 EAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHGG 220
|
....*.
gi 504696061 218 YIVEQG 223
Cdd:cd03270 221 EIVAQG 226
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
4-218 |
5.96e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.80 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 4 KLNGINCFYGAHQalFDITLnCPEGETLVLLGPSGAGKSSLLRVLnllemprsgTLAIAGNHFDFAKTPSDKAIR---EL 80
Cdd:cd03279 7 ELKNFGPFREEQV--IDFTG-LDNNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQENLRSVFapgED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 81 RQNVGMVFQQYNlwphltvLQNLIEapcRVLGLSKDQAI-------GRAEKLLERlrlkPYSDryplhLSGGQQQRVAIA 153
Cdd:cd03279 75 TAEVSFTFQLGG-------KKYRVE---RSRGLDYDQFTrivllpqGEFDRFLAR----PVST-----LSGGETFLASLS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 154 RALMMEPAV---------LLF-DEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYMENGY 218
Cdd:cd03279 136 LALALSEVLqnrggarleALFiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-200 |
6.08e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVLNllemPRSGTLAIAGNHFDFAKTPSDKAireLRQNVGMVFQQYNLWPHLTVLQNLIEA- 106
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA----ERVTTGVITGGDRLVNGRPLDSS---FQRSIGYVQQQDLHLPTSTVRESLRFSa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 107 ----PCRVLGLSKDQAIgraEKLLERLRLKPYSDRY----PLHLSGGQQQRVAIARALMMEPAVLLF-DEPTAALDPEIT 177
Cdd:TIGR00956 862 ylrqPKSVSKSEKMEYV---EEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTA 938
|
170 180
....*....|....*....|...
gi 504696061 178 AQIVSIIRELAETNITQVIVTHE 200
Cdd:TIGR00956 939 WSICKLMRKLADHGQAILCTIHQ 961
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
101-238 |
6.64e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 101 QNLIEAPCRVLGLSKDQAIGRAEKLLERLRLKP-YSDRYPLHLSGGQQQRVAIARALMMEPAVLLFDEPTAALDPEITAQ 179
Cdd:PLN03073 303 QRLEEIYKRLELIDAYTAEARAASILAGLSFTPeMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLW 382
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 180 IVSIIRELAETNItqvIVTHEVEVARKTASRVVYMENGYIVE-QGDASCFANPQTDAFKN 238
Cdd:PLN03073 383 LETYLLKWPKTFI---VVSHAREFLNTVVTDILHLHGQKLVTyKGDYDTFERTREEQLKN 439
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-175 |
1.66e-06 |
|
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: 48.39 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGaHQALF-DITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAgnhfDFAKtpsdkairelr 81
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIdDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVK----------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 82 qnVGMVFQQY-NLWPHLTVLQnLIEAPCRVLGLSKDQAIGRAekLLERLRLKPySDRYPL--HLSGGQQQRVAIARALMM 158
Cdd:TIGR03719 387 --LAYVDQSRdALDPNKTVWE-EISGGLDIIKLGKREIPSRA--YVGRFNFKG-SDQQKKvgQLSGGERNRVHLAKTLKS 460
|
170
....*....|....*..
gi 504696061 159 EPAVLLFDEPTAALDPE 175
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVE 477
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-200 |
9.81e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 16 QALFDITLNCPEGETLVLLGPSGAGKSSLLRVL------NLLEmprsGTLAIAGnhfdFAKTpsdkaiRELRQNVGMVFQ 89
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrktgGYIE----GDIRISG----FPKK------QETFARISGYCE 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 90 QYNLW-PHLTVLQNLIEA-----PCRVlglSKDQAIGRAEKLLERLRLKPYSDR---YP--LHLSGGQQQRVAIARALMM 158
Cdd:PLN03140 960 QNDIHsPQVTVRESLIYSaflrlPKEV---SKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504696061 159 EPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHE 200
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
142-198 |
1.02e-05 |
|
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: 45.33 E-value: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 142 LSGGQQQRVAIARAL---MMEPA-VLLFDEPTAALDPEITAQIVSIIRELAETniTQVIVT 198
Cdd:cd03272 159 LSGGQKSLVALALIFaiqKCDPApFYLFDEIDAALDAQYRTAVANMIKELSDG--AQFITT 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-221 |
6.28e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.97 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSL-LRVLNLLEMpRSGTLAIAGnhFDFAKTPsdkaIRELRQNVGMVFQ---------QYNLWPhl 97
Cdd:cd03288 47 GQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDG--IDISKLP----LHTLRSRLSIILQdpilfsgsiRFNLDP-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 98 tvlqnliEAPCrvlglsKDQAIGRAeklLERLRLKPYSDRYPLHL-----------SGGQQQRVAIARALMMEPAVLLFD 166
Cdd:cd03288 118 -------ECKC------TDDRLWEA---LEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 167 EPTAALDpEITAQIVSIIRELAETNITQVIVTHEVEVARkTASRVVYMENGYIVE 221
Cdd:cd03288 182 EATASID-MATENILQKVVMTAFADRTVVTIAHRVSTIL-DADLVLVLSRGILVE 234
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-223 |
7.19e-05 |
|
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: 42.99 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 142 LSGGQQQRVAIARALMME---PAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVArKTASRVVYM---- 214
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDLgpeg 248
|
90
....*....|.
gi 504696061 215 --ENGYIVEQG 223
Cdd:cd03271 249 gdGGGQVVASG 259
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-204 |
7.37e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 20 DITLncPEGETLVLLGPSGAGKSSLLRvlnllemprsGTLAIAGNHFDFAKTPSDKAIRELRQNVGMVFqqynlwpHLTV 99
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILD----------AIGLALGGAQSATRRRSGVKAGCIVAAVSAEL-------IFTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 100 LQnlieapcrvlglskdqaigraekllerlrlkpysdryplhLSGGQQQRVAIARAL---MMEPAVL-LFDEPTAALDPE 175
Cdd:cd03227 76 LQ----------------------------------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPR 115
|
170 180
....*....|....*....|....*....
gi 504696061 176 ITAQIVSIIRELAETNITQVIVTHEVEVA 204
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLPELA 144
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-200 |
7.96e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 142 LSGGQQQRVAIARALMMEPA--VLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHE 200
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-226 |
9.07e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVlnllemprsgtlaIAGnHFDFAKTPSD-----KAIREL----RQNVGmVF 88
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKV-------------IAG-HPAYKILEGDilfkgESILDLepeeRAHLG-IF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 89 QQYnlwphltvlQNLIEAPC---------------RVLGLSKDQAIGRAEKLLERLRLKPYSDRYpLH------LSGGQQ 147
Cdd:CHL00131 88 LAF---------QYPIEIPGvsnadflrlaynskrKFQGLPELDPLEFLEIINEKLKLVGMDPSF-LSrnvnegFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 148 QRVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVARKTASRVVY-MENGYIVEQGDAS 226
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHvMQNGKIIKTGDAE 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-223 |
1.01e-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: 43.08 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 142 LSGGQQQRVAIARALMME---PAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVArKTASRVVYM---- 214
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDLgpeg 908
|
90
....*....|.
gi 504696061 215 --ENGYIVEQG 223
Cdd:TIGR00630 909 gdGGGTVVASG 919
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-207 |
1.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 3 IKLNGINCFYGAHQALFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAgnhfdfaktpsdKAIRelrq 82
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIK---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 83 nVGMvFQQYN---LWPHLTVLQNLIEAPCRVLGLSKDQAIG----RAEKLLERlrlkpySDRYplhlSGGQQQRVAIARA 155
Cdd:PRK10636 377 -LGY-FAQHQlefLRADESPLQHLARLAPQELEQKLRDYLGgfgfQGDKVTEE------TRRF----SGGEKARLVLALI 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504696061 156 LMMEPAVLLFDEPTAALDPEITAqivSIIRELAETNITQVIVTHEVEVARKT 207
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQ---ALTEALIDFEGALVVVSHDRHLLRST 493
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-223 |
1.33e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLrvLNLLEMPRSGTLAIAGNHFDFAKTpsdkAIRELRQNVGMVFQQynlwPHL---TVLQNL- 103
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLL--LTFMRMVEVCGGEIRVNGREIGAY----GLRELRRQFSMIPQD----PVLfdgTVRQNVd 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 104 --IEA-PCRV------LGLsKDQAIGRAEKLLERLrLKPYSDryplhLSGGQQQRVAIARALMME-PAVLLFDEPTAALD 173
Cdd:PTZ00243 1406 pfLEAsSAEVwaalelVGL-RERVASESEGIDSRV-LEGGSN-----YSVGQRQLMCMARALLKKgSGFILMDEATANID 1478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 174 PEITAQIVSIIRElAETNITQVIVTHEVE-VARktASRVVYMENGYIVEQG 223
Cdd:PTZ00243 1479 PALDRQIQATVMS-AFSAYTVITIAHRLHtVAQ--YDKIIVMDHGAVAEMG 1526
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-173 |
1.37e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 31 LVLLGPSGAGKSSLLRVLNLLEMPRSGT--------LAIAGNH----FDFAKTPsdkairelrqnvgmVFQQYNLWPhlT 98
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTvfrsakvrMAVFSQHhvdgLDLSSNP--------------LLYMMRCFP--G 601
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696061 99 VLQNLIEAPCRVLGLSKDqaigraekllerLRLKP-YSdryplhLSGGQQQRVAIARALMMEPAVLLFDEPTAALD 173
Cdd:PLN03073 602 VPEQKLRAHLGSFGVTGN------------LALQPmYT------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
150-202 |
2.40e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 41.57 E-value: 2.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 504696061 150 VAIARALM---MEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIV-THEVE 202
Cdd:COG1106 211 LALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFtTHSTE 267
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-175 |
3.85e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 18 LFDITLNCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLAIAGNHFDFAKTPSDKAIrelRQNVGM-----VFQQYN 92
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYI---GHNLGLklemtVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 93 LWPHLTVLQNLIEAPCRVLglskdqaigraeKLLERLRLKPYSdryplhLSGGQQQRVAIARALMMEPAVLLFDEPTAAL 172
Cdd:PRK13541 93 FWSEIYNSAETLYAAIHYF------------KLHDLLDEKCYS------LSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
...
gi 504696061 173 DPE 175
Cdd:PRK13541 155 SKE 157
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
27-51 |
5.52e-04 |
|
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: 39.69 E-value: 5.52e-04
10 20
....*....|....*....|....*
gi 504696061 27 EGETLVLLGPSGAGKSSLlrvLNLL 51
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNAL 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
142-217 |
5.64e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 142 LSGGQQQRVAIA--RALMM-EPAVL-LFDEPTAALDPEITAQIVSIIRELAETniTQVIV-THE---VEVARKTaSRVVY 213
Cdd:pfam02463 1078 LSGGEKTLVALAliFAIQKyKPAPFyLLDEIDAALDDQNVSRVANLLKELSKN--AQFIViSLReemLEKADKL-VGVTM 1154
|
....
gi 504696061 214 MENG 217
Cdd:pfam02463 1155 VENG 1158
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-223 |
5.65e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 28 GETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLAIAGNH----------FDFAKTPSdkairelrqnvgmVFQQYNLWPH 96
Cdd:PRK15064 345 GERLAIIGENGVGKTTLLRTLvGELE-PDSGTVKWSENAnigyyaqdhaYDFENDLT-------------LFDWMSQWRQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 97 LTVLQNLIEApcrVLG---LSKDQaIGRAEKLLerlrlkpysdryplhlSGGQQQRVAIARALMMEPAVLLFDEPTAALD 173
Cdd:PRK15064 411 EGDDEQAVRG---TLGrllFSQDD-IKKSVKVL----------------SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504696061 174 PEitaQIVSIIRELAETNITQVIVTHEVEVARKTASRVVYM-ENGYIVEQG 223
Cdd:PRK15064 471 ME---SIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEItPDGVVDFSG 518
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
149-199 |
6.08e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 149 RVAIARALMMEPAVLLFDEPTAALDpeitaqiVSIIR----ELAETNITQVIVTH 199
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-------INTIRwledVLNERNSTMIIISH 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-242 |
8.11e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 142 LSGGQQQRVAIARALM--MEPAVLLFDEPTAALDPEITAQIVSIIRELAETNITqVIVTHEVEVARKTASRVVYM----- 214
Cdd:PRK00635 1388 LSDGEHYRLHLAKKISsnLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT-VIATDRSGSLAEHADHLIHLgpgsg 1466
|
90 100
....*....|....*....|....*....
gi 504696061 215 -ENGYIVeqgDASCFANPQTDAFKNYLSH 242
Cdd:PRK00635 1467 pQGGYLL---STSALKQSQPDLHNTRSSE 1492
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
139-199 |
1.09e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 39.50 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504696061 139 PLHLSG-GQQQRVAIA--RALMME--------PAVLLFDEPTAALDPEitAQIVSI--IRELAETNITQVIV-TH 199
Cdd:pfam13175 315 PLNKNGsGVQRLILLIffIAEAERkedeieekNVILAIEEPEAHLHPQ--AQRVLIklLKELANDNKTQVIItTH 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-217 |
1.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 121 RAEKllERLRLKPYSD--RYPLH-LSGGQQQ------RVAIARALMMEPAVLLFDEPTAALDPEITAQIVSII-RELAEt 190
Cdd:PRK03918 767 KAEE--NKVKLFVVYQgkERPLTfLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMeRYLRK- 843
|
90 100 110
....*....|....*....|....*....|
gi 504696061 191 nITQVI-VTHEVEVaRKTASRV--VYMENG 217
Cdd:PRK03918 844 -IPQVIiVSHDEEL-KDAADYVirVSLEGG 871
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
27-48 |
1.53e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.29 E-value: 1.53e-03
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
142-175 |
2.34e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.34e-03
10 20 30
....*....|....*....|....*....|....
gi 504696061 142 LSGGQQQRVAIARALMMEPAVLLFDEPTAALDPE 175
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
25-48 |
2.99e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 2.99e-03
10 20
....*....|....*....|....
gi 504696061 25 CPEGETLVLLGPSGAGKSSLLRVL 48
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-216 |
3.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 3.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696061 149 RVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNitQVIV----THEVEVARKTASRVVYMEN 216
Cdd:COG4717 572 RLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGR--QVIYftchEELVELFQEEGAHVIELES 641
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
142-203 |
3.60e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 3.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696061 142 LSGGQQQ------RVAIARALMMEPAVLLFDEPTAALDPEITAQIVSIIR-ELAETN-ITQVI-VTHEVEV 203
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSdIPQVImISHHREL 872
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
12-56 |
4.23e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 4.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 504696061 12 YGAHQALFDitlncPEGETLvLLGPSGAGKSSLLRVLNLLEMPRS 56
Cdd:pfam13555 12 FDGHTIPID-----PRGNTL-LTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-227 |
6.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696061 139 PLH-LSGGQQQRVAIARALMM---EPAVLLFDEPTAALDPEITAQIVSIIRELAETNITQVIVTHEVEVArKTASRVVYM 214
Cdd:PRK00635 806 PLSsLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLEL 884
|
90
....*....|....*....
gi 504696061 215 ------ENGYIVeqgdASC 227
Cdd:PRK00635 885 gpeggnLGGYLL----ASC 899
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
157-199 |
8.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.67 E-value: 8.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 504696061 157 MMEPAVLLFDEPTAALDPEITAQIVSIIRELAETNiTQVIV-TH 199
Cdd:COG3910 150 FRGNGLYLLDEPEAALSPSRQLALLALIHDLVREG-SQFIIaTH 192
|
|
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