|
Name |
Accession |
Description |
Interval |
E-value |
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-248 |
1.10e-176 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 486.11 E-value: 1.10e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 1 MTTSRLNQGTPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARE 80
Cdd:PRK11247 2 MNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMMFQDARLLPWKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 161 GALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVELPHPRHHGTPRLAELEARVLNR 240
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPRPRRRGSARLAELEAEVLQR 241
|
....*...
gi 506220968 241 VMRKAPAP 248
Cdd:PRK11247 242 VMSRGESE 249
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-248 |
1.85e-108 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 313.56 E-value: 1.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRY----GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQ 87
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGLTGDWQPA------ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG1116 88 EPALLPWLTVLDNVALGLELRGVPKaerrerARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIED--GKIGLDMAVELPHPRHH---GTPRLAELEAR 236
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVDLPRPRDRelrTSPEFAALRAE 247
|
250
....*....|..
gi 506220968 237 VLNRVMRKAPAP 248
Cdd:COG1116 248 ILDLLREEAERA 259
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-219 |
1.73e-95 |
|
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: 278.97 E-value: 1.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYG----EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQ 87
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03293 81 QDALLPWLTVLDNVALGLelqgvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIE--DGKIGLDMAVEL 219
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAEVEVDL 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-211 |
4.12e-81 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 242.43 E-value: 4.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD---AREDTRMMFQD 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03259 81 YALFPHLTVAENIAFGLKlrgvpkAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-211 |
1.32e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 230.76 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD---AREDTRMMFQD 88
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEKRNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLTGDWQPAARR------ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRGVPKAEIrarvaeLLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG3842 166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-210 |
7.61e-70 |
|
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: 212.43 E-value: 7.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD-------AREDTRM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledelppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGLtgdwqpaarraleevgladrandwpaalSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-211 |
2.13e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 212.98 E-value: 2.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYG----EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR- 83
Cdd:COG1136 2 SPLLeLRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 --------MMFQDARLLPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:COG1136 82 rlrrrhigFVFQFFNLLPELTALENVALPLLlagvsrKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 150 RPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDvSESVAMAERVLLIEDGKI 211
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-211 |
2.41e-66 |
|
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: 205.03 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYG----EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---- 83
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 -----MMFQDARLLPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPG 152
Cdd:cd03255 81 rrhigFVFQSFNLLPDLTALENVELPLLlagvpkKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-211 |
3.01e-63 |
|
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: 197.46 E-value: 3.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQDAR 90
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpvnTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALGLTGDWQPAA------RRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03300 83 LFPHLTVFENIAFGLRLKKLPKAeikervAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-211 |
7.47e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 200.30 E-value: 7.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQD 88
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRniaMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG3839 84 YALYPHMTVYENIAFPLKlrkvpkAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-211 |
1.11e-61 |
|
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: 194.04 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR--------MM 85
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrrrigML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGLT--GDWQPA-----ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1127 88 FQGGALFDSLTVFENVAFPLRehTDLSEAeirelVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-211 |
4.60e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.80 E-value: 4.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR--------M 84
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrrigV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGL--TG----DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLrvTGksrkEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-218 |
4.13e-60 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.58 E-value: 4.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEkTILNAlDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQD 88
Cdd:COG3840 2 LRLDDLTYRYGD-FPLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvsMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALG------LTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALI-HRPgLLLLDEPLG 161
Cdd:COG3840 80 NNLFPHLTVAQNIGLGlrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE 218
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-205 |
6.07e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 190.07 E-value: 6.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYG----EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQ 87
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRlrgvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLL 205
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-211 |
7.80e-60 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 188.23 E-value: 7.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAR---EDTRMMFQD 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLTGDWQPAA------RRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDeidervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-211 |
9.59e-60 |
|
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: 188.12 E-value: 9.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR-------MMF 86
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvgMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPWKKVLDNVALGLT-------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPIkvkgmskAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 160 LGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-211 |
1.48e-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: 188.09 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR--------MM 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlrrrmgML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGL---TGDWQPAARR----ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLrehTRLSEEEIREivleKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-211 |
2.34e-59 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 191.51 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA---DAREdtR---MM 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlPPRE--RrvgFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGLTGDWQPAARRA------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRarveelLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-244 |
1.50e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 185.65 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR----MMFQDA 89
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrrigYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVAL-----GLTGDWQPA-ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG1131 83 ALYPDLTVRENLRFfarlyGLPRKEARErIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 164 DALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIgldmavelphpRHHGTPrlAELEARVLNRVMR 243
Cdd:COG1131 163 DPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI-----------VADGTP--DELKARLLEDVFL 228
|
.
gi 506220968 244 K 244
Cdd:COG1131 229 E 229
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
12-211 |
4.78e-58 |
|
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: 188.32 E-value: 4.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGN---APLADAREDTRMMFQD 88
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGrdiTRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLTGDWQPAARRA------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAervaelLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-211 |
5.55e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.43 E-value: 5.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR-------MMF 86
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrrkvgMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPWKKVLDNVALGLT----GDWQPA---ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1126 84 QQFNLFPHLTVLENVTLAPIkvkkMSKAEAeerAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 160 LGALD-ALTRlEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1126 164 TSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-229 |
3.04e-57 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 186.69 E-value: 3.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 1 MTTSRLNQGTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAR 79
Cdd:PRK09452 3 KLNKQPSSLSPLVeLRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTR---MMFQDARLLPWKKVLDNVALGLTGDWQPAA------RRALEEVGLADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:PRK09452 83 AENRhvnTVFQSYALFPHMTVFENVAFGLRMQKTPAAeitprvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDmavelphprhhGTPR 229
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD-----------GTPR 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-211 |
4.59e-57 |
|
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: 181.86 E-value: 4.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRY----GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---- 83
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 -----MMFQDARLLPWKKVLDNVALGL----TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG4181 89 arhvgFVFQSFQLLPTLTALENVMLPLelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESvAMAERVLLIEDGKI 211
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRL 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-239 |
9.38e-57 |
|
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: 181.12 E-value: 9.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQDARLLPWKKVLDNVALGL- 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 106 -------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSL 178
Cdd:TIGR01184 81 rvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 179 WREHGFTVLLVTHDVSESVAMAERVLLIEDG---KIGLDMAVELPHPRHH----GTPRLAELEARVLN 239
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVPFPRPRDRlevvEDPSYYDLRNEALY 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
14-218 |
9.58e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.10 E-value: 9.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--------RAGNAPLADAREDTRM 84
Cdd:COG3638 5 LRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIlvdgqdvtALRGRALRRLRRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGLTGDW--------------QPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:COG3638 85 IFQQFNLVPRLSVLTNVLAGRLGRTstwrsllglfppedRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 151 PGLLLLDEPLGALD-ALTRLEMqEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE 218
Cdd:COG3638 165 PKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
3.88e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 180.27 E-value: 3.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY----GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--------ARED 81
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserelraARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TRMMFQDARLLPWKKVLDNVALGL--TGdWQPAARRA-----LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLeiAG-VPKAEIRKrvaelLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTH--DVSESVamAERVLLIEDGKI 211
Cdd:COG1135 163 LCDEATSALDPETTRSILDLLKDINRELGLTIVLITHemDVVRRI--CDRVAVLENGRI 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-211 |
4.83e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 4.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRMMF 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppewRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPwKKVLDNVALGLT----GDWQPAARRALEEVGLADRANDWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQlrerKFDRERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-209 |
1.17e-53 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 173.73 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQDARL 91
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK11248 82 LPWRNVQDNVAFGLQlagvekMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506220968 166 LTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDG 209
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-211 |
1.19e-53 |
|
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: 173.15 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEK----TILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRA--------GNAPLADARED 81
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdgtdltllSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TRMMFQDARLLPWKKVLDNVALGLTGDWQPAARRA------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEervlelLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-211 |
1.43e-53 |
|
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: 173.45 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGE----KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRM 84
Cdd:COG1124 4 VRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrkafRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDAR--LLPWKKVLDNVALGLT----GDWQPAARRALEEVGLADRAND-WPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:COG1124 84 VFQDPYasLHPRHTVDRILAEPLRihglPDREERIAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220968 158 EPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1124 164 EPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-211 |
3.20e-53 |
|
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: 171.75 E-value: 3.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAP-----LADAREDTRMMFQ 87
Cdd:COG1122 3 LENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DAR---LLPwkKVLDNVA-----LGLTGDW-QPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1122 83 NPDdqlFAP--TVEEDVAfgpenLGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-211 |
1.35e-52 |
|
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: 178.17 E-value: 1.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLL-LEGVTKRY-----GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARED 81
Cdd:COG1123 256 AAEPLLeVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TR--------MMFQD--ARLLPWKKVLDNVALGLT--GDWQPAARRA-----LEEVGL-ADRANDWPAALSGGQKQRVAL 143
Cdd:COG1123 336 SLrelrrrvqMVFQDpySSLNPRMTVGDIIAEPLRlhGLLSRAERRErvaelLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 144 ARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-211 |
1.99e-52 |
|
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: 167.96 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM----MFQDA 89
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrigyLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVALgltgdwqpaarraleevgladrandwpaalSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03230 83 SLYENLTVRENLKL------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506220968 170 EMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03230 133 EFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-241 |
6.06e-52 |
|
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: 168.90 E-value: 6.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGE-KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--------RAGNAPLADAREDTRM 84
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinKLKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGLTGDW--------------QPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGRRstwrslfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDmavelphprhhGTPrl 230
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD-----------GPP-- 229
|
250
....*....|.
gi 506220968 231 AELEARVLNRV 241
Cdd:cd03256 230 AELTDEVLDEI 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-211 |
1.08e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.34 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREdtRM-----MFQD 88
Cdd:COG1121 9 LENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR--RIgyvpqRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPwKKVLDNVALGLTG-----------DWQpAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:COG1121 87 DWDFP-ITVRDVVLMGRYGrrglfrrpsraDRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 158 EPLGALDAltrlEMQEMIVSL---WREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1121 165 EPFAGVDA----ATEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-210 |
1.84e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.87 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADAREDTRMMF 86
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARL-LPWKKVLDNVA-----LGLTGDWQPA-ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03225 82 QNPDDqFFGPTVEEEVAfglenLGLPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 160 LGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-211 |
3.66e-51 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 166.90 E-value: 3.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-----AGNAPLADarEDTRMMF 86
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRlngqdATRVHARD--RKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPWKKVLDNVALGLTGDWQPAAR------RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKikarveELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 161 GALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-214 |
1.23e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 165.65 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG----NAPLADAREDTR---MMFQDA 89
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglkvNDPKVDERLIRQeagMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVALGLT-------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK09493 87 YLFPHLTALENVMFGPLrvrgaskEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 163 LDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:PRK09493 167 LDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
14-210 |
5.65e-50 |
|
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: 163.19 E-value: 5.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA--------REDTRM 84
Cdd:TIGR02673 4 FHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrqlpllRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENVALPLevrgkkEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 159 PLGALDAltrlEMQEMIVSLWRE---HGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:TIGR02673 164 PTGNLDP----DLSERILDLLKRlnkRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-211 |
8.86e-50 |
|
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: 166.81 E-value: 8.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTiLNAlDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---------MMFQ 87
Cdd:COG4148 7 FRLRRGGFT-LDV-DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlpphrrrigYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGLTGDWQPAARRALEEV----GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG4148 85 EARLFPHLSVRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 164 DALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-211 |
8.95e-50 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 166.82 E-value: 8.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA---REDTRMMFQD 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiqQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLTGDWQPAARR------ALEEVGLA---DRANDwpaALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERkqrvkeALELVDLAgfeDRYVD---QISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-211 |
1.08e-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: 163.68 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--AREDTR---MMFQD 88
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARriaYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLT---GDWQP-------AARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1120 84 PPAPFGLTVRELVALGRYphlGLFGRpsaedreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-211 |
6.00e-49 |
|
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: 161.35 E-value: 6.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQDARL 91
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERnvgFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLtgDWQPAARRA------------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03296 86 FRHMTVFDNVAFGL--RVKPRSERPpeaeirakvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-211 |
9.40e-49 |
|
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: 160.36 E-value: 9.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEK----TILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE--------LRAGNAPLADARED 81
Cdd:cd03257 4 VKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdlLKLSRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TRMMFQDAR--LLPWKKVLDNVA---LGLTGDWQPAARRA-----LEEVGL-ADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:cd03257 84 IQMVFQDPMssLNPRMTIGEQIAeplRIHGKLSKKEARKEavlllLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-211 |
1.38e-48 |
|
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: 161.27 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA---------REDTRMMFQ 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGLTGDWQPA------ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRaereerAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-211 |
1.97e-48 |
|
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: 160.16 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGE-KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA--DAREDTRMM---FQ 87
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIgyvIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVAL--GLTGdWQPAARRA----------LEEVGLADRandWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03295 83 QIGLFPHMTVEENIALvpKLLK-WPKEKIREradellalvgLDPAEFADR---YPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-211 |
2.86e-48 |
|
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: 159.64 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR----MMFQDA 89
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqigVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVAL-----GLTGD-WQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG4555 84 GLYDRLTVRENIRYfaelyGLFDEeLKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 164 DALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4555 164 DVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-211 |
9.23e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 160.26 E-value: 9.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTI-LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDT--RMM---FQ 87
Cdd:COG1125 4 FENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIgyvIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVAL--GLTGdWQPAARRA-----LEEVGL-----ADRandWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG1125 84 QIGLFPHMTVAENIATvpRLLG-WDKERIRArvdelLELVGLdpeeyRDR---YPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-211 |
1.02e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 161.40 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA--DARE-DTRMMFQDAR 90
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlHARDrKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALGLTgdWQPAARRA------------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10851 85 LFRHMTVFDNIAFGLT--VLPRRERPnaaaikakvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-224 |
1.73e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.35 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY----GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--------RAGNAPLADARED 81
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TRMMFQDARLLPWKKVLDNVALGLTGDWQPAARRA------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKarvtelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTH--DVSESVamAERVLLIEDGKIgldmaVEL-------PHPRH 224
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKRI--CDRVAVIDAGRL-----VEQgtvsevfSHPKH 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-211 |
2.45e-47 |
|
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: 156.30 E-value: 2.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 37 GQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM---------MFQDARLLPWKKVLDNVALGLTG 107
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrkiglVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 108 DWQPAARRALEEV----GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHG 183
Cdd:cd03297 103 KRNREDRISVDELldllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLN 182
|
170 180
....*....|....*....|....*...
gi 506220968 184 FTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03297 183 IPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-211 |
9.15e-47 |
|
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: 158.43 E-value: 9.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 42 VVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQDARLLPWKKVLDNVALGLTGDWQPAA----- 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhinMVFQSYALFPHMTVEENVAFGLKMRKVPRAeikpr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 114 -RRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHD 192
Cdd:TIGR01187 81 vLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*....
gi 506220968 193 VSESVAMAERVLLIEDGKI 211
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKI 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-211 |
1.10e-46 |
|
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: 165.01 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRMMF 86
Cdd:COG2274 476 LENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdpaslRRQIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPwKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG2274 556 QDVFLFS-GTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLwrEHGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLS-TIRLADRIIVLDKGRI 687
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-211 |
1.38e-46 |
|
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: 154.49 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTI-LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA--------REDTRM 84
Cdd:cd03292 3 FINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraipylRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGL--TG----DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALevTGvpprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-211 |
2.00e-46 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 153.80 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTIlnALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQDAR 90
Cdd:cd03298 3 LDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpvsMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALG------LTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03298 81 LFAHLTVEQNVGLGlspglkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-210 |
3.23e-46 |
|
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: 152.15 E-value: 3.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD-AREDTR----MMF 86
Cdd:cd03228 3 FKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRkniaYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPwKKVLDNValgltgdwqpaarraleevgladrandwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03228 83 QDPFLFS-GTIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506220968 167 TRLEMQEMIVSLwrEHGFTVLLVTHDVSeSVAMAERVLLIEDGK 210
Cdd:cd03228 131 TEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-206 |
4.42e-46 |
|
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: 153.07 E-value: 4.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQdARLLP 93
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQ-RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 WK---KVLDNVALGLTG-----------DWQpAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03235 81 RDfpiSVRDVVLMGLYGhkglfrrlskaDKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 160 LGALDAltrlEMQEMIVSL---WREHGFTVLLVTHDVSESVAMAERVLLI 206
Cdd:cd03235 160 FAGVDP----KTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-210 |
9.41e-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: 150.47 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADaredtrmmfqdarlLP 93
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------------LP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 WKKVLDNVALgltgDWQpaarraleevgladrandwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQE 173
Cdd:cd00267 68 LEELRRRIGY----VPQ----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 506220968 174 MIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:cd00267 122 LLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-211 |
3.55e-45 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 151.18 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPDGGELRAGNAPLADARED-----TR 83
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 --MMFQDARLLPwKKVLDNVALGLT--GDW-----QPAARRALEEVGLADRAND--WPAALSGGQKQRVALARALIHRPG 152
Cdd:cd03260 83 vgMVFQKPNPFP-GSIYDNVAYGLRlhGIKlkeelDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
14-206 |
8.87e-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: 149.30 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR---AGNAPLADA------REDTRM 84
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYlngQETPPLNSKkaskfrREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLkykklsKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 159 PLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDvSESVAMAERVLLI 206
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-246 |
1.06e-44 |
|
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: 156.99 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDG---GELRAGNAPLADAREDTR 83
Cdd:COG1123 2 TPLLeVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 -----MMFQD--ARLLPWKkVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:COG1123 82 grrigMVFQDpmTQLNPVT-VGDQIAEALEnlglsrAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE--LPHPRH-HGT 227
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEeiLAAPQAlAAV 240
|
250
....*....|....*....
gi 506220968 228 PRLAELEARVLNRVMRKAP 246
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEP 259
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-214 |
1.11e-44 |
|
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: 150.53 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGE-KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--------RAGNAPLADAREDT 82
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNV---ALGLTGDWQPAARR-----------ALEEVGLADRANDWPAALSGGQKQRVALARALI 148
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLGRfseedkeralsALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 149 HRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-229 |
1.62e-44 |
|
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: 150.66 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA------REDTRMM 85
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenlweiRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQD------ARLlpwkkVLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:TIGR04520 83 FQNpdnqfvGAT-----VEDDVAFGLenlgvpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSEsVAMAERVLLIEDGKIGLDmavelphprhhGTPR 229
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEE-AVLADRVIVMNKGKIVAE-----------GTPR 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-211 |
3.38e-44 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 148.65 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEK----TILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR------- 83
Cdd:TIGR02211 5 ENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 --MMFQDARLLPWKKVLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:TIGR02211 85 lgFIYQFHHLLPDFTALENVAMPLligkksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQL 219
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
21-211 |
6.38e-44 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 147.86 E-value: 6.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGE----KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR--------AGNAPLADAREDTRMMFQD 88
Cdd:TIGR02982 11 YGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvlgqelhgASKKQLVQLRRRIGYIFQA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNV--ALGLTGDWQPAARRA-----LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR02982 91 HNLLGFLTARQNVqmALELQPNLSYQEAREraramLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDvSESVAMAERVLLIEDGKI 211
Cdd:TIGR02982 171 ALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-211 |
1.33e-43 |
|
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: 145.66 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADaredtrmmfqdarlLP 93
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------LS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 WKKVLDNVALGLTgdwqpaarrALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQE 173
Cdd:cd03214 68 PKELARKIAYVPQ---------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 506220968 174 MIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03214 139 LLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-211 |
8.54e-43 |
|
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: 152.60 E-value: 8.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 7 NQGTPLLLEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM- 84
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 ----MFQDARLLPWKkVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIH 149
Cdd:COG4988 412 qiawVPQNPYLFAGT-IRENLRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 150 RPGLLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-210 |
8.84e-43 |
|
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: 144.16 E-value: 8.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR----MMFQ 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVAL--GLTGDWQPAAR--RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG4133 83 ADGLKPELTVRENLRFwaALYGLRADREAidEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 164 DALTRLEMQEMIVSlWREHGFTVLLVTHDVSESVAMaeRVLLIEDGK 210
Cdd:COG4133 163 DAAGVALLAELIAA-HLARGGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-210 |
1.32e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 148.83 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MM 85
Cdd:PRK11607 17 TPLLeIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGLTGDWQPAARRA------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIAsrvnemLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
32-211 |
1.43e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 148.71 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 32 LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA---------REDTRMMFQDARLLPWKKVLDNVA 102
Cdd:COG4175 48 FDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLskkelrelrRKKMSMVFQHFALLPHRTVLENVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 103 LGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIV 176
Cdd:COG4175 128 FGLeiqgvpKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELL 207
|
170 180 190
....*....|....*....|....*....|....*
gi 506220968 177 SLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4175 208 ELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRI 242
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
12-211 |
1.78e-42 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 147.53 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTiLNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQD 88
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRgiaYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKlrkvpkEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 163 LDALTRLE-MQEMivSLW-REHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:NF040840 161 LDVQTRDElIREM--KRWhREFGFTAIHVTHNFEEALSLADRVGIMLNGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-211 |
2.82e-42 |
|
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: 144.02 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNaLDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNA---PLADAREDTRMMFQD 88
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGL---TGDWQPAARRALE---EVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLkkrKVDKKEIERKVLEiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-214 |
2.96e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 143.95 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 31 DLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD---AREDTRMMFQDARLLPWKKVLDNVALG--- 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtppSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 105 ---LTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWRE 181
Cdd:PRK10771 99 glkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|...
gi 506220968 182 HGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-211 |
3.14e-42 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 143.08 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 20 RYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAP---LADAREDTRMMFQDARLLPWKK 96
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtgLAPYQRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 97 VLDNVALG------LTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:TIGR01277 87 VRQNIGLGlhpglkLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506220968 171 MQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-208 |
3.66e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 143.01 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPD---GGELRAGNAPLADAREDTR---MM 85
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRrigIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGLTGDWQPAARR-----ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALPPTIGRAQRRarveqALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 161 GALDALTRLEMQEMIVSLWREHGFTVLLVTHDVsESVAMAERVLLIED 208
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDE-EDAPAAGRVLDLGN 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
4.86e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 143.61 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGN-----APLADA-----REDT 82
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiAGHqfdfsQKPSEKairllRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNV------ALGLTGdwQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLieapckVLGLSK--EQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 154 LLLDEPLGALDAltrlEMQEMIVSLWRE---HGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4161 163 LLFDEPTAALDP----EITAQVVEIIRElsqTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-211 |
1.83e-41 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 145.56 E-value: 1.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR---MMFQDAR 90
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERgvgMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALG--LTGDWQPAARRALEEVG-------LADRAndwPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK11000 86 LYPHLSVAENMSFGlkLAGAKKEEINQRVNQVAevlqlahLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-211 |
1.84e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 139.38 E-value: 1.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGN------APLADA----REDT 82
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiAGNhfdfskTPSDKAirelRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNV------ALGLTGdwQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLieapcrVLGLSK--DQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 154 LLLDEPLGALDAltrlEMQEMIVSLWRE---HGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11124 163 LLFDEPTAALDP----EITAQIVSIIRElaeTGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-229 |
2.26e-40 |
|
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: 140.28 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYG-----EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG--------NAPLADARE 80
Cdd:TIGR04521 3 LKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDgrditakkKKKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMMFQdarlLPWKK-----VLDNVA-----LGLTGD-WQPAARRALEEVGL----ADRAndwPAALSGGQKQRVALAR 145
Cdd:TIGR04521 83 KVGLVFQ----FPEHQlfeetVYKDIAfgpknLGLSEEeAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 146 ALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDmavelphprhh 225
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD----------- 224
|
....
gi 506220968 226 GTPR 229
Cdd:TIGR04521 225 GTPR 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-211 |
1.12e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.54 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD-AREDTR----MMFQ 87
Cdd:COG1132 342 FENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRrqigVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPwKKVLDNVALGltgdwQPAA-----RRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRP 151
Cdd:COG1132 422 DTFLFS-GTIRENIRYG-----RPDAtdeevEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 152 GLLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-211 |
1.94e-39 |
|
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: 135.81 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRA-GNAPLADAREDTRM--MFQDAR 90
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIgaLIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALGLTGDWQPAAR--RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRidEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 506220968 169 LEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03268 163 KELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-218 |
2.14e-39 |
|
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: 136.75 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETP-DGGEL-----RAGNAPLADARedT 82
Cdd:COG1119 1 DPLLeLRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVrlfgeRRGGEDVWELR--K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RM----MFQDARLLPWKKVLDNVALGLT---GDWQP-------AARRALEEVGLADRANDWPAALSGGQKQRVALARALI 148
Cdd:COG1119 79 RIglvsPALQLRFPRDETVLDVVLSGFFdsiGLYREptdeqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 149 HRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE 218
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-211 |
1.35e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.91 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 7 NQGTPLLLEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA-----DAR 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTRMMFQ--DARLLPwKKVLDNVALGLTG------DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRP 151
Cdd:PRK13635 81 RQVGMVFQnpDNQFVG-ATVQDDVAFGLENigvpreEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 152 GLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSEsVAMAERVLLIEDGKI 211
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDE-AAQADRVIVMNKGEI 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-211 |
1.46e-38 |
|
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: 134.78 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARED--TRM- 84
Cdd:COG0411 1 SDPLLeVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 ---MFQDARLLPWKKVLDNVALG------------LTGDWQPA---------ARRALEEVGLADRANDWPAALSGGQKQR 140
Cdd:COG0411 81 iarTFQNPRLFPELTVLENVLVAaharlgrgllaaLLRLPRARreerearerAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 141 VALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-211 |
1.72e-38 |
|
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: 133.47 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFvAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMF----Q 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKV---LDNVAL--GLTGDWQPAA-RRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03264 80 EFGVYPNFTVrefLDYIAWlkGIPSKEVKARvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-211 |
2.42e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.11 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-------------RE 80
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglirqlRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMMFQDARLLPWKKVLDNVALGLT-------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPVivkgepkEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLWREHGfTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-211 |
3.69e-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: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 19 KRYGEKTIlnALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM---------MFQDA 89
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppekrrigyVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVALGLTgDWQPAARRALEE-----VGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMK-RARPSERRISFErvielLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-211 |
4.10e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 132.40 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-REDTRMMFQDAR 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAaRNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDN-VALG-LTG----DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03269 81 LYPKMKVIDQlVYLAqLKGlkkeEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-211 |
5.56e-38 |
|
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: 139.52 E-value: 5.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 2 TTSRLNQGTPLLLEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAR 79
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTR-----MMFQDARLLPwKKVLDNVALGltgdwQPAA-----RRALEEVGLADRANDWP-----------AALSGGQK 138
Cdd:COG4987 404 EDDLrrriaVVPQRPHLFD-TTLRENLRLA-----RPDAtdeelWAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 139 QRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSEsVAMAERVLLIEDGKI 211
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAG-LERMDRILVLEDGRI 547
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-211 |
1.19e-37 |
|
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: 131.72 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAREDTR---MMFQDAR 90
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvAGHDVVREPREVRRrigIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVAL-----GLTGD-WQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03265 84 VDDELTGWENLYIharlyGVPGAeRRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-211 |
1.47e-37 |
|
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: 131.79 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR------MM 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGL-------TGDWQPA---------ARRALEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAqartgsgLLLARARreerearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 150 RPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-211 |
2.47e-37 |
|
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: 130.63 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR------MM 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGLTGDWQPAARRALEEV-----GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 161 GALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03224 161 EGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-211 |
7.40e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.66 E-value: 7.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--AREDTR---MMFQDA 89
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELARrraVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RL-LPWkKVLDNVALGLTgDW-------QPAARRALEEVGLADRANDWPAALSGGQKQRVALARALI------HRPGLLL 155
Cdd:PRK13548 86 SLsFPF-TVEEVVAMGRA-PHglsraedDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-252 |
1.70e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.81 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 16 GVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA--------DAREDTRMMFQ 87
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnraqrkAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DA--RLLPWKKVLDNVALGLTG--DWQPAARRA-----LEEVGLADR-ANDWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRHllSLDKAERLArasemLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 158 EPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVELPHPRHHGTPRLaeLEARV 237
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRV--LQNAV 254
|
250
....*....|....*
gi 506220968 238 LnrvmrkAPAPVRAV 252
Cdd:PRK10419 255 L------PAFPVRRR 263
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-211 |
2.24e-36 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 131.89 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD---AREDTRMMFQ 87
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGL----TGDWQPAAR-----RALEEVGLADRAndwPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLkirgMPKAEIEERvaeaaRILELEPLLDRK---PRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-211 |
5.23e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 128.31 E-value: 5.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--AREDTRM---MFQDA 89
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwsPWELARRravLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RL-LPWKkVLDNVALGLT------GDWQPAARRALEEVGLADRAN-DWPAaLSGGQKQRVALARALI-------HRPGLL 154
Cdd:COG4559 85 SLaFPFT-VEEVVALGRAphgssaAQDRQIVREALALVGLAHLAGrSYQT-LSGGEQQRVQLARVLAqlwepvdGGPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 155 LLDEPLGALDaltrLEMQEMIVSLWRE---HGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4559 163 FLDEPTSALD----LAHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-211 |
1.18e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.50 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRagnapladAREDTRMMF--QDARL 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------IPKGLRIGYlpQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLTG--------------------------------------DWQPAARRALEEVGLADRANDWP-AA 132
Cdd:COG0488 73 DDDLTVLDTVLDGDAElraleaeleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPvSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlemqEMIvsLW-----REHGFTVLLVTHDVS--ESVamAERVLL 205
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESI--EWleeflKNYPGTVLVVSHDRYflDRV--ATRILE 221
|
....*.
gi 506220968 206 IEDGKI 211
Cdd:COG0488 222 LDRGKL 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-211 |
1.54e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 126.14 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--------RAGNAPLADAREDTRM 84
Cdd:PRK10908 4 FEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLDNVALGL--TGDWQPAARR----ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLiiAGASGDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 159 PLGALDAltrlEMQEMIVSLWREH---GFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10908 164 PTGNLDD----ALSEGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-159 |
1.75e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 123.91 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-ADAREDTR----MMFQDARLLPWKKVLDNV 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRkeigYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 102 ALGLT-GDWQPAAR-----RALEEVGLAD----RANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:pfam00005 81 RLGLLlKGLSKREKdaraeEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-211 |
3.53e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 125.28 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEK----TILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR--------- 83
Cdd:PRK10584 12 LKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 MMFQDARLLPWKKVLDNVALG--LTG----DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPalLRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220968 158 EPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDvSESVAMAERVLLIEDGKI 211
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-211 |
4.46e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.38 E-value: 4.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA-----DAREDTRMMFQ--DARLLPwK 95
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvwDIRHKIGMVFQnpDNQFVG-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 KVLDNVALGLTG------DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:PRK13650 98 TVEDDVAFGLENkgipheEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506220968 170 EMQEMIVSLWREHGFTVLLVTHDVSEsVAMAERVLLIEDGKI 211
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
36-232 |
4.53e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 126.11 E-value: 4.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 36 AGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA--DAR---EDTRMMFQDARL-----LPWKKVLDnVALGL 105
Cdd:COG4167 38 AGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKyrcKHIRMIFQDPNTslnprLNIGQILE-EPLRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 106 TGDWQPAARRA-----LEEVGL-ADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLW 179
Cdd:COG4167 117 NTDLTAEEREErifatLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQ 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 180 REHGFTVLLVTHDVSESVAMAERVLLIEDGKIgldmaVE-------LPHPRHHGTPRLAE 232
Cdd:COG4167 197 EKLGISYIYVSQHLGIVKHISDKVLVMHQGEV-----VEygktaevFANPQHEVTKRLIE 251
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-214 |
8.60e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 126.38 E-value: 8.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLadAREDTRM---MFQD 88
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRRRigyLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDN-VALG-LTG-DWQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG4152 80 RGLYPKMKVGEQlVYLArLKGlSKAEAKRRAdewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 163 LDALTRLEMQEMIVSLwREHGFTVLLVTHDVsESV-AMAERVLLIEDGKIGLD 214
Cdd:COG4152 160 LDPVNVELLKDVIREL-AAKGTTVIFSSHQM-ELVeELCDRIVIINKGRKVLS 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-217 |
1.38e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.16 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLL-EGVTKRYGEKTI----LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL----ADARE 80
Cdd:PRK11629 3 KILLQcDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTR-----MMFQDARLLPWKKVLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:PRK11629 83 ELRnqklgFIYQFHHLLPDFTALENVAMPLligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 150 RPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAeRVLLIEDGKIGLDMAV 217
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELSL 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-204 |
1.38e-34 |
|
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: 126.32 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY----GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETP---DGGELRAGNAPLADAREDTR--- 83
Cdd:COG0444 4 VRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 ------MMFQD--ARLLPWKKVLDNVALGLT--GDWQPAARRA-----LEEVGL---ADRANDWPAALSGGQKQRVALAR 145
Cdd:COG0444 84 rgreiqMIFQDpmTSLNPVMTVGDQIAEPLRihGGLSKAEAREraielLERVGLpdpERRLDRYPHELSGGMRQRVMIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 146 ALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVL 204
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
11-211 |
1.41e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.53 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 11 PLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL------------RAGNAPLADA 78
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIrvggeeirlkpdRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 79 REDTR------MMFQDARLLPWKKVLDNV------ALGLT-GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALAR 145
Cdd:COG4598 88 RQLQRirtrlgMVFQSFNLWSHMTVLENVieapvhVLGRPkAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 146 ALIHRPGLLLLDEPLGALDAltrlEMQEMIVSLWR---EHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRdlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-211 |
2.63e-34 |
|
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: 121.55 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMF--- 86
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 --QDARLLPwKKVLDNValgltgdwqpaarraleevgladrandwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03246 81 lpQDDELFS-GSIAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLwREHGFTVLLVTHDvSESVAMAERVLLIEDGKI 211
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-224 |
1.02e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.07 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLL-LEGVTKRY--------GEKTILNALD---LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR------ 69
Cdd:COG4608 3 MAEPLLeVRDLKKHFpvrgglfgRTVGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 70 --AGNAPLADAREDTRMMFQD--ARLLPWKKVLDNVALGLT--GDWQPAARRA-----LEEVGL-ADRANDWPAALSGGQ 137
Cdd:COG4608 83 tgLSGRELRPLRRRMQMVFQDpyASLNPRMTVGDIIAEPLRihGLASKAERRErvaelLELVGLrPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 138 KQRVALARALIHRPGLLLLDEPLGALDaltrLEMQEMIVSLW----REHGFTVLLVTHDVSESVAMAERVLLIEDGKIgl 213
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALD----VSIQAQVLNLLedlqDELGLTYLFISHDLSVVRHISDRVAVMYLGKI-- 236
|
250
....*....|....*...
gi 506220968 214 dmaVEL-------PHPRH 224
Cdd:COG4608 237 ---VEIaprdelyARPLH 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-211 |
2.37e-33 |
|
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: 120.86 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMF-- 86
Cdd:COG0410 1 MPMLeVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 ----QDARLLPWKKVLDNVALGL-TGDWQPAARRALEEVG-----LADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:COG0410 81 gyvpEGRRIFPSLTVEENLLLGAyARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-230 |
2.59e-33 |
|
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: 126.34 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 19 KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLEtPDGGELRAGNAPLADA--------REDTRMMFQD-- 88
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLsrralrplRRRMQVVFQDpf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLT---GDWQPAARR-----ALEEVGL-ADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLRvhgPGLSAAERRarvaeALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIgldmaVE-------LPHPRHHGTPRL 230
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV-----VEqgpteqvFDAPQHPYTRAL 525
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-211 |
2.85e-33 |
|
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: 120.34 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLadaredTRM-MFQDAR 90
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI------TKLpMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 L----LP-----WKK--VLDNVALGLTGDWQPAARRA------LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:cd03218 75 LgigyLPqeasiFRKltVEENILAVLEIRGLSKKEREekleelLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-211 |
7.14e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 7.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPD----------GGELRAGNapLADAREDTRMMFQ--DAR 90
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdGITLTAKT--VWDIREKVGIVFQnpDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPwKKVLDNVALGLTGDWQP------AARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:PRK13640 97 FVG-ATVGDDVAFGLENRAVPrpemikIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESvAMAERVLLIEDGKI 211
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
12-211 |
8.93e-33 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 119.32 E-value: 8.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-ADAREDTRMM---FQ 87
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLrRAPRAALARLgvvFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNV----ALGLTGDWQPAAR--RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR03864 82 QPTLDLDLSVRQNLryhaALHGLSRAEARARiaELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSEsVAMAERVLLIEDGKI 211
Cdd:TIGR03864 162 GLDPASRAAITAHVRALARDQGLSVLWATHLVDE-IEASDRLVVLHRGRV 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-211 |
1.04e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 122.83 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 32 LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGN---APLADA------REDTRMMFQDARLLPWKKVLDNVA 102
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAelrevrRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 103 LGLTGDWQPAARR------ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIV 176
Cdd:PRK10070 129 FGMELAGINAEERrekaldALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*
gi 506220968 177 SLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-212 |
1.30e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.13 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG--NAPLADAREDTRMMFQDA- 89
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkPIKAKERRKSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVALGL--TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:cd03226 82 YQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506220968 168 RLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKIG 212
Cdd:cd03226 162 MERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-211 |
2.46e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.64 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGnapladarEDTRMMF--Q 87
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG--------ETVKIGYfdQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLL-PWKKVLDNVALGLTGDWQPAARRALEEVGLA-DRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 165
Cdd:COG0488 386 HQEELdPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD- 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 166 ltrLEMQEMIVSLWREHGFTVLLVTHD---VSesvAMAERVLLIEDGKI 211
Cdd:COG0488 465 ---IETLEALEEALDDFPGTVLLVSHDryfLD---RVATRILEFEDGGV 507
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-241 |
3.55e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 124.07 E-value: 3.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRY--GEKTI--LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA------ 78
Cdd:PRK10535 2 TALLeLKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 79 ---REDTRMMFQDARLLPWKKVLDNVAL-GLTGDWQPAARRA-----LEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVpAVYAGLERKQRLLraqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 150 RPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDvSESVAMAERVLLIEDGKIGLDmavelphPRHHGTPR 229
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRN-------PPAQEKVN 232
|
250
....*....|..
gi 506220968 230 LAELEARVLNRV 241
Cdd:PRK10535 233 VAGGTEPVVNTA 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-211 |
3.96e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 120.36 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTIlnALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM---------MFQ 87
Cdd:PRK11144 6 FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekrrigyVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK11144 84 DARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506220968 168 RLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-247 |
5.08e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.19 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGG-----EL------RAGNAP--LA 76
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELlgrtvqREGRLArdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 77 DAREDTRMMFQDARLLPWKKVLDNV---ALGLTGDWQPAAR-----------RALEEVGLADRANDWPAALSGGQKQRVA 142
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVligALGSTPFWRTCFSwftreqkqralQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 143 LARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAvelphP 222
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS-----S 237
|
250 260
....*....|....*....|....*
gi 506220968 223 RHHGTPRLAELeARVLNRVMRKAPA 247
Cdd:PRK09984 238 QQFDNERFDHL-YRSINRVEENAKA 261
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-214 |
1.18e-31 |
|
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: 116.28 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 5 RLNQGTPLLLEGVT----KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAR 79
Cdd:cd03267 11 RVYSKEPGLIGSLKslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTR----MMFQDARL---LPwkkVLDNVAL-----GLTGDwqpAARRALEEvgLADRAN-----DWPA-ALSGGQKQRV 141
Cdd:cd03267 91 KFLRrigvVFGQKTQLwwdLP---VIDSFYLlaaiyDLPPA---RFKKRLDE--LSELLDleellDTPVrQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 142 ALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-206 |
1.61e-31 |
|
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: 121.24 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 11 PLLLEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM----- 84
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPwKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGL 153
Cdd:TIGR02857 401 VPQHPFLFA-GTIAENIRLARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVsESVAMAERVLLI 206
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRL-ALAALADRIVVL 529
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-211 |
2.61e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.44 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRY---------GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA---- 78
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 79 ----REDTRMMFQDA--RLLPWKKVLDNVALGLTG--DWQPAARRA-----LEEVGL-ADRANDWPAALSGGQKQRVALA 144
Cdd:TIGR02769 83 rrafRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHltSLDESEQKAriaelLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 145 RALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-211 |
2.87e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.39 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAP-----LADAREDTRMMFQDarllPWKK----- 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKHIGIVFQN----PDNQfvgsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 97 VLDNVALGL------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:PRK13648 101 VKYDVAFGLenhavpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506220968 171 MQEMIVSLWREHGFTVLLVTHDVSESVAmAERVLLIEDGKI 211
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-214 |
7.12e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.18 E-value: 7.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYG-----EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMM- 85
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 ----FQD------ARLlpwkKVLDNVAL------------GLTGDWQPAARRALEEV--GLADRANDWPAALSGGQKQRV 141
Cdd:COG1101 82 igrvFQDpmmgtaPSM----TIEENLALayrrgkrrglrrGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 142 ALARALIHRPGLLLLDEPLGALD---ALTRLEMQEMIVslwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKIV---EENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-206 |
8.87e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 112.71 E-value: 8.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 20 RYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL-RAGNAPLADAREDTRMmfqdARLLPwKKVL 98
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAYVPQRSEV----PDSLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 DNVALG----------LTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:NF040873 76 DLVAMGrwarrglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 506220968 169 LEMQEMIVSlWREHGFTVLLVTHDVsESVAMAERVLLI 206
Cdd:NF040873 156 ERIIALLAE-EHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-211 |
1.65e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.48 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 16 GVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--RAGNAP------LADAREDTRMMFQ 87
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfDGENIPamsrsrLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALGLTGDWQ-PAA------RRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK11831 92 SGALFTDMNVFDNVAYPLREHTQlPAPllhstvMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 161 GALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-211 |
2.68e-30 |
|
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: 110.60 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA-----DARED-TRMMFQ 87
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfasprDARRAgIAMVYQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 darllpwkkvldnvalgltgdwqpaarraleevgladrandwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:cd03216 83 ---------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506220968 168 RLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03216 118 VERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-253 |
2.78e-30 |
|
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: 117.86 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKS----TLLRLLAGLETPDGGELRAGNAPLADAREDTR---------MMFQD 88
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrrirgnriaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 --ARLLPWKKVLDNVA------LGLTGdwQPAARRA---LEEVGLAD---RANDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG4172 101 pmTSLNPLHTIGKQIAevlrlhRGLSG--AAARARAlelLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHD---VSEsvaMAERVLLIEDGKIgldmaVE-------LPHPRH 224
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVMRQGEI-----VEqgptaelFAAPQH 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 225 -----------HGTPRLAELEARVLNRV-------------MRKAPAPVRAVK 253
Cdd:COG4172 251 pytrkllaaepRGDPRPVPPDAPPLLEArdlkvwfpikrglFRRTVGHVKAVD 303
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-214 |
4.34e-30 |
|
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: 111.91 E-value: 4.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTI--LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADAREDTRMMF 86
Cdd:cd03245 5 FRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLpWKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03245 85 QDVTLF-YGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 156 LDEPLGALDalTRLEMQEM-IVSLWREHGfTVLLVTHDVSeSVAMAERVLLIEDGKIGLD 214
Cdd:cd03245 164 LDEPTSAMD--MNSEERLKeRLRQLLGDK-TLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-220 |
4.99e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.60 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 7 NQGTPLLLEGVT-KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAgnaPladarEDTRMM 85
Cdd:COG4178 358 SEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P-----AGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FqdarlLPWKKVL------DNVALGLTGDWQP--AARRALEEVGLA------DRANDWPAALSGGQKQRVALARALIHRP 151
Cdd:COG4178 430 F-----LPQRPYLplgtlrEALLYPATAEAFSdaELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 152 GLLLLDEPLGALDALTRLEMQEMIVSlwREHGFTVLLVTHDvSESVAMAERVLLIEDGKIGLDMAVELP 220
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGSWQLLPAEAP 570
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-229 |
8.37e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 5 RLNQGTPLllegvtkrygEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG---------NAPL 75
Cdd:PRK13634 11 RYQYKTPF----------ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkkNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 76 ADAREDTRMMFQ--DARLLPwKKVLDNVALGLTG------DWQPAARRALEEVGLA----DRAndwPAALSGGQKQRVAL 143
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFE-ETVEKDICFGPMNfgvseeDAKQKAREMIELVGLPeellARS---PFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 144 ARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLdmavelphpr 223
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL---------- 226
|
....*.
gi 506220968 224 hHGTPR 229
Cdd:PRK13634 227 -QGTPR 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-211 |
1.06e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.98 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 19 KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARED----------------T 82
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrllrT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 R--MMFQDARLLPWKKVLDNV------ALGLT-GDWQPAARRALEEVGLADRAND-WPAALSGGQKQRVALARALIHRPG 152
Cdd:PRK10619 93 RltMVFQHFNLWSHMTVLENVmeapiqVLGLSkQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-229 |
1.27e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.10 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA------REDTRMMFQ--DARLLPw 94
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenlwdiRNKAGMVFQnpDNQIVA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 KKVLDNVA-----LGLtgdwQPAARR-----ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:PRK13633 101 TIVEEDVAfgpenLGI----PPEEIRervdeSLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 165 ALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAmAERVLLIEDGKIGLDmavelphprhhGTPR 229
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME-----------GTPK 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-211 |
1.49e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.89 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELragnapLADAREDTRM-MFQDAR 90
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI------FLDGEDITHLpMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 L----LP------WK-KVLDNVALGL-TGDWQPAARRA-----LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG1137 78 LgigyLPqeasifRKlTVEDNILAVLeLRKLSKKEREErleelLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
3.09e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.51 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 1 MTTSRLNQGTPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGL-ETPDG----GELRAGNAPL 75
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 76 ADARED-----TR--MMFQDARLLPwKKVLDNVALGL-------TGDWQPAARRALEEVGL----ADRANDWPAALSGGQ 137
Cdd:COG1117 81 YDPDVDvvelrRRvgMVFQKPNPFP-KSIYDNVAYGLrlhgiksKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 138 KQRVALARALIHRPGLLLLDEPLGALD--ALTRLEmqEMIVSLwREHgFTVLLVTHD------VSESVA---MAErvlLI 206
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILEL-KKD-YTIVIVTHNmqqaarVSDYTAffyLGE---LV 232
|
....
gi 506220968 207 EDGK 210
Cdd:COG1117 233 EFGP 236
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-211 |
3.24e-29 |
|
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: 115.73 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTI--LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADAREDTRMMF 86
Cdd:TIGR03375 466 FRNVSFAYPGQETpaLDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqidpADLRRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLpWKKVLDNVALGltgdwQPAAR-----RALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHR 150
Cdd:TIGR03375 546 QDPRLF-YGTLRDNIALG-----APYADdeeilRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 151 PGLLLLDEPLGALDAltRLEMQeMIVSLWRE-HGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:TIGR03375 620 PPILLLDEPTSAMDN--RSEER-FKDRLKRWlAGKTLVLVTHRTS-LLDLVDRIIVMDNGRI 677
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-211 |
4.26e-29 |
|
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: 109.63 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKT--ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLL-------AGLETPDGGELRAgnAPLADAREDTRM 84
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGHDVRD--YTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPwKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGL 153
Cdd:cd03251 81 VSQDVFLFN-DTVAENIAYGRPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLWRehGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKI 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-211 |
4.99e-29 |
|
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: 109.50 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRMMF 86
Cdd:cd03252 3 FEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPwKKVLDNVALGLTGdwqPAARRALEEVGLADrANDW---------------PAALSGGQKQRVALARALIHRP 151
Cdd:cd03252 83 QENVLFN-RSIRDNIALADPG---MSMERVIEAAKLAG-AHDFiselpegydtivgeqGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 152 GLLLLDEPLGALDaltrLEMQEMIVSLWRE--HGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:cd03252 158 RILIFDEATSALD----YESEHAIMRNMHDicAGRTVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-192 |
6.96e-29 |
|
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: 113.99 E-value: 6.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLLLEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDT---- 82
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 -RMMFQDARLLPwKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHR 150
Cdd:TIGR02868 411 vSVCAQDAHLFD-TTVRENLRLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLwrEHGFTVLLVTHD 192
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-191 |
1.22e-28 |
|
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: 107.44 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREdtrmmfQDARL 91
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD------EPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLT------------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:TIGR01189 75 ILYLGHLPGLKPELSalenlhfwaaihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 506220968 160 LGALDAltrlEMQEMIVSLWREH---GFTVLLVTH 191
Cdd:TIGR01189 155 TTALDK----AGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-211 |
1.88e-28 |
|
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: 108.01 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEK---TILNALDLHVPAGQFVAVVGRSGGGKSTLLRLL-------AGLETPDGGELRAGNapLADAREDTR 83
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVDIRDLN--LRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 MMFQDARLLPwKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPG 152
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLWRehGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-210 |
2.14e-28 |
|
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: 105.22 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGnapladaredtrmmfqdarllp 93
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 wkkvlDNVALGLTgdwqpaarraleevgladrandwpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrLEMQE 173
Cdd:cd03221 61 -----STVKIGYF------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIE 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 506220968 174 MIVSLWREHGFTVLLVTHDVS--ESVamAERVLLIEDGK 210
Cdd:cd03221 108 ALEEALKEYPGTVILVSHDRYflDQV--ATKIIELEDGK 144
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-210 |
2.80e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.12 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 11 PLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMF---- 86
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPWKKVLDNVAL-----GLTGdwqpAARRA-----LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVfgryfGLSA----AAARAlvpplLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWrEHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-229 |
3.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.60 E-value: 3.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 7 NQGTPLllegvtkrygEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETP-------DGGELRAGNAPLADAR 79
Cdd:PRK13637 13 MEGTPF----------EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPtsgkiiiDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTRMMFQ--DARLLPwKKVLDNVA-----LGLT-GDWQPAARRALEEVGL-----ADRAndwPAALSGGQKQRVALARA 146
Cdd:PRK13637 83 KKVGLVFQypEYQLFE-ETIEKDIAfgpinLGLSeEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 147 LIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDmavelphprhhG 226
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ-----------G 227
|
...
gi 506220968 227 TPR 229
Cdd:PRK13637 228 TPR 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-211 |
6.73e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 106.54 E-value: 6.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRMMFQD 88
Cdd:cd03254 6 ENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPwKKVLDNVALGltgdwQPAAR-----RALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPG 152
Cdd:cd03254 86 TFLFS-GTIMENIRLG-----RPNATdeeviEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLwrEHGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-236 |
7.09e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.51 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLLL-EGVTKRY--------GEKTI--LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR------- 69
Cdd:PRK11308 1 SQQPLLQaIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 70 -AGNAPLADAREDTRMMFQD--ARLLPWKKVLDNVA--LGLTGDWQPAARRA-----LEEVGL-ADRANDWPAALSGGQK 138
Cdd:PRK11308 81 kADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQILEepLLINTSLSAAERREkalamMAKVGLrPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 139 QRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKigldmAVE 218
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR-----CVE 235
|
250 260 270
....*....|....*....|....*....|..
gi 506220968 219 L-------PHPRH-------HGTPRLAELEAR 236
Cdd:PRK11308 236 KgtkeqifNNPRHpytqallSATPRLNPDDRR 267
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-228 |
8.24e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD------AREDT 82
Cdd:PRK11300 3 QPLLsVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghqiARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNVALG---------LTGDWQ-PAARRA-----------LEEVGLADRANDWPAALSGGQKQRV 141
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAqhqqlktglFSGLLKtPAFRRAesealdraatwLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 142 ALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKigldmavelph 221
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT----------- 231
|
....*..
gi 506220968 222 PRHHGTP 228
Cdd:PRK11300 232 PLANGTP 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-211 |
9.74e-28 |
|
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: 110.66 E-value: 9.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLL-LEGVTKRYG--EKTILNALD---LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL--RAGN--APLAD 77
Cdd:TIGR03269 275 VGEPIIkVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDewVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 78 AREDTR--------MMFQDARLLPWKKVLDNV--ALGLTGDWQPAARRA---LEEVGLADRA-----NDWPAALSGGQKQ 139
Cdd:TIGR03269 355 PGPDGRgrakryigILHQEYDLYPHRTVLDNLteAIGLELPDELARMKAvitLKMVGFDEEKaeeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 140 RVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-228 |
9.86e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.32 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR-----MMFQD 88
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrlaILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ----ARLlpwkKVLDNVALG--------LTG-DWQpAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG4604 84 nhinSRL----TVRELVAFGrfpyskgrLTAeDRE-IIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIgldmavelphpRHHGTP 228
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV-----------VAQGTP 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-195 |
1.34e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 6 LNQGTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----R 79
Cdd:PRK10247 1 MQENSPLLqLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeiyR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTRMMFQDARLLPwKKVLDNVALgltgDWQ-------PAA-RRALEEVGLADRANDWP-AALSGGQKQRVALARALIHR 150
Cdd:PRK10247 81 QQVSYCAQTPTLFG-DTVYDNLIF----PWQirnqqpdPAIfLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSE 195
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-211 |
1.35e-27 |
|
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: 105.78 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYG-EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRMMFQ 87
Cdd:cd03253 3 FENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtldslRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPwKKVLDNVALGLTGDWQPAARRALEEVGLADRANDWPAA-----------LSGGQKQRVALARALIHRPGLLLL 156
Cdd:cd03253 83 DTVLFN-DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWRehGFTVLLVTHDVSEsVAMAERVLLIEDGKI 211
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-211 |
1.81e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLllegvtkrygEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL---------RAGNAPLADAR 79
Cdd:PRK13641 15 GTPM----------EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpETGNKNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTRMMFQ--DARLLPwKKVLDNVALG---LTGDWQPAARRALE---EVGLA-DRANDWPAALSGGQKQRVALARALIHR 150
Cdd:PRK13641 85 KKVSLVFQfpEAQLFE-NTVLKDVEFGpknFGFSEDEAKEKALKwlkKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-191 |
3.12e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 104.12 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDtrmMFQD-----------AR 90
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---YHQDllylghqpgikTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALGLTGDwQPAARRALEEVGLADRAnDWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDA---- 165
Cdd:PRK13538 89 LTALENLRFYQRLHGPGD-DEALWEALAQVGLAGFE-DVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKqgva 166
|
170 180
....*....|....*....|....*..
gi 506220968 166 -LTRLEMQEMivslwrEHGFTVLLVTH 191
Cdd:PRK13538 167 rLEALLAQHA------EQGGMVILTTH 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-211 |
3.65e-27 |
|
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: 104.37 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKT----ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE-----LRAGNAPlADAREDT 82
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgFDVVKEP-AEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNVAL-----GLTGDwqpAARRALEEV----GLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaglyGLKGD---ELTARLEELadrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-214 |
5.19e-27 |
|
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: 102.78 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQdarLLPWKKVLDNVA 102
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS---VLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 103 LgltgdwqpaarraLEEVGladrandwpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREH 182
Cdd:cd03247 91 L-------------RNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK 148
|
170 180 190
....*....|....*....|....*....|..
gi 506220968 183 gfTVLLVTHDVSeSVAMAERVLLIEDGKIGLD 214
Cdd:cd03247 149 --TLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-211 |
6.79e-27 |
|
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: 108.65 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAR-EDTRMMF----Q 87
Cdd:TIGR02203 334 RNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlASLRRQValvsQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPwKKVLDNVALGLTGDWQPA-ARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGLLL 155
Cdd:TIGR02203 414 DVVLFN-DTIANNIAYGRTEQADRAeIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
8.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAP-------LADAREDTR 83
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysrkgLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 MMFQDA-RLLPWKKVLDNVALGLTG------DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK13636 86 MVFQDPdNQLFSASVYQDVSFGAVNlklpedEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-213 |
9.03e-27 |
|
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: 103.25 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELragnapLADAREDTRMMFQDARL 91
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI------IFDGHPWTRKDLHKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 L----PWKKVL---DNVALGLTGDWQPAAR--RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:TIGR03740 75 LiespPLYENLtarENLKVHTTLLGLPDSRidEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 163 LDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGL 213
Cdd:TIGR03740 155 LDPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGY 204
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-224 |
1.05e-26 |
|
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: 103.76 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 11 PLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADaREDTRMMFQDA 89
Cdd:TIGR02323 2 PLLqVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAE-LELYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLL---PWKKVLDNVALGLT---------------------GDWQPAARRALEEVGL-ADRANDWPAALSGGQKQRVALA 144
Cdd:TIGR02323 81 RRLmrtEWGFVHQNPRDGLRmrvsaganigerlmaigarhyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 145 RALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI---GLDMAVeLPH 221
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesGLTDQV-LDD 239
|
...
gi 506220968 222 PRH 224
Cdd:TIGR02323 240 PQH 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
36-230 |
1.21e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.10 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 36 AGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA--DAR---EDTRMMFQDA--RLLPWKKV--LDNVALGLT 106
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSyrsQRIRMIFQDPstSLNPRQRIsqILDFPLRLN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 107 GDWQPAARR-----ALEEVGL-ADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWR 180
Cdd:PRK15112 118 TDLEPEQREkqiieTLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 181 EHGFTVLLVTHDVSESVAMAERVLLIEDGKI---GlDMAVELPHPRHHGTPRL 230
Cdd:PRK15112 198 KQGISYIYVTQHLGMMKHISDQVLVMHQGEVverG-STADVLASPLHELTKRL 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-211 |
1.39e-26 |
|
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: 102.58 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMM---- 85
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVAL-----GLTGDWQPA-ARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFyarlkGLPKSEIKEeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-211 |
1.80e-26 |
|
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: 107.14 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMF--- 86
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHigy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 --QDARLLPwKKVLDNVALglTGDWQP-----AARRA-LEE--VGLAD----RANDWPAALSGGQKQRVALARALIHRPG 152
Cdd:COG4618 411 lpQDVELFD-GTIAENIAR--FGDADPekvvaAAKLAgVHEmiLRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-211 |
2.15e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--AREDTRMMfq 87
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRQLARRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 daRLLPWK-------KVLDNVALG----------LTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:PRK11231 79 --ALLPQHhltpegiTVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-229 |
4.56e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA-----------DAREDTRMM 85
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgrsifnyrdvlEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPwKKVLDNVALGLTG-------DWQPAARRALEEVGL----ADRANDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK14271 107 FQRPNPFP-MSIMDNVLAGVRAhklvprkEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREhgFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE--LPHPRHHGTPR 229
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEqlFSSPKHAETAR 260
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-211 |
5.23e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 5.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPDGGELRAGN----APLADA---REDTRMMFQD 88
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrniySPDVDPievRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLTGDWQPAARRALEEV------------GLADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKELDERvewalkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWREhgFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-210 |
7.63e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 100.24 E-value: 7.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 26 ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG-------------NAPLAD----AREdtrmmFQD 88
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgsiayvsqepwiqNGTIREnilfGKP-----FDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLlpwKKVLDNVALGL------TGDwqpaarraLEEVGlaDRAndwpAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03250 95 ERY---EKVIKACALEPdleilpDGD--------LTEIG--EKG----INLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALT-RLEMQEMIVSLWREHGfTVLLVTHDVsESVAMAERVLLIEDGK 210
Cdd:cd03250 158 VDAHVgRHIFENCILGLLLNNK-TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-211 |
1.38e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADARED-T 82
Cdd:COG1129 2 EPLLeMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrspRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNVALG--LTG----DWQ---PAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGrePRRggliDWRamrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 154 LLLDEPlgaLDALTRLEMQ---EMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1129 162 LILDEP---TASLTEREVErlfRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-209 |
1.92e-25 |
|
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: 99.82 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLLEGVTKRY-----GEKTI--LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE--LRAGNAPLADARE 80
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMMF-----------QDARLLPWKKVLDNVAlgltgdwQPAARRALEEVGLADRANDW--------------PAALSG 135
Cdd:COG4778 83 SPREILalrrrtigyvsQFLRVIPRVSALDVVA-------EPLLERGVDREEARARARELlarlnlperlwdlpPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506220968 136 GQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDG 209
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
2.40e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.84 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYG--EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETP-------DGGELRAGNapLADAREDTRM 84
Cdd:PRK13632 10 VENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPqsgeikiDGITISKEN--LKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQ--DARLLPwKKVLDNVALGLT------GDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK13632 88 IFQnpDNQFIG-ATVEDDIAFGLEnkkvppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVaMAERVLLIEDGKI 211
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-211 |
2.77e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 99.53 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 19 KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGG------------ELRAGNAPLADAREDTRMMf 86
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtvtvrgrvssllGLGGGFNPELTGRENIYLN- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 qdARLLpwkkvldnvalGLTGDwQPAARraLEEV----GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03220 109 --GRLL-----------GLSRK-EIDEK--IDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03220 173 GDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-232 |
2.91e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.45 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--AREDTR---MMFQDA 89
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARrigLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNVALG------LTGDW----QPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK10253 91 TTPGDITVQELVARGryphqpLFTRWrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 160 LGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAvelphPRHHGTPRLAE 232
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-----PKEIVTAELIE 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-210 |
3.52e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD----AREDTRMMFQDA 89
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArarlARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RLLPWKKVLDNvaLGLTGDWQPAARRALEEV--------GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK13536 124 NLDLEFTVREN--LLVFGRYFGMSTREIEAVipsllefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 162 ALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-211 |
3.68e-25 |
|
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: 99.14 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTR----MMF- 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaragIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 -QDARLLPWKKVLDNVALGLTGdwQPAARR-----------ALEEVgLADRANDwpaaLSGGQKQRVALARALIHRPGLL 154
Cdd:TIGR03410 81 pQGREIFPRLTVEENLLTGLAA--LPRRSRkipdeiyelfpVLKEM-LGRRGGD----LSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-203 |
4.04e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.86 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 3 TSRLNQGTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLR-------LLAGLE-----TPDGGELR 69
Cdd:PRK14243 1 TSTLNGTETVLrTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRvegkvTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 70 AGNAPLADAREDTRMMFQDARLLPwKKVLDNVA-----LGLTGDWQPAARRALEEVGL----ADRANDWPAALSGGQKQR 140
Cdd:PRK14243 81 APDVDPVEVRRRIGMVFQKPNPFP-KSIYDNIAygariNGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 141 VALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhgFTVLLVTHDVSEsvamAERV 203
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQ----AARV 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
27-211 |
5.19e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE-------LRAGNAPLADAREDTRMMFQ---DARLLPwkK 96
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlikgepIKYDKKSLLEVRKTVGIVFQnpdDQLFAP--T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 97 VLDNVA-----LGLTGD-WQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:PRK13639 96 VEEDVAfgplnLGLSKEeVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506220968 171 MQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-224 |
5.56e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.94 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALD---LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE--------LRAGNAPLADAREDTRMMFQD--ARLLP 93
Cdd:PRK15079 34 LKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvawlgkdlLGMKDDEWRAVRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 WKKVLDNVALGLTgDWQPAARRA---------LEEVGL-ADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:PRK15079 114 RMTIGEIIAEPLR-TYHPKLSRQevkdrvkamMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 164 DALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKigldmAVEL-------PHPRH 224
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH-----AVELgtydevyHNPLH 255
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-191 |
8.42e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 98.11 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 16 GVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGletpdggelRAGNAPLADAREdtrmmFQDARLLPWK 95
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------ALKGTPVAGCVD-----VPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 KVLDNValGLTGDwQPAARRALEEVGLADRANdW---PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:COG2401 101 SLIDAI--GRKGD-FKDAVELLNAVGLSDAVL-WlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*....
gi 506220968 173 EMIVSLWREHGFTVLLVTH 191
Cdd:COG2401 177 RNLQKLARRAGITLVVATH 195
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-211 |
8.91e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.81 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 30 LDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGN---------APLADAREDTRMMFQ--DARLLPwKKVL 98
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIKPVRKKVGVVFQfpESQLFE-ETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 DNVALGLTG------DWQPAARRALEEVGLADRAndW---PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:PRK13643 104 KDVAFGPQNfgipkeKAEKIAAEKLEMVGLADEF--WeksPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506220968 170 EMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13643 182 EMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-227 |
1.13e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 98.46 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-----AGNAPLADAREDTR 83
Cdd:PRK11701 4 QPLLsVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdGQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 mmfqdaRLL---PWKKVLDNVALGLT---------------------GDWQPAARRALEEVGL-ADRANDWPAALSGGQK 138
Cdd:PRK11701 84 ------RRLlrtEWGFVHQHPRDGLRmqvsaggnigerlmavgarhyGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 139 QRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI---GLDM 215
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesGLTD 237
|
250
....*....|..
gi 506220968 216 AVeLPHPRHHGT 227
Cdd:PRK11701 238 QV-LDDPQHPYT 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-229 |
1.29e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.45 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPDGGELRAG-----NAPLADAREDTRMMFQDAR 90
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDgqdifKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALGLT--------GDWQPAARRALEEVGLADRAND---WPAA-LSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK14247 93 PIPNLSIFENVALGLKlnrlvkskKELQERVRWALEKAQLWDEVKDrldAPAGkLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREhgFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE--LPHPRHHGTPR 229
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRevFTNPRHELTEK 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-211 |
1.63e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.85 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 24 KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLE------TPDGGELRagNAPLADAREDTRMMFQDArLLPWKKV 97
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLpyqgslKINGIELR--ELDPESWRKHLSWVGQNP-QLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 98 LDNVALGLTGDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506220968 167 TRLEMQEMIVSLWREHgfTVLLVTHDVSESVAMaERVLLIEDGKI 211
Cdd:PRK11174 520 SEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-210 |
1.73e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.26 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADARedt 82
Cdd:COG3845 2 MPPALeLRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirspRDAI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 R----MMFQDARLLPWKKVLDNVALGLTGDWQP-----AARRALEEvgLADRAN---DwPAA----LSGGQKQRVALARA 146
Cdd:COG3845 79 AlgigMVHQHFMLVPNLTVAENIVLGLEPTKGGrldrkAARARIRE--LSERYGldvD-PDAkvedLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 147 LIHRPGLLLLDEPLGaldALTRLEMQEMIVSLWR--EHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:COG3845 156 LYRGARILILDEPTA---VLTPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-211 |
2.84e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.05 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDT---RMMF 86
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrqAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPWKKVL-DNVALGltgdwQPAA-----RRALEEVGLADRANDWPA----------ALSGGQKQRVALARALIHR 150
Cdd:PRK11160 419 VSQRVHLFSATLrDNLLLA-----APNAsdealIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 151 PGLLLLDEPLGALDALTrlEMQemIVSLWREH--GFTVLLVTHDVSESVAMaERVLLIEDGKI 211
Cdd:PRK11160 494 APLLLLDEPTEGLDAET--ERQ--ILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-191 |
3.95e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.71 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMF---QD 88
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ArLLPWKKVLDNVAL--GLTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALI-HRPgLLLLDEPLGALDA 165
Cdd:PRK13539 83 A-MKPALTVAENLEFwaAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALDA 160
|
170 180
....*....|....*....|....*....
gi 506220968 166 LTrlemQEMIVSLWREH---GFTVLLVTH 191
Cdd:PRK13539 161 AA----VALFAELIRAHlaqGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-214 |
1.06e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAREDTR----MMFQDARL 91
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPFKRRKEFARrigvVFGQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 ---LPwkkVLDNVAL-----GLTgdwQPAARRALEEV----GLAD------RAndwpaaLSGGQKQRVALARALIHRPGL 153
Cdd:COG4586 108 wwdLP---AIDSFRLlkaiyRIP---DAEYKKRLDELvellDLGElldtpvRQ------LSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 154 LLLDEP-LGaLDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:COG4586 176 LFLDEPtIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-211 |
1.64e-23 |
|
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: 99.12 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAR------------ED 81
Cdd:COG5265 361 ENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTqaslraaigivpQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TrMMFQDArllpwkkVLDNVALGltgdwQPAARRalEEVGLADRAndwpAA----------------------LSGGQKQ 139
Cdd:COG5265 441 T-VLFNDT-------IAYNIAYG-----RPDASE--EEVEAAARA----AQihdfieslpdgydtrvgerglkLSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 140 RVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLS-TIVDADEILVLEAGRI 570
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-211 |
3.69e-23 |
|
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: 93.69 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLLEGVTK---------RYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD--- 77
Cdd:cd03248 4 APDHLKGIVKfqnvtfaypTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyeh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 78 --AREDTRMMFQDARLLPwKKVLDNVALGLTG----DWQPAARRA-------LEEVGLADRANDWPAALSGGQKQRVALA 144
Cdd:cd03248 84 kyLHSKVSLVGQEPVLFA-RSLQDNIAYGLQScsfeCVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 145 RALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-222 |
5.00e-23 |
|
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: 93.33 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD-AREDTRMMF----Q 87
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRIsiipQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLP--WKKVLDnvALGLTGDWQpaARRALEEVGLADRANDWPAAL-----------SGGQKQRVALARALIHRPGLL 154
Cdd:cd03244 86 DPVLFSgtIRSNLD--PFGEYSDEE--LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 155 LLDEPLGALDALTRLEMQEMIvslwREH--GFTVLLVTHDVsESVAMAERVLLIEDGKIgldmaVELPHP 222
Cdd:cd03244 162 VLDEATASVDPETDALIQKTI----REAfkDCTVLTIAHRL-DTIIDSDRILVLDKGRV-----VEFDSP 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-211 |
5.64e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL--ADAREDTRMMF 86
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeaLSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 ---QDARLLPWKKVLDNVALGLT------GDWQP----AARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGL 153
Cdd:PRK09536 81 svpQDTSLSFEFDVRQVVEMGRTphrsrfDTWTEtdraAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-211 |
8.77e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 96.71 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD-----AREDTRMMFQ 87
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPwKKVLDNVALGLTGD----WQpaarrALEEVGLADRANDWPAA-----------LSGGQKQRVALARALIHRPG 152
Cdd:PRK10790 423 DPVVLA-DTFLANVTLGRDISeeqvWQ-----ALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLwREHGfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAV-REHT-TLVVIAHRLS-TIVEADTILVLHRGQA 552
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-240 |
1.01e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLllegvtkrygEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG---------NAPLADAR 79
Cdd:PRK13649 15 GTPF----------EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstskNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTRMMFQ--DARLLPwKKVLDNVALGLTG------DWQPAARRALEEVGLADRANDW-PAALSGGQKQRVALARALIHR 150
Cdd:PRK13649 85 KKVGLVFQfpESQLFE-ETVLKDVAFGPQNfgvsqeEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD-------MAVELPHPR 223
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSgkpkdifQDVDFLEEK 242
|
250
....*....|....*..
gi 506220968 224 HHGTPRLAELEARVLNR 240
Cdd:PRK13649 243 QLGVPKITKFAQRLADR 259
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-211 |
1.40e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETP-------DGGELRAGNapLADAREDTRMMFQDA-RLLPWKKVL 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfegkvkiDGELLTAEN--VWNLRRKIGMVFQNPdNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 DNVALGLTGDWQPAAR------RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:PRK13642 101 DDVAFGMENQGIPREEmikrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 506220968 173 EMIVSLWREHGFTVLLVTHDVSESvAMAERVLLIEDGKI 211
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-211 |
3.71e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 16 GVTKR-YGEKTILNALDLHVPAGQFVAVVGRSGGGKST----LLRLLA--GLETPDGGELRAGN-APLADAREDTRMMFQ 87
Cdd:PRK15134 290 GILKRtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNLNrRQLLPVRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 D--ARLLPWKKVLDNVALGLTGDwQP---AARR------ALEEVGL-ADRANDWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK15134 370 DpnSSLNPRLNVLQIIEEGLRVH-QPtlsAAQReqqviaVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-211 |
4.45e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLL------------AGLETPDGGELRAGNAPLADAREDTRMMFQD 88
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKkVLDNVALGL----TGDWQ---PAARRAL------EEVglADRANDWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK14239 95 PNPFPMS-IYENVVYGLrlkgIKDKQvldEAVEKSLkgasiwDEV--KDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 156 LDEPLGALDALTRLEMQEMIVSLwrEHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-212 |
6.87e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAreDTRMMFQDARLLPWKKVL---- 98
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY--DHHYLHRQVALVGQEPVLfsgs 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 --DNVALGLTGDWQPAARRALEEVGLADRANDWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:TIGR00958 571 vrENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 166 LTRLEMQEmivslWRE-HGFTVLLVTHDVSeSVAMAERVLLIEDGKIG 212
Cdd:TIGR00958 651 ECEQLLQE-----SRSrASRTVLLIAHRLS-TVERADQILVLKKGSVV 692
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-211 |
9.33e-22 |
|
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: 89.15 E-value: 9.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGL--ETPDGGELRAGNAPLadaredtrmmfqdaRLLPWKKVL- 98
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--------------DKRSFRKIIg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 ----DNVALG-LTgdwqpaARRALeevgladrandWPAA----LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03213 86 yvpqDDILHPtLT------VRETL-----------MFAAklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 506220968 170 EMQEMIVSLwREHGFTVLLVTHDVSESV-AMAERVLLIEDGKI 211
Cdd:cd03213 149 QVMSLLRRL-ADTGRTIICSIHQPSSEIfELFDKLLLLSQGRV 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-211 |
1.09e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLE-------TPDGGELRAGNAPLA-DA---REDTRMMFQDARL 91
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQiDAiklRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLTG-------DWQPAARRALEEVGL----ADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK14246 102 FPHLSIYDNIAYPLKShgikekrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 161 GALDALTRLEMQEMIVSLWREhgFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-254 |
1.77e-21 |
|
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: 92.94 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLET--PDGGEL-----------------RAG-NA 73
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGePC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 74 PL--------------------ADAREDTRMMFQDA-RLLPWKKVLDNV-----ALGLTGDwqPAARRA---LEEVGLAD 124
Cdd:TIGR03269 83 PVcggtlepeevdfwnlsdklrRRIRKRIAIMLQRTfALYGDDTVLDNVlealeEIGYEGK--EAVGRAvdlIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 125 RANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTH--DVSESVamAER 202
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIEDL--SDK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 506220968 203 VLLIEDGKIgldmavelphpRHHGTPrlaeleARVLNRVMRKAPAPVRAVKV 254
Cdd:TIGR03269 239 AIWLENGEI-----------KEEGTP------DEVVAVFMEGVSEVEKECEV 273
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-211 |
1.87e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNA-----PL-ADAREDTRMM 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALGL-------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLqirddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-204 |
2.20e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.88 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMMFQDA---- 89
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAympq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 ----RLLPWKKVLDNVAL--GLTGdwQPAARRA------LEEVGLA---DRandwPAA-LSGGQKQRVALARALIHRPGL 153
Cdd:NF033858 84 glgkNLYPTLSVFENLDFfgRLFG--QDAAERRrridelLRATGLApfaDR----PAGkLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 154 LLLDEPLGALDALTRLEMQEMIVSLWREH-GFTVLLVTHDVSES------VAM-AERVL 204
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAerfdwlVAMdAGRVL 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
2.58e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAREDTR----MMFQ 87
Cdd:PRK13647 7 VEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWVRskvgLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DarllPWKKVL-----DNVA-----LGLTGD-WQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK13647 87 D----PDDQVFsstvwDDVAfgpvnMGLDKDeVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 157 DEPLGALDALTRLEMQEMivsLWREH--GFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEI---LDRLHnqGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-211 |
2.59e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRA-GN-APLAD----------AR 79
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGRvSALLElgagfhpeltGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 EDTRMMfqdARLlpwkkvldnvaLGLTGDwqpAARRALEEV----GLADRAnDWPA-ALSGGQKQRVALARALIHRPGLL 154
Cdd:COG1134 107 ENIYLN---GRL-----------LGLSRK---EIDEKFDEIvefaELGDFI-DQPVkTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 155 LLDEPLGALDA------LTRleMQEMivslwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1134 169 LVDEVLAVGDAafqkkcLAR--IREL-----RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-211 |
5.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKT-----ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGN----------APLA 76
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 77 DAREDTRMMFQDARLLPWKKVLD-NVALG---LTGDWQPAARRALEEVGLADRANDW----PAALSGGQKQRVALARALI 148
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEkDIAFGpvnLGENKQEAYKKVPELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 149 HRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-234 |
6.98e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKS-TLLRLLAGLETPD----GGELRAGNAPLADAREDT---------RMMFQD 88
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTlrgvrgnkiAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 --ARLLPW---KKVLDNVALGLTGDWQPAAR----RALEEVGL---ADRANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK15134 101 pmVSLNPLhtlEKQLYEVLSLHRGMRREAARgeilNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKigldmAVE-------LPHPRHHGTPR 229
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR-----CVEqnraatlFSAPTHPYTQK 255
|
....*
gi 506220968 230 LAELE 234
Cdd:PRK15134 256 LLNSE 260
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-219 |
9.58e-21 |
|
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: 86.81 E-value: 9.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPDGGELRAGNAPLADAREDTRmmfqdA 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEER-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 RllpwkkvldnvaLGLTGDWQ-PAarrALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTR 168
Cdd:cd03217 76 R------------LGIFLAFQyPP---EIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 169 LEMQEMIVSLWREHGFTVLLVTH--DVSESVAmAERVLLIEDGKI----GLDMAVEL 219
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIvksgDKELALEI 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-211 |
1.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-----REDTRMMFQ---DARLLP 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevRKFVGLVFQnpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 wkKVLDNVALGLTG---DWQPAARR---ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK13652 95 --TVEQDIAFGPINlglDEETVAHRvssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506220968 168 RLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-211 |
1.75e-20 |
|
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: 90.10 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDT-----RM 84
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkhiGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPwKKVLDNVALgLTGDWQP-----AARRA-LEEV------GLADRANDWPAALSGGQKQRVALARALIHRPG 152
Cdd:TIGR01842 397 LPQDVELFP-GTVAENIAR-FGENADPekiieAAKLAgVHELilrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 153 LLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-211 |
2.05e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.22 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKT--ILNALD---LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL-------RAGNAPLADAREDTRM 84
Cdd:PRK13651 8 IVKIFNKKLptELKALDnvsVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKEKVLEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 85 MFQDARLLPWKKVLD----------------------------NVALGLTGdwQPAARRA---LEEVGLA----DRAndw 129
Cdd:PRK13651 88 VIQKTRFKKIKKIKEirrrvgvvfqfaeyqlfeqtiekdiifgPVSMGVSK--EEAKKRAakyIELVGLDesylQRS--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 130 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDG 209
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 506220968 210 KI 211
Cdd:PRK13651 242 KI 243
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-202 |
2.22e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.15 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 1 MTTSRLNQGTPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAre 80
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMMFQDARLLPWK-------KVLDNVALG------LTGDWQPAARRALEE----VGLADRANDWPAALSGGQKQRVAL 143
Cdd:PRK10575 79 SSKAFARKVAYLPQQlpaaegmTVRELVAIGrypwhgALGRFGAADREKVEEaislVGLKPLAHRLVDSLSGGERQRAWI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 144 ARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSesvaMAER 202
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDIN----MAAR 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-211 |
2.71e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLL-------AGLETPDGGELRagNAPLADAREDTRMMFQDARLLPwK 95
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLDGHDLR--DYTLASLRNQVALVSQNVHLFN-D 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 KVLDNVALGLTG-----DWQPAAR--RALE-----EVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:PRK11176 432 TIANNIAYARTEqysreQIEEAARmaYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 164 DALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:PRK11176 512 DTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEI 556
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-208 |
3.83e-20 |
|
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: 84.13 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 24 KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELragnaplaDAREDTRMMFqdarlLPWKKVLDNVAL 103
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLF-----LPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 104 gltgdwqpaaRRALeevgladrANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlEMQEMIVSLWREHG 183
Cdd:cd03223 81 ----------REQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKELG 138
|
170 180
....*....|....*....|....*.
gi 506220968 184 FTVLLVTHdvSESV-AMAERVLLIED 208
Cdd:cd03223 139 ITVISVGH--RPSLwKFHDRVLDLDG 162
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-214 |
6.49e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKT-ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE-----LRAGN-APLADAREDTRMMF 86
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvlvsgIDTGDfSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARL-LPWKKVLDNVALGLTGDWQPAAR------RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK13644 84 QNPETqFVGRTVEEDLAFGPENLCLPPIEirkrvdRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 160 LGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVsESVAMAERVLLIEDGKIGLD 214
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNL-EELHDADRIIVMDRGKIVLE 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-211 |
1.03e-19 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 84.73 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 30 LDLHVPAGQFVAVVGRSGGGKST----LLRLLAGLETPDGGELRAGNAPLADAR---EDTRMMFQDAR--LLPWKKVLDN 100
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSirgRHIATIMQNPRtaFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 101 V------ALGLTGDWQPAARRALEEVGLADRA---NDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:TIGR02770 85 AietlrsLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 506220968 172 QEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-191 |
1.42e-19 |
|
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: 83.70 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTrmmfqdARL 91
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI------ARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLTGD-----WQP-----AARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03231 75 LLYLGHAPGIKTTLSVLenlrfWHAdhsdeQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|...
gi 506220968 162 ALDALTrlemQEMIVSLWREH---GFTVLLVTH 191
Cdd:cd03231 155 ALDKAG----VARFAEAMAGHcarGGMVVLTTH 183
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-214 |
1.61e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD------AREDTRMM 85
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 FQDARLLPWKKVLDNVALG-LTGDWQPAARRaLEEV-----GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGgFFAERDQFQER-IKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 160 LGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-210 |
1.68e-19 |
|
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: 87.19 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLEtPDG---GELRAGNAPL-ADAREDTR---- 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLkASNIRDTEragi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 -MMFQDARLLPWKKVLDNVALG----LTG---DWQPAARRA---LEEVGLADRANDWPAA-LSGGQKQRVALARALIHRP 151
Cdd:TIGR02633 81 vIIHQELTLVPELSVAENIFLGneitLPGgrmAYNAMYLRAknlLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506220968 152 GLLLLDEPLGaldALTRLEMQEM--IVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:TIGR02633 161 RLLILDEPSS---SLTEKETEILldIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-211 |
2.22e-19 |
|
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: 82.48 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTIlnalDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA----DAREDTRMMF- 86
Cdd:cd03215 5 LEVRGLSVKGAVRDV----SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrspRDAIRAGIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 ----QDARLLPWKKVLDNVALgltgdwqpaarraleevgladrandwPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03215 81 pedrKREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506220968 163 LDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:cd03215 135 VDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-204 |
5.61e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGG------ELRAGNAPLADAREDT----- 82
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGvikrngKLRIGYVPQKLYLDTTlpltv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 -RMMfqdaRLLPWKKvldnvalglTGDWQPAarraLEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK09544 87 nRFL----RLRPGTK---------KEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVL 204
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-195 |
7.30e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDG-----GELRAGNAPLADAR-------EDTRMMFQD 88
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRvnlnrlrRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPwKKVLDNVALG--LTGdWQPA------ARRALEEVGLAD----RANDWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGvkIVG-WRPKleiddiVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSE 195
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-211 |
1.52e-18 |
|
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: 84.41 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYG-EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAreDTRMMFQDARLLPWK 95
Cdd:TIGR01193 479 VSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPQE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 ------KVLDNVALGLT-GDWQPAARRALEEVGLADRANDWP-----------AALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:TIGR01193 557 pyifsgSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220968 158 EPLGALDALTRLEMQEMIVSLWREhgfTVLLVTHDVSESvAMAERVLLIEDGKI 211
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKI 686
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-223 |
1.89e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLllegvtkrygEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAP---------LADA 78
Cdd:PRK13646 14 KGTPY----------EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 79 REDTRMMFQ--DARLLP-------------WKKVLDNValgltgdwQPAARRALEEVGLA-DRANDWPAALSGGQKQRVA 142
Cdd:PRK13646 84 RKRIGMVFQfpESQLFEdtvereiifgpknFKMNLDEV--------KNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 143 LARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIgldmaVELPHP 222
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI-----VSQTSP 230
|
.
gi 506220968 223 R 223
Cdd:PRK13646 231 K 231
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-192 |
1.97e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 81.70 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 3 TSRLNQGTPLLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARED- 81
Cdd:COG4674 2 SLDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 -TRMM----FQDARLLPWKKVLDNVALGLTGD---WQPAARR-----------ALEEVGLADRANDWPAALSGGQKQRVA 142
Cdd:COG4674 82 iARLGigrkFQKPTVFEELTVFENLELALKGDrgvFASLFARltaeerdrieeVLETIGLTDKADRLAGLLSHGQKQWLE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 143 LARALIHRPGLLLLDEPLGaldALTRLEMQ---EMIVSLWREHgfTVLLVTHD 192
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVA---GMTDAETErtaELLKSLAGKH--SVVVVEHD 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-211 |
2.28e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-----AGNAPLADAREDTRMMFQD 88
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPwKKVLDNVALGLTGDWQPAARRALE-----------EVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK13657 418 AGLFN-RSIEDNIRVGRPDATDEEMRAAAEraqahdfierkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220968 158 EPLGALDALTRLEMQEMIVSLwrEHGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:PRK13657 497 EATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-219 |
2.30e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.83 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLLE--GVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLeTPDG---GELRAGNAPL-ADAREDTR 83
Cdd:PRK13549 2 MEYLLEmkNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELqASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 -----MMFQDARLLPWKKVLDNVALG---LTG---DWQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:PRK13549 81 ragiaIIHQELALVKELSVLENIFLGneiTPGgimDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 150 RPGLLLLDEPLGaldALTRLEMQEM--IVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK-IGLDMAVEL 219
Cdd:PRK13549 161 QARLLILDEPTA---SLTESETAVLldIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRhIGTRPAAGM 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-192 |
3.96e-18 |
|
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: 83.06 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 16 GVTKRY-GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGElragnaplADAREDTR--MMFQDARLL 92
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGIKvgYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 93 PWKKVLDNVALGLtGDWQPAARRaLEEVGLA------------------------------DR------------ANDWP 130
Cdd:TIGR03719 81 PTKTVRENVEEGV-AEIKDALDR-FNEISAKyaepdadfdklaaeqaelqeiidaadawdlDSqleiamdalrcpPWDAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 131 AA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrlemqemiVSlWREHGF-----TVLLVTHD 192
Cdd:TIGR03719 159 VTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES--------VA-WLERHLqeypgTVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-192 |
4.84e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.86 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 16 GVTKRYG-EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAgnAP------LAdaredtrmmfQD 88
Cdd:PRK11819 11 RVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APgikvgyLP----------QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ARLLPWKKVLDNVALGLtGDWQPAARRaLEEVG------------LADR------------------------------A 126
Cdd:PRK11819 79 PQLDPEKTVRENVEEGV-AEVKAALDR-FNEIYaayaepdadfdaLAAEqgelqeiidaadawdldsqleiamdalrcpP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 127 NDWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlemqEMIvsLWREH------GfTVLLVTHD 192
Cdd:PRK11819 157 WDAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESV--AWLEQflhdypG-TVVAVTHD 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-211 |
6.39e-18 |
|
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: 79.62 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLEtpDGGELRAGNApLADAREDTRMMF--------QDARLLPW 94
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQI-LFNGQPRKPDQFqkcvayvrQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 KKV---LDNVALGLTGDWQPAARR-------ALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03234 96 LTVretLTYTAILRLPRKSSDAIRkkrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 165 ALTRLEMQEMIVSLWREhGFTVLLVTHD-VSESVAMAERVLLIEDGKI 211
Cdd:cd03234 176 SFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-213 |
1.10e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 7 NQGTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRMM 85
Cdd:PRK15439 6 TTAPPLLcARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 86 F------QDARLLPWKKVLDNVALGLTGDWQPAARRA--LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK15439 86 LgiylvpQEPLLFPNLSVKENILFGLPKRQASMQKMKqlLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 158 EPLGaldALTRLEMQEM---IVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGL 213
Cdd:PRK15439 166 EPTA---SLTPAETERLfsrIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-211 |
1.59e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 81.48 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAREDTRMMFQDAR 90
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIGYYAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LL-----PWKKVLDN--VALGLTGdwqpaarRALEEvglADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:PRK15064 400 TLfdwmsQWRQEGDDeqAVRGTLG-------RLLFS---QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 164 D-----AL-TRLEMQEmivslwrehGfTVLLVTHD---VSesvAMAERVLLIEDGKI 211
Cdd:PRK15064 470 DmesieSLnMALEKYE---------G-TLIFVSHDrefVS---SLATRIIEITPDGV 513
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-167 |
2.60e-17 |
|
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: 80.75 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGnapladarEDTRMMFQD---ARL 91
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------ETVKLAYVDqsrDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGL----TGDWQPAARRALEEVGLadRANDWP---AALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR03719 398 DPNKTVWEEISGGLdiikLGKREIPSRAYVGRFNF--KGSDQQkkvGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
...
gi 506220968 165 ALT 167
Cdd:TIGR03719 476 VET 478
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-210 |
4.14e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.38 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKS----TLLRLLA------GLETPDGGE-LRAGNAPLADAR-EDTRMMFQD- 88
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangrigGSATFNGREiLNLPEKELNKLRaEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 -ARLLPWKKVLDNVALGLTGDWQPAARRALEE-VGLAD---------RANDWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEEsVRMLDavkmpearkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 158 EPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-192 |
1.01e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGN----APLADAREDtrmmfqda 89
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTklevAYFDQHRAE-------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 rLLPWKKVLDNVA---------------LGLTGDWQPAARRALEEVgladrandwpAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK11147 394 -LDPEKTVMDNLAegkqevmvngrprhvLGYLQDFLFHPKRAMTPV----------KALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190
....*....|....*....|....*....|....*...
gi 506220968 155 LLDEPLGALDALTrLEMQEmivSLWREHGFTVLLVTHD 192
Cdd:PRK11147 463 ILDEPTNDLDVET-LELLE---ELLDSYQGTVLLVSHD 496
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
1.31e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 6 LNQGTPLLLEGVTKRYGEKT-----ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARE 80
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTR---------------------MMFQDARLLPWKKVLDN------VALGLTG-DWQPAARRALEEVGLADRANDW-PA 131
Cdd:PRK13631 96 NHElitnpyskkiknfkelrrrvsMVFQFPEYQLFKDTIEKdimfgpVALGVKKsEAKKLAKFYLNKMGLDDSYLERsPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 132 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-211 |
1.40e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 37 GQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL-----RAGNAP---LADAREDTRMMFQD--ARLLPWKKVLDNVALGLT 106
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRIDTLSpgkLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 107 ----GDWQPAARRA---LEEVGL-ADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSL 178
Cdd:PRK10261 430 vhglLPGKAAAARVawlLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190
....*....|....*....|....*....|...
gi 506220968 179 WREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-222 |
1.80e-16 |
|
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: 75.53 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEK--TILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNA-----PLADAREDTRMMF 86
Cdd:cd03369 9 VENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLL--PWKKVLDnvalgltgdwqPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03369 89 QDPTLFsgTIRSNLD-----------PFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 165 ALTRLEMQEMIVSLWRehGFTVLLVTHDVSeSVAMAERVLLIEDGKIgldmaVELPHP 222
Cdd:cd03369 158 YATDALIQKTIREEFT--NSTILTIAHRLR-TIIDYDKILVMDAGEV-----KEYDHP 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-210 |
2.74e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 18 TKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGL---ETPDGGELRAGNAPLADAREDTRMMFQDARLLPW 94
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqgNNFTGTILANNRKPTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 KKVLDNVAL--------GLTGDWQP-AARRALEEVGLAD-----RANDWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PLN03211 155 LTVRETLVFcsllrlpkSLTKQEKIlVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 161 GALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESV-AMAERVLLIEDGK 210
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGR 284
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-211 |
2.76e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 77.90 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE-------------------LR 69
Cdd:PRK10636 310 NPLLkMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiglakgiklgyfaqhqlefLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 70 AGNAPLADAredtrmmfqdARLLPwkKVLDNvalgltgdwqpAARRALEEVGL-ADRANDWPAALSGGQKQRVALARALI 148
Cdd:PRK10636 390 ADESPLQHL----------ARLAP--QELEQ-----------KLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 149 HRPGLLLLDEPLGALDaltrLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10636 447 QRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-211 |
3.50e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.51 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 30 LDLHVPAGQFVAVVGRSGGGKStlLRLLAGLET-PDG-----GELRAGNAPLADAR----------EDTRMMFQDARLLP 93
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAALGIlPAGvrqtaGRVLLDGKPVAPCAlrgrkiatimQNPRSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 WKKVLDNVALGLTGDWQpAARRALEEVGLADRA---NDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:PRK10418 100 THARETCLALGKPADDA-TLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506220968 171 MQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10418 179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-209 |
5.64e-16 |
|
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: 74.29 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLL-RLLAGLETPDG----GELRAGNAPLADAREDTRMMFQDARLLPW------- 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSVAYAAQKPWllnatve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 --------------KKVLDNVALGLTGDWQPAArralEEVGLADRANDwpaaLSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03290 97 enitfgspfnkqryKAVTDACSLQPDIDLLPFG----DQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 161 GALDA-LTRLEMQEMIVSLWREHGFTVLLVTHDVsESVAMAERVLLIEDG 209
Cdd:cd03290 169 SALDIhLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-211 |
5.95e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 18 TKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPD--GGELRAGNAPLADAREDTRM---MFQDARLL 92
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkGSGSVLLNGMPIDAKEMRAIsayVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 93 PWKKVLDNVA----LGLTGDWQPAARRA-----LEEVGLADRAN------DWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:TIGR00955 112 PTLTVREHLMfqahLRMPRRVTKKEKRErvdevLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 158 EPLGALDALtrleMQEMIVSLWRE---HGFTVLLVTHD-VSESVAMAERVLLIEDGKI 211
Cdd:TIGR00955 192 EPTSGLDSF----MAYSVVQVLKGlaqKGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-166 |
1.40e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGnapladarEDTRMMFQD---ARL 91
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--------ETVKLAYVDqsrDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGL----TGDWQPAARRAL-----------EEVGLadrandwpaaLSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK11819 400 DPNKTVWEEISGGLdiikVGNREIPSRAYVgrfnfkggdqqKKVGV----------LSGGERNRLHLAKTLKQGGNVLLL 469
|
170
....*....|....*....
gi 506220968 157 DEP--------LGAL-DAL 166
Cdd:PRK11819 470 DEPtndldvetLRALeEAL 488
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-191 |
1.58e-15 |
|
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: 75.56 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTIlNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRA---------------GNAPL------ADARE 80
Cdd:TIGR00954 464 GDVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpakgklfyvpqrpymTLGTLrdqiiyPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMM-FQDARLlpwKKVLDNVALGltgdwqpaarRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:TIGR00954 543 DMKRRgLSDKDL---EQILDNVQLT----------HILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 506220968 160 LGALDaltrLEMQEMIVSLWREHGFTVLLVTH 191
Cdd:TIGR00954 610 TSAVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-207 |
2.26e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLLL--EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADArEDTRMMFQ 87
Cdd:PRK13543 8 APPLLaaHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVA-----LGLTG-DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK13543 87 LGHLPGLKADLSTLEnlhflCGLHGrRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506220968 162 ALDALTRLEMQEMIVSLWREHGFTvLLVTHDVSESVAMAERVLLIE 207
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLRGGGAA-LVTTHGAYAAPPVRTRMLTLE 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-211 |
2.49e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 20 RYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-------REDTRMMFQDA-RL 91
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgllalRQQVATVFQDPeQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLDNVALGLTGDWQPA---ARRALEEVGLAD--RANDWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK13638 90 IFYTDIDSDIAFSLRNLGVPEaeiTRRVDEALTLVDaqHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506220968 166 LTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-194 |
3.91e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.78 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 13 LLEGVTKRYGEktilNALDLH---VPA-GQFVAVVGRSGGGKSTLLRLLAGLETPD------------------GGELRA 70
Cdd:cd03236 2 LEDEPVHRYGP----NSFKLHrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwdeildefrGSELQN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 71 GNAPLADAREDTRMMFQDARLLPwKKVLDNVALGLTgdwQPAARRALEEV-------GLADRANDwpaALSGGQKQRVAL 143
Cdd:cd03236 78 YFTKLLEGDVKVIVKPQYVDLIP-KAVKGKVGELLK---KKDERGKLDELvdqlelrHVLDRNID---QLSGGELQRVAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 144 ARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVS 194
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLA 200
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-211 |
5.41e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTI-LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-ADAREDTRMMFQDA 89
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 90 --------RLLPWKKVLDNVALGltGDWqpaarraLEEVGLAD--RANDWPAA---LSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK10522 403 ftdfhlfdQLLGPEGKPANPALV--EKW-------LERLKMAHklELEDGRISnlkLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 157 DEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDvSESVAMAERVLLIEDGKI 211
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-191 |
6.97e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGEL----RAGNAPLADAREDTRMMFQDARLLPWKK 96
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 97 VLDNVALGLTGDWQPAARRALEEVGLADRANDWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrlemQEMI 175
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS----LLTI 166
|
170
....*....|....*....
gi 506220968 176 VSLWREH---GFTVLLVTH 191
Cdd:PRK13540 167 ITKIQEHrakGGAVLLTSH 185
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-247 |
1.16e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.46 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 1 MTTSRLNQGTPLLLE--GVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLlRLLAGLETPDGGE----------- 67
Cdd:NF000106 1 MTRKTISNGARNAVEvrGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*twcan 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 68 -------------LRAGNAPLADAREDTRMMfqdARLLPWKKvldnvalgltGDWQPAARRALEEVGLADRANDWPAALS 134
Cdd:NF000106 80 rralrrtig*hrpVR*GRRESFSGRENLYMI---GR*LDLSR----------KDARARADELLERFSLTEAAGRAAAKYS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 135 GGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKIGLD 214
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
250 260 270
....*....|....*....|....*....|...
gi 506220968 215 MAVElphprhhgtprlaELEARVLNRVMRKAPA 247
Cdd:NF000106 226 GKVD-------------ELKTKVGGRTLQIRPA 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-202 |
1.50e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLaDARE-DTRM----MFQ-- 87
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDiATRRrvgyMSQaf 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 --------------DARL--LPwkkvldnvalglTGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRP 151
Cdd:NF033858 349 slygeltvrqnlelHARLfhLP------------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 152 GLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSEsvamAER 202
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNE----AER 463
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-240 |
1.58e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 37 GQFVAVVGRSGGGKS----TLLRLL---AGLETPDGGELRAGNAPLADARE------------DTRMMFQD--ARLLPWK 95
Cdd:PRK10261 42 GETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRQVIELSEqsaaqmrhvrgaDMAMIFQEpmTSLNPVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 KVLDNVA------LGLTGDWQPA-ARRALEEVGLADRA---NDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK10261 122 TVGEQIAesirlhQGASREEAMVeAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 166 LTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKIGLDMAVE--LPHPRHHGT-------PRLAELEAR 236
Cdd:PRK10261 202 TIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEqiFHAPQHPYTrallaavPQLGAMKGL 281
|
....
gi 506220968 237 VLNR 240
Cdd:PRK10261 282 DYPR 285
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-211 |
1.61e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLeTPDGGELRAGNAPLAD--AREDTR---MMFQDARLLPWKKVLDNV 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwsAAELARhraYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 102 ALGLTGDWQPAARRAL-----EEVGLADRANDWPAALSGGQKQRVALARAL------IHRPG-LLLLDEPLGALD----- 164
Cdd:COG4138 91 ALHQPAGASSEAVEQLlaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINPEGqLLLLDEPMNSLDvaqqa 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 165 ALTRLemqemiVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG4138 171 ALDRL------LRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-233 |
1.61e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.90 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQF-----VAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLA----DAREDTRMMFQDarLLpwKKV 97
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD--LL--SSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 98 LDNvaLGLTGDWQPAARRALEEVGLADR-ANDwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIV 176
Cdd:cd03237 86 TKD--FYTHPYFKTEIAKPLQIEQILDReVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 177 SLWREHGFTVLLVTHDVSESVAMAERVLLIeDGKIGLDMAVELPHPRHHGTPR-LAEL 233
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVANPPQSLRSGMNRfLKNL 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-209 |
1.93e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGN------APLADAREDT 82
Cdd:PRK09700 3 TPYIsMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RMMFQDARLLPWKKVLDNVALG------LTG----DWQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGrhltkkVCGvniiDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506220968 150 RPGLLLLDEPlgaLDALTRLEMQE--MIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDG 209
Cdd:PRK09700 163 DAKVIIMDEP---TSSLTNKEVDYlfLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-211 |
2.09e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 21 YGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR---------------------------AGNA 73
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarlqqdpprnvegtvydfvaEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 74 PLADAREDTRMMFQDARLLPWKKVLDNVA-----LGLTGDWQPAAR--RALEEVGLAdrANDWPAALSGGQKQRVALARA 146
Cdd:PRK11147 93 EQAEYLKRYHDISHLVETDPSEKNLNELAklqeqLDHHNLWQLENRinEVLAQLGLD--PDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 147 LIHRPGLLLLDEPLGALD--ALTRLEmqemivSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDieTIEWLE------GFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-211 |
2.35e-14 |
|
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: 72.29 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLR-LLAGLETPDGGELRAGNAPL----ADAREDT---RMMFQDARLLP 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKGSVAYvpqqAWIQNDSlreNILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 -WKKVLDNVALGLTGDWQPAARRAleEVGladranDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:TIGR00957 729 yYQQVLEACALLPDLEILPSGDRT--EIG------EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 506220968 173 EMIVS-LWREHGFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:TIGR00957 801 EHVIGpEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKI 839
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-210 |
3.59e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLeTPDGGELRAGNAPLAD--AREDTRM---MFQDARLLPWKK 96
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsAAELARHrayLSQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 97 VLDNVALGL-----TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARAL--IHRPG-----LLLLDEPLGALD 164
Cdd:PRK03695 86 VFQYLTLHQpdktrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWPDInpagqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 165 -----ALTRLemqemiVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK03695 166 vaqqaALDRL------LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-211 |
1.22e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 70.32 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLLLEGVTKRYGE--KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGgELRAGNapladaredtrMMF 86
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDG-----------VSW 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDARLLPWKK---VLDNVALGLTGDWQ----PAAR-------RALEEVGLADRANDWPA-----------ALSGGQKQRV 141
Cdd:TIGR01271 1283 NSVTLQTWRKafgVIPQKVFIFSGTFRknldPYEQwsdeeiwKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLM 1362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 142 ALARALIHRPGLLLLDEPLGALDALTRLEMQEMIvslwrEHGF---TVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL-----KQSFsncTVILSEHRV-EALLECQQFLVIEGSSV 1429
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-212 |
1.27e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.13 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADARED-----------TRMMFQDArl 91
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsrlavvsqTPFLFSDT-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 lpwkkVLDNVALGltgdwQPAARRA-LEEVG-LADRAND---WPAA-----------LSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK10789 405 -----VANNIALG-----RPDATQQeIEHVArLASVHDDilrLPQGydtevgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 156 LDEPLGALDAltRLEMQEMI-VSLWREhGFTVLLVTHDVSeSVAMAERVLLIEDGKIG 212
Cdd:PRK10789 475 LDDALSAVDG--RTEHQILHnLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-191 |
1.42e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.66 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 5 RLNQGTPLL-LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGlETPDG--------GELRAGNAPL 75
Cdd:PRK10938 253 ALPANEPRIvLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 76 ADARED----TRMMFQDARLlpwKKVLDNVAL-------GL---TGDWQPA-ARRALEEVGLADRANDWP-AALSGGQkQ 139
Cdd:PRK10938 332 WDIKKHigyvSSSLHLDYRV---STSVRNVILsgffdsiGIyqaVSDRQQKlAQQWLDILGIDKRTADAPfHSLSWGQ-Q 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 140 RVAL-ARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTH 191
Cdd:PRK10938 408 RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-211 |
1.91e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLL-LEGVTKRYGektiLNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADAR--- 79
Cdd:COG1129 253 GEVVLeVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirspRDAIrag 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 80 -----EDtrmmfqdaR----LLPWKKVLDNVALGLTGDWQP-----------AARRALEEVGLadRANDWPAA---LSGG 136
Cdd:COG1129 329 iayvpED--------RkgegLVLDLSIRENITLASLDRLSRgglldrrreraLAEEYIKRLRI--KTPSPEQPvgnLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 137 QKQRVALARALIHRPGLLLLDEP-----LGAldaltRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPtrgidVGA-----KAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-211 |
2.08e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALD---LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDG----GELRAGNAPLADAREDTR---------MMF 86
Cdd:PRK11022 16 ESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERrnlvgaevaMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDA--RLLPWKKVLDNV--ALGLTGDWQPAARRA-----LEEVGLAD---RANDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK11022 96 QDPmtSLNPCYTVGFQImeAIKVHQGGNKKTRRQraidlLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-211 |
2.16e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.90 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 19 KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDG---GELRAGNAPLADAREDTRmmfqdarllpwK 95
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYP-----------G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 KVLDNVAlgltGDWQPA---ARRALEEVGLAdRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:cd03233 84 EIIYVSE----EDVHFPtltVRETLDFALRC-KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 506220968 173 EMIVSLWREHGFTVLLVTHDVS-ESVAMAERVLLIEDGKI 211
Cdd:cd03233 159 KCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQ 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-193 |
3.33e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGEKTILNAlDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADA-REDTRMMFQDARLLPWK 95
Cdd:PRK15056 14 VTWRNGHTALRDA-SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlQKNLVAYVPQSEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 96 ---KVLDNVALGLTGD--W--QPAAR------RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK15056 93 fpvLVEDVVMMGRYGHmgWlrRAKKRdrqivtAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|....
gi 506220968 163 LDALTrlemQEMIVSLWRE---HGFTVLLVTHDV 193
Cdd:PRK15056 173 VDVKT----EARIISLLRElrdEGKTMLVSTHNL 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-193 |
3.72e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 18 TKRYGEktilnaLDLHVPAGQF-----VAVVGRSGGGKSTLLRLLAGLETPDGGE----LRAGNAP--LADAREDTRMMF 86
Cdd:PRK13409 347 TKKLGD------FSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpeLKISYKPqyIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 qdarllpwkkvLDNVALGLTGDW---QPAARRALEEVgLADRANDwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:PRK13409 421 -----------LRSITDDLGSSYyksEIIKPLQLERL-LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190
....*....|....*....|....*....|
gi 506220968 164 DALTRLEMQEMIVSLWREHGFTVLLVTHDV 193
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-211 |
4.09e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 24 KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLET----PDG----GELRAGNAPLA--DAREDTRM---MFQDAR 90
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaPRGarvtGDVTLNGEPLAaiDAPRLARLravLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LLPWKKVLDNVALGLTgdwqPAARRA----LEEVGLADRANDWPAA----------LSGGQKQRVALARAL--------- 147
Cdd:PRK13547 94 PAFAFSAREIVLLGRY----PHARRAgaltHRDGEIAWQALALAGAtalvgrdvttLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506220968 148 IHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-209 |
5.46e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.19 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 26 ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRagnapladarEDTRMMF--QDARLLPwKKVLDNVAL 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----------HSGRISFssQFSWIMP-GTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 104 GLTGD---WQPAARRA-LEE--VGLADRAN----DWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQE 173
Cdd:cd03291 121 GVSYDeyrYKSVVKACqLEEdiTKFPEKDNtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170 180 190
....*....|....*....|....*....|....*.
gi 506220968 174 MIVSLWREHGfTVLLVTHDVsESVAMAERVLLIEDG 209
Cdd:cd03291 201 SCVCKLMANK-TRILVTSKM-EHLKKADKILILHEG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-211 |
6.51e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGletpdggELragnAPLADAREDTRMMFQDARLLPW---KKVLD 99
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------EL----SHAETSSVVIRGSVAYVPQVSWifnATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 100 NVALGltGDWQPAAR-RALEEVGLADRANDWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PLN03232 698 NILFG--SDFESERYwRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506220968 168 rleMQEMIVSLWRE--HGFTVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:PLN03232 776 ---AHQVFDSCMKDelKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-209 |
8.44e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.01 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 26 ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRagnapladarEDTRMMF--QDARLLPwKKVLDNVAL 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----------HSGRISFspQTSWIMP-GTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 104 GLTGD---WQPAARRALEEVGLADRAN-------DWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQE 173
Cdd:TIGR01271 510 GLSYDeyrYTSVIKACQLEEDIALFPEkdktvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
170 180 190
....*....|....*....|....*....|....*.
gi 506220968 174 MIVSLWREHGfTVLLVTHDVsESVAMAERVLLIEDG 209
Cdd:TIGR01271 590 SCLCKLMSNK-TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-211 |
9.34e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 38 QFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG----NAPLADAREDTRMMFQDARLLPWKKVLDNVAL--GLTG-DWQ 110
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgkdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFyaQLKGrSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 111 PAA---RRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIvsLWREHGFTVL 187
Cdd:TIGR01257 1037 EAQlemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTII 1114
|
170 180
....*....|....*....|....
gi 506220968 188 LVTHDVSESVAMAERVLLIEDGKI 211
Cdd:TIGR01257 1115 MSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-210 |
1.28e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 12 LLLEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAreDTR-------- 83
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STTaalaagva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 MMFQDARLLPWKKVLDNVALGL---------TGDWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQlphkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-209 |
1.69e-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: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 7 NQGTPLLLEGVTKRYGEKT--ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAREdtr 83
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvAGKSILTNISD--- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 84 mMFQDARLLPWKKVLDNVALG---------LTG----DWQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHR 150
Cdd:TIGR01257 2010 -VHQNMGYCPQFDAIDDLLTGrehlylyarLRGvpaeEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 151 PGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDG 209
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-219 |
1.71e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.09 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPDGGELRAGNAPLADAREDTR------MMFQD----- 88
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaragifLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 89 ----ARLLpwKKVLDNVALGL--TGDWQPAARRALEEVGL----ADRA-NDwpaALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:COG0396 91 gvsvSNFL--RTALNARRGEElsAREFLKLLKEKMKELGLdedfLDRYvNE---GFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220968 158 EPLGALD--ALTRLemQEMIVSLwREHGFTVLLVTH-----DVSEsvamAERVLLIEDGKI----GLDMAVEL 219
Cdd:COG0396 166 ETDSGLDidALRIV--AEGVNKL-RSPDRGILIITHyqrilDYIK----PDFVHVLVDGRIvksgGKELALEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-193 |
1.94e-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: 66.35 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 2 TTSRLNQGTPLLLE--GVTKRYGEktilnaLDLHVPAGQF-----VAVVGRSGGGKSTLLRLLAGLETPDGGELragNAP 74
Cdd:COG1245 330 HAPRREKEEETLVEypDLTKSYGG------FSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 75 L----------ADAREDTRMMFQDArllpwkkvldnVALGLTGDW---QPAARRALEEvgLADR-ANDwpaaLSGGQKQR 140
Cdd:COG1245 401 LkisykpqyisPDYDGTVEEFLRSA-----------NTDDFGSSYyktEIIKPLGLEK--LLDKnVKD----LSGGELQR 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 141 VALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDV 193
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-212 |
3.68e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 10 TPLL-LEGVTKRY-GEKTILNAlDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR------AGNAPLADARED 81
Cdd:PRK10762 2 QALLqLKGIDKAFpGVKALSGA-ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 82 TRMMFQDARLLPWKKVLDNVALG--LTG-----DWQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIHRP 151
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGreFVNrfgriDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 152 GLLLLDEPlgaLDALTRLEMQEM---IVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGK-IG 212
Cdd:PRK10762 161 KVIIMDEP---TDALTDTETESLfrvIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIA 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-212 |
5.52e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 30 LDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAREDTRM---------------MFQDARLlPW 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLarglvylpedrqssgLYLDAPL-AW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 KKVldNVALGLTGDW-QPAARRALEE-----VGLADRANDWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK15439 361 NVC--ALTHNRRGFWiKPARENAVLEryrraLNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506220968 168 RLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIG 212
Cdd:PRK15439 439 RNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-210 |
6.08e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 13 LLE--GVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLE---TPDG-----GELRAgnapLADAREDT 82
Cdd:NF040905 1 ILEmrGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphgSYEGeilfdGEVCR----FKDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 83 RM----MFQDARLLPWKKVLDNVALG---LTG---DWQPAARRA---LEEVGLADRANDWPAALSGGQKQRVALARALIH 149
Cdd:NF040905 77 ALgiviIHQELALIPYLSIAENIFLGnerAKRgviDWNETNRRArelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506220968 150 RPGLLLLDEPLGAL-----DALTRLemqemIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:NF040905 157 DVKLLILDEPTAALneedsAALLDL-----LLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-211 |
7.30e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRllAGLetpdgGELragnAPLADAREDTRMMFQDARLLPW---KKVL 98
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS--AML-----GEL----PPRSDASVVIRGTVAYVPQVSWifnATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 DNVALGLTGDwqpAAR--RALEEVGLADRANDWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PLN03130 697 DNILFGSPFD---PERyeRAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 166 ltRLEMQEMIVSLWRE-HGFTVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:PLN03130 774 --HVGRQVFDKCIKDElRGKTRVLVTNQL-HFLSQVDRIILVHEGMI 817
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-211 |
7.92e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 9 GTPLL-LEGVT-KRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLADAredTRMMF 86
Cdd:COG3845 254 GEVVLeVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL---SPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 87 QDAR------------LLPWKKVLDNVALGLTG----------DWQPAARRALEEV--------GLADRAndwpAALSGG 136
Cdd:COG3845 331 RRLGvayipedrlgrgLVPDMSVAENLILGRYRrppfsrggflDRKAIRAFAEELIeefdvrtpGPDTPA----RSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 137 QKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-211 |
1.26e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 24 KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG--------NAPLADAREDTRMMFQD----ARL 91
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAErsiayvpqQAWIMNATVRGNILFFDeedaARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 92 LPWKKVLdnvalgltgdwQPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRLE 170
Cdd:PTZ00243 753 ADAVRVS-----------QLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506220968 171 MQEMIvsLWREHGFTVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:PTZ00243 822 VEECF--LGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-211 |
1.70e-11 |
|
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: 62.56 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 17 VTKRYGE--KTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAG----NAPLADAREDTRMMFQDAR 90
Cdd:cd03289 8 LTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswnSVPLQKWRKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 LL--PWKKVLDNvalglTGDWQPAA-RRALEEVGLADRANDWPA-----------ALSGGQKQRVALARALIHRPGLLLL 156
Cdd:cd03289 88 IFsgTFRKNLDP-----YGKWSDEEiWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 157 DEPLGALDALTRLEMQEMIvslwrEHGF---TVLLVTHDVsESVAMAERVLLIEDGKI 211
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTL-----KQAFadcTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-211 |
2.67e-11 |
|
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: 63.43 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 20 RYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPLAD-AREDTRMMFQdarLLPWKKVL 98
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDLRFKIT---IIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 DNVALGLTGDwqPAARRALEEVGLA-------DRANDWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:TIGR00957 1372 FSGSLRMNLD--PFSQYSDEEVWWAlelahlkTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 161 GALDaltrLEMQEMIVSLWREH--GFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:TIGR00957 1450 AAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLN-TIMDYTRVIVLDKGEV 1497
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-203 |
4.31e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.85 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 29 ALD---LHVPAGQFVAVVGRSGGGKSTLLRLLAGLeTPDGGELRAGNAPLAD-------ARE-------DTRMMFQDAR- 90
Cdd:COG4170 22 AVDrvsLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADRFRWNGidllklsPRErrkiigrEIAMIFQEPSs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 -LLPWKKVLDNV-----ALGLTGDW----QPAARRALE---EVGLADRA---NDWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG4170 101 cLDPSAKIGDQLieaipSWTFKGKWwqrfKWRKKRAIEllhRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506220968 155 LLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVsESVA-MAERV 203
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDL-ESISqWADTI 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
133-211 |
8.22e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 8.22e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIvSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-202 |
9.27e-11 |
|
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: 58.54 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 37 GQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNApladaredtrmmfqdarllpwkkvldnvalgltgdwqPAARRA 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------------------------------EDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 117 LEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLW-----REHGFTVLLVTH 191
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkSEKNLTVILTTN 124
|
170
....*....|.
gi 506220968 192 DVSESVAMAER 202
Cdd:smart00382 125 DEKDLGPALLR 135
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-249 |
1.18e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 32 LHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADAREDTRMMFQDAR----LLPWKKVLDNVA 102
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirspRDAIRAGIMLCPEDRkaegIIPVHSVADNIN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 103 LG-----------LTGDWQPA-ARRALEEVGLADRANDWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:PRK11288 354 ISarrhhlragclINNRWEAEnADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 170 EMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKIgldmAVELPHprHHGTprlaelEARVLNRVMRKAPAPV 249
Cdd:PRK11288 434 EIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRI----AGELAR--EQAT------ERQALSLALPRTSAAV 500
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-211 |
1.20e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELragnapLADAREDTRMMFQDAR- 90
Cdd:PLN03232 1237 FEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI------MIDDCDVAKFGLTDLRr 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 91 ---LLPWKKVLDNVALGLTGD----------WQPAARRALEEV------GLADRANDWPAALSGGQKQRVALARALIHRP 151
Cdd:PLN03232 1311 vlsIIPQSPVLFSGTVRFNIDpfsehndadlWEALERAHIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 152 GLLLLDEPLGALDALTRLEMQEMIVSLWREhgFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLN-TIIDCDKILVLSSGQV 1447
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
15-207 |
2.16e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.97 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 15 EGVTKRYGEKTILNALDLhVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRagnapladaredtrmmfqdarllpW 94
Cdd:cd03222 4 PDCVKRYGVFFLLVELGV-VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE------------------------W 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 KkvldnvalGLTGDWQPAArraleevgladrandwpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEM 174
Cdd:cd03222 59 D--------GITPVYKPQY-----------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|...
gi 506220968 175 IVSLWREHGFTVLLVTHDVSESVAMAERVLLIE 207
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-223 |
5.47e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 8 QGTPLLLEGVTKRY--GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRA-----GNAPLADARE 80
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVngreiGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 81 DTRMMFQDARLLPwKKVLDNVALGLTGdwQPA-ARRALEEVGLADRAndwpAALSG---------------GQKQRVALA 144
Cdd:PTZ00243 1385 QFSMIPQDPVLFD-GTVRQNVDPFLEA--SSAeVWAALELVGLRERV----ASESEgidsrvleggsnysvGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 145 RALIHR-PGLLLLDEPLGALD-ALTRlEMQEMIVSLWREHgfTVLLVTHDVsESVAMAERVLLIEDGKIGldmavELPHP 222
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDpALDR-QIQATVMSAFSAY--TVITIAHRL-HTVAQYDKIIVMDHGAVA-----EMGSP 1528
|
.
gi 506220968 223 R 223
Cdd:PTZ00243 1529 R 1529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
110-215 |
6.70e-10 |
|
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: 58.68 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 110 QPAARRALEEVGLADRANDWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLL 188
Cdd:TIGR02633 380 LQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIV 458
|
90 100
....*....|....*....|....*..
gi 506220968 189 VTHDVSESVAMAERVLLIEDGKIGLDM 215
Cdd:TIGR02633 459 VSSELAEVLGLSDRVLVIGEGKLKGDF 485
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-204 |
1.11e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 55.83 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLR---LLAGLETPDGGELRAGNAPladaredtrmmfqdarllpwkkvl 98
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAG------------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 99 DNVAlgltgdwQPAARRALEEVGLadrandwpaalSGGQKQRVALARALIH----RPGLLLLDEPLGALDALTRLEMQEM 174
Cdd:cd03227 62 CIVA-------AVSAELIFTRLQL-----------SGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|
gi 506220968 175 IVSLwREHGFTVLLVTHDvSESVAMAERVL 204
Cdd:cd03227 124 ILEH-LVKGAQVIVITHL-PELAELADKLI 151
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-194 |
1.30e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.79 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLrlLAGLETPdgGELRAGNAPLADAREDTRMMFQDARLLpwkkvldNVALG-L 105
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYAS--GKARLISFLPKFSRNKLIFIDQLQFLI-------DVGLGyL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 106 TGDwQPAArraleevgladrandwpaALSGGQKQRVALARALIHRPG--LLLLDEPLGALDALTRLEMQEMIVSLwREHG 183
Cdd:cd03238 80 TLG-QKLS------------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLG 139
|
170
....*....|.
gi 506220968 184 FTVLLVTHDVS 194
Cdd:cd03238 140 NTVILIEHNLD 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-208 |
1.63e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.63e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506220968 132 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVSeSVAMAERVLLIED 208
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNN 1433
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
24-211 |
1.82e-09 |
|
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: 56.46 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 24 KTILNALDLHVPAGQFVAVVGRSGGGKSTL-LRLLAGLETPDGGELRAG----NAPLADAREDTRMMFQDARLL------ 92
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFDGKIVIDGidisKLPLHTLRSRLSIILQDPILFsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 93 ---PWKKVLDNVAlgltgdWQpaarrALEEVGLADRANDWPAAL-----------SGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03288 114 nldPECKCTDDRL------WE-----ALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506220968 159 PLGALDALTRLEMQEMIVSLWREHgfTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:cd03288 183 ATASIDMATENILQKVVMTAFADR--TVVTIAHRVS-TILDADLVLVLSRGIL 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-209 |
2.02e-09 |
|
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: 55.71 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPD--GGELRAGNAPLAD--AREDTRMMFQDArLLPWKKV 97
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKnfQRSTGYVEQQDV-HSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 98 ldnvalgltgdwqpaaRRALeevgladRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlEMQEMIVS 177
Cdd:cd03232 97 ----------------REAL-------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 506220968 178 LWR---EHGFTVLLVTHDVSESV-AMAERVLLIEDG 209
Cdd:cd03232 150 FLKklaDSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
131-211 |
4.19e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 131 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
.
gi 506220968 211 I 211
Cdd:PRK13549 483 L 483
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
37-203 |
5.22e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 37 GQFVAVVGRSGGGKSTLLRLLAGLeTPDGGELRAGNAPLAD-------AREDTR-------MMFQDAR--LLPWKKVLDN 100
Cdd:PRK15093 33 GEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDidllrlsPRERRKlvghnvsMIFQEPQscLDPSERVGRQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 101 VALGLTGD------WQP---AARRALE---EVGLADRAN---DWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK15093 112 LMQNIPGWtykgrwWQRfgwRKRRAIEllhRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEP 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 506220968 166 LTRLEMQEMIVSLWREHGFTVLLVTHDVSESVAMAERV 203
Cdd:PRK15093 192 TTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-207 |
8.86e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 20 RYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELR-AGNAPLADAREDTRMMFQ----------- 87
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfPGNWQLAWVNQETPALPQpaleyvidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 -----DARLLPWKKVLDNVALGL-------TGDWQPAARRA--LEEVGLADRANDWP-AALSGGQKQRVALARALIHRPG 152
Cdd:PRK10636 90 eyrqlEAQLHDANERNDGHAIATihgkldaIDAWTIRSRAAslLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506220968 153 LLLLDEPLGA--LDALTRLEMqemivslW-REHGFTVLLVTHDVSESVAMAERVLLIE 207
Cdd:PRK10636 170 LLLLDEPTNHldLDAVIWLEK-------WlKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-208 |
9.78e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 26 ILNALDLHvpAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAgnaplaDAREDTRMMFQDARLLPWKKVLDNVALGL 105
Cdd:PRK10938 20 QLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQS------QFSHITRLSFEQLQKLVSDEWQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 106 TGDWQPAARRA----LEEVGLADRANDWPAA-------------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK10938 92 SPGEDDTGRTTaeiiQDEVKDPARCEQLAQQfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 506220968 169 LEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIED 208
Cdd:PRK10938 172 QQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-210 |
5.05e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELRAGNAPL-----ADARED-TRMMFQ 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkssKEALENgISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 88 DARLLPWKKVLDNVALG---LTG---DWQPAAR---RALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGmfvDQDKMYRdtkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220968 159 PlgaLDALTRLEMQEM--IVSLWREHGFTVLLVTHDVSESVAMAERVLLIEDGK 210
Cdd:PRK10982 161 P---TSSLTEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-194 |
1.54e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506220968 131 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHGFTVLLVTHDVS 194
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-192 |
1.92e-07 |
|
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: 51.32 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 13 LLEGVTKRYGEktilNALDLH---VP-AGQFVAVVGRSGGGKSTLLRLLAGLETPD------------------GGELRA 70
Cdd:COG1245 75 LEEDPVHRYGE----NGFRLYglpVPkKGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfrGTELQD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 71 GNAPLADAREDTRMMFQDARLLPwkKVLD-NVALGLTG-DWQPAARRALEEVGLA---DRANDwpaALSGGQKQRVALAR 145
Cdd:COG1245 151 YFKKLANGEIKVAHKPQYVDLIP--KVFKgTVRELLEKvDERGKLDELAEKLGLEnilDRDIS---ELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506220968 146 ALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHD 192
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-192 |
2.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 13 LLEGVTKRYGEktilNALDLH---VP-AGQFVAVVGRSGGGKSTLLRLLAGLETPD------------------GGELRA 70
Cdd:PRK13409 75 LEEEPVHRYGV----NGFKLYglpIPkEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfrGTELQN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 71 GNAPLADAREDTRMMFQDARLLPwkKVLDnvalGLTGDWQPAA--RRALEEV-------GLADRANDwpaALSGGQKQRV 141
Cdd:PRK13409 151 YFKKLYNGEIKVVHKPQYVDLIP--KVFK----GKVRELLKKVdeRGKLDEVverlgleNILDRDIS---ELSGGELQRV 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506220968 142 ALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREHgfTVLLVTHD 192
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHD 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-211 |
2.65e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 40 VAVVGRSGGGKSTLLRLLAG-LETPDGGELRAGNAPLA-------DAREDTR----MMFQDARLLPWKKVLDNV-ALGLT 106
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRMAvfsqhhvDGLDLSSnpllYMMRCFPGVPEQKLRAHLgSFGVT 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 107 GDWqpaarrALEEVgladrandwpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRLEmqEMIVSLWREHGfTV 186
Cdd:PLN03073 618 GNL------ALQPM----------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVE--ALIQGLVLFQG-GV 677
|
170 180
....*....|....*....|....*...
gi 506220968 187 LLVTHD---VSESVamaERVLLIEDGKI 211
Cdd:PLN03073 678 LMVSHDehlISGSV---DELWVVSEGKV 702
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-211 |
3.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 26 ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELragnapLADAREDTRMMFQDAR----LLPWKKVLDNV 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI------LIDGCDISKFGLMDLRkvlgIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 102 ALGLTGD----------WQPAARRALEEV------GLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PLN03130 1328 TVRFNLDpfnehndadlWESLERAHLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506220968 166 LTRLEMQEMIvslwREH--GFTVLLVTHDVSeSVAMAERVLLIEDGKI 211
Cdd:PLN03130 1408 RTDALIQKTI----REEfkSCTMLIIAHRLN-TIIDCDRILVLDAGRV 1450
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
128-207 |
1.23e-06 |
|
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: 47.60 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 128 DWPAA-----LSGGQKQ------RVALARALIHRPGLLLLDEPLGALDAlTRLEMQ--EMIVSLWREHGFTVLLVTHDvS 194
Cdd:cd03240 106 NWPLLdmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE-ENIEESlaEIIEERKSQKNFQLIVITHD-E 183
|
90
....*....|...
gi 506220968 195 ESVAMAERVLLIE 207
Cdd:cd03240 184 ELVDAADHIYRVE 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
132-211 |
1.47e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 132 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-191 |
1.91e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 14 LEGVTKRYGEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAgLETPDG----------------GELRAGNAPLAD 77
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDGipkncqilhveqevvgDDTTALQCVLNT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 78 AREDTRMMFQDARLLPWKKVLDNVALG-------LTGDWQPAARRALEEV----GLAD------RANDWPAALS------ 134
Cdd:PLN03073 259 DIERTQLLEEEAQLVAQQRELEFETETgkgkganKDGVDKDAVSQRLEEIykrlELIDaytaeaRAASILAGLSftpemq 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506220968 135 --------GGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSlWREhgfTVLLVTH 191
Cdd:PLN03073 339 vkatktfsGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSH 399
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-211 |
2.25e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGELragnaplaDAREDTRMMFQDARLLPWKKVLDNVAL--- 103
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--------DIKGSAALIAISSGLNGQLTGIENIELkgl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 104 --GLTGDW-QPAARRALEEVGLADRANDWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD-ALTRLEMQEMivSLW 179
Cdd:PRK13545 112 mmGLTKEKiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDKM--NEF 189
|
170 180 190
....*....|....*....|....*....|..
gi 506220968 180 REHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
133-211 |
8.40e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 8.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-59 |
5.88e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 5.88e-05
10 20 30
....*....|....*....|....*....|....*...
gi 506220968 22 GEKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAG 59
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-191 |
9.84e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 23 EKTILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPDGGELRAGN------APLADAREDTRMMFQDARLLPW 94
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGkdllelSPEDRAGEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 95 --KKVLDNVALGLTGDWQpaARRALEEVGLAD------RANDWPAAL---------SGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK09580 93 vsNQFFLQTALNAVRSYR--GQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190
....*....|....*....|....*....|....
gi 506220968 158 EPLGALDaLTRLEMQEMIVSLWREHGFTVLLVTH 191
Cdd:PRK09580 171 ESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
27-192 |
3.86e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.68 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLR--LLAGLE------------------------------TPDGGELRAGNAP 74
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALArrlhlkkeqpgnhdrieglehidkvividqSPIGRTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 75 LADAREDTRMMFQD----ARLLPwkKVLD------NVA--LGLTGDW-------QPAARR---ALEEVGLADRANDWPAA 132
Cdd:cd03271 91 YTGVFDEIRELFCEvckgKRYNR--ETLEvrykgkSIAdvLDMTVEEaleffenIPKIARklqTLCDVGLGYIKLGQPAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 133 -LSGGQKQRVALARALIHR---PGLLLLDEPlgaldaLTRL---EMQEMIVSLWR--EHGFTVLLVTHD 192
Cdd:cd03271 169 tLSGGEAQRIKLAKELSKRstgKTLYILDEP------TTGLhfhDVKKLLEVLQRlvDKGNTVVVIEHN 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-209 |
4.28e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 131 AALSGGQKQRVALARaliHRPGLL-----LLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVTHDvSESVAMAERVLL 205
Cdd:PRK00635 475 ATLSGGEQERTALAK---HLGAELigityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADRIID 549
|
....
gi 506220968 206 IEDG 209
Cdd:PRK00635 550 IGPG 553
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
26-192 |
6.37e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.04 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 26 ILNALDLHVPAGQFVAVVGRSGGGKSTLLRLLAGLETPDGGE---LRAGNAPLA---------DAREDTRMMfqdARLlp 93
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDfigLRGDALPLGansfilpglTGEENARMM---ASL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 94 wkkvldnvaLGLTGDWQPAARRALEEVG--LADRANDWPAALsggqKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:PRK15177 77 ---------YGLDGDEFSHFCYQLTQLEqcYTDRVSEYSVTM----KTHLAFAINLLLPCRLYIADGKLYTGDNATQLRM 143
|
170 180
....*....|....*....|.
gi 506220968 172 QEMIVSLWREHGFTVLlvTHD 192
Cdd:PRK15177 144 QAALACQLQQKGLIVL--THN 162
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
110-193 |
7.15e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 110 QPAARRALE---EVGLadranDW-----PAA-LSGGQKQRVALARALIHRPG---LLLLDEP------------LGALDA 165
Cdd:COG0178 800 IPKIARKLQtlqDVGL-----GYiklgqPATtLSGGEAQRVKLASELSKRSTgktLYILDEPttglhfhdirklLEVLHR 874
|
90 100 110
....*....|....*....|....*....|
gi 506220968 166 LtrlemqemivslwREHGFTVLLVTH--DV 193
Cdd:COG0178 875 L-------------VDKGNTVVVIEHnlDV 891
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
30-54 |
8.82e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 8.82e-04
10 20
....*....|....*....|....*
gi 506220968 30 LDLHVPAGQFVAVVGRSGGGKSTLL 54
Cdd:PRK00349 628 VDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-164 |
9.24e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 43 VGRSGGGKSTLLRLLAGLETPDGGELRAG-NAPLADAREDtRMMFQDARllpwkkVLDNVALGLTGDWQPAARR----AL 117
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQD-QFAFEEFT------VLDTVIMGHTELWEVKQERdriyAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 118 EEVGLAD--RANDWPAA----------------LSG-----------------GQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK15064 106 PEMSEEDgmKVADLEVKfaemdgytaearagelLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
..
gi 506220968 163 LD 164
Cdd:PRK15064 186 LD 187
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
102-192 |
3.83e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 102 ALGLTGDWQPAARRALEE----------VGLA----DRandwPAA-LSGGQKQRVALARALihrpG------LLLLDEP- 159
Cdd:COG0178 444 NLELTEREAEIAERILKEirsrlgflvdVGLDyltlDR----SAGtLSGGEAQRIRLATQI----GsglvgvLYVLDEPs 515
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 506220968 160 ----------LgaLDALTRLemqemivslwREHGFTVLLVTHD 192
Cdd:COG0178 516 iglhqrdndrL--IETLKRL----------RDLGNTVIVVEHD 546
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
27-62 |
6.35e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|....*...
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTLLR--LLAGLET 62
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALAN 661
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
117-203 |
6.96e-03 |
|
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: 36.85 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 117 LEEVGLA----DRANdwpAALSGGQKQRVALARALIHR-PGLL-LLDEPLGALDALTRLEMQEMIVSLwREHGFTVLLVT 190
Cdd:cd03270 121 LVDVGLGyltlSRSA---PTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVE 196
|
90
....*....|...
gi 506220968 191 HDvSESVAMAERV 203
Cdd:cd03270 197 HD-EDTIRAADHV 208
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
27-53 |
7.67e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 7.67e-03
10 20
....*....|....*....|....*..
gi 506220968 27 LNALDLHVPAGQFVAVVGRSGGGKSTL 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
103-206 |
8.51e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220968 103 LGLTGDWQPAARRALEE----------VGLA----DRANDwpaALSGGQKQRVALAR----ALIhrpGLL-LLDEPLGAL 163
Cdd:TIGR00630 448 LTLTPEEKKIAEEVLKEirerlgflidVGLDylslSRAAG---TLSGGEAQRIRLATqigsGLT---GVLyVLDEPSIGL 521
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 506220968 164 DALTRLEMQEMIVSLwREHGFTVLLVTHDvSESVAMAERVLLI 206
Cdd:TIGR00630 522 HQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDI 562
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-211 |
8.75e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.08 E-value: 8.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506220968 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQEMIVSLWREhGFTVLLVTHDVSESVAMAERVLLIEDGKI 211
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| |
