|
Name |
Accession |
Description |
Interval |
E-value |
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-256 |
0e+00 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 508.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 1 MNTARLNQGTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD 80
Cdd:PRK11247 2 MNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 81 DTRMMFQDARLLPWKTVMDNVGLGLKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRVGSARLAELEAEVLDR 240
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPRPRRRGSARLAELEAEVLQR 241
|
250
....*....|....*.
gi 1880204416 241 VMKRGEAEIQRIKANA 256
Cdd:PRK11247 242 VMSRGESEPTRLRWAG 257
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-248 |
3.42e-111 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 320.50 E-value: 3.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRY----GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQ 87
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGLKGSW------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG1116 88 EPALLPWLTVLDNVALGLELRGvpkaerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDIPRPRRV---GSARLAELEAE 236
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVDLPRPRDRelrTSPEFAALRAE 247
|
250
....*....|..
gi 1880204416 237 VLDRVMKRGEAE 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 |
9.48e-97 |
|
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: 282.44 E-value: 9.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQ 87
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03293 81 QDALLPWLTVLDNVALGLelqgvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDI 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 |
6.05e-83 |
|
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: 247.05 E-value: 6.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI---QDDTRMMFQD 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLK------GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03259 81 YALFPHLTVAENIAFGLKlrgvpkAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-211 |
2.93e-77 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 237.30 E-value: 2.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI---QDDTRMMFQD 88
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLKGSW------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRGvpkaeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 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 |
1.52e-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: 214.36 E-value: 1.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD-------DTRM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNVGLGLkgswredarqalaavglenragewpaalSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 165 ALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-211 |
2.28e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 207.97 E-value: 2.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR- 83
Cdd:COG1136 2 SPLLeLRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --------MMFQDARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:COG1136 82 rlrrrhigFVFQFFNLLPELTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 150 RPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-211 |
2.50e-65 |
|
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: 202.85 E-value: 2.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQDAR 90
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpvnTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03300 83 LFPHLTVFENIAFGLrlkklpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-211 |
1.59e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 204.92 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQD 88
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRniaMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG3839 84 YALYPHMTVYENIAFPLklrkvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-211 |
2.80e-64 |
|
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: 199.64 E-value: 2.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---- 83
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 -----MMFQDARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:cd03255 81 rrhigFVFQSFNLLPDLTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 153 LLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-211 |
7.93e-63 |
|
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: 196.74 E-value: 7.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR--------MM 85
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrrrigML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGLK--GSWRED-----ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1127 88 FQGGALFDSLTVFENVAFPLRehTDLSEAeirelVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-248 |
1.57e-62 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 197.01 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQ 87
Cdd:COG4525 4 LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLrlrgvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDIPRPRRVG--------SARLA 231
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLELDFSRRFLAGedaraiksDPAFI 243
|
250
....*....|....*..
gi 1880204416 232 ELEAEVLDRVMKRGEAE 248
Cdd:COG4525 244 ALREELLDIIFAQEEAE 260
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-218 |
2.68e-62 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 195.36 E-value: 2.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDnTILNAlDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQD 88
Cdd:COG3840 2 LRLDDLTYRYGD-FPLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvsMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLKGSWREDARQ------ALAAVGLENRAGEWPAALSGGQKQRVALARALI-HRPgLLLLDEPLG 161
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQraqveqALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-211 |
4.81e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.12 E-value: 4.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRY-GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR--------M 84
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrrigV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLrvtgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-218 |
8.96e-62 |
|
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: 193.87 E-value: 8.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR--------MM 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlrrrmgML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGL-------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLrehtrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-239 |
3.65e-61 |
|
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: 192.30 E-value: 3.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQDARLLPWKTVMDNVGLGL- 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 106 -------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETL 178
Cdd:TIGR01184 81 rvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 179 WQTHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTVDIPRPRR----VGSARLAELEAEVLD 239
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVPFPRPRDrlevVEDPSYYDLRNEALY 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-211 |
3.87e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 196.14 E-value: 3.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD--DTRM--MFQ 87
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprERRVgfVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG1118 83 HYALFPHMTVAENIAFGLrvrppsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-211 |
4.99e-60 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 193.40 E-value: 4.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL---AGTTPLSTIQDDTRMMFQD 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFidgEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLK--GSWREDARQ----ALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKmlGVPKEERKQrvkeALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-255 |
1.88e-59 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 192.47 E-value: 1.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 1 MNTARLNQGTPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAG--TTPLS 76
Cdd:PRK09452 3 KLNKQPSSLSPLVeLRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImLDGqdITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 77 TIQDDTRMMFQDARLLPWKTVMDNVGLGLK------GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:PRK09452 83 AENRHVNTVFQSYALFPHMTVFENVAFGLRmqktpaAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTvdiPR-----PRRV 225
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT---PReiyeePKNL 239
|
250 260 270
....*....|....*....|....*....|....
gi 1880204416 226 GSARLAE----LEAEVLDRVmkrgeaEIQRIKAN 255
Cdd:PRK09452 240 FVARFIGeiniFDATVIERL------DEQRVRAN 267
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-211 |
8.70e-59 |
|
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: 185.54 E-value: 8.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG---TTPLSTIQDDTRMMFQD 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLK------GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKlrkvpkDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
12-211 |
9.24e-59 |
|
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: 190.25 E-value: 9.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG---TTPLSTIQDDTRMMFQD 88
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGgrdITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLKGSW------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGmgraevAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-211 |
3.45e-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: 184.81 E-value: 3.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-------MMF 86
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrrkvgMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPWKTVMDNVGLG----LKGSW---REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1126 84 QQFNLFPHLTVLENVTLApikvKKMSKaeaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 160 LGALD-ALTRiEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1126 164 TSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-211 |
4.89e-58 |
|
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: 183.50 E-value: 4.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-------AGTTPLSTIQDDTRMMF 86
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltDDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPWKTVMDNVGLGL---KGSWREDA----RQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPikvKGMSKAEAeeraLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-218 |
1.11e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.34 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR----MMFQDA 89
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrrigYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVGL--GLKG----SWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG1131 83 ALYPDLTVRENLRFfaRLYGlprkEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 164 DALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG1131 163 DPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-211 |
1.57e-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: 183.02 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---- 83
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 -----MMFQDARLLPWKTVMDNVGLGL----KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG4181 89 arhvgFVFQSFQLLPTLTALENVMLPLelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 155 LLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRL 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
14-233 |
3.62e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.25 E-value: 3.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRY-GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST--------IQDDTRM 84
Cdd:COG3638 5 LRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgralrrLRRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNV---GLGLKGSWR-----------EDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:COG3638 85 IFQQFNLVPRLSVLTNVlagRLGRTSTWRsllglfppedrERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 151 PGLLLLDEPLGALD-ALTRIEMQDLIEtLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTvdiprPRRVGSAR 229
Cdd:COG3638 165 PKLILADEPVASLDpKTARQVMDLLRR-IAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGP-----PAELTDAV 238
|
....
gi 1880204416 230 LAEL 233
Cdd:COG3638 239 LREI 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-218 |
4.60e-55 |
|
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: 177.30 E-value: 4.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYG----DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD-----DTRM 84
Cdd:COG1124 4 VRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafrrRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDAR--LLPWKTVMDNVGLGLK----GSWREDARQALAAVGLENR-AGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:COG1124 84 VFQDPYasLHPRHTVDRILAEPLRihglPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 158 EPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG1124 164 EPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-211 |
3.48e-54 |
|
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: 174.44 E-value: 3.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLStiQDDTR-------MM 85
Cdd:COG1122 3 LENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRelrrkvgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDAR---LLPwkTVMDNVGLGLK--GSWREDAR----QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:COG1122 81 FQNPDdqlFAP--TVEEDVAFGPEnlGLPREEIRerveEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-211 |
5.27e-54 |
|
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: 181.64 E-value: 5.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 8 QGTPLL-LNGVTKRY-----GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD 81
Cdd:COG1123 256 AAEPLLeVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 TR--------MMFQD--ARLLPWKTVMDNVGLGL-------KGSWREDARQALAAVGLENRAGEW-PAALSGGQKQRVAL 143
Cdd:COG1123 336 SLrelrrrvqMVFQDpySSLNPRMTVGDIIAEPLrlhgllsRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 144 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-211 |
9.19e-54 |
|
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: 173.68 E-value: 9.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG---TTPLSTIQDDTRMMFQDARLL 92
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedATDVPVQERNVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PWKTVMDNVGLGL----------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03296 87 RHMTVFDNVAFGLrvkprserppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-248 |
1.46e-53 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 173.73 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQDARL 91
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK11248 82 LPWRNVQDNVAFGLqlagveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 166 LTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIE--EGKIGLDLTVDIPRPRRVGSA--------RLAELEA 235
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLNFARRFVAGESsrsiksdpQFIAMRE 241
|
250
....*....|...
gi 1880204416 236 EVLDRVMKRGEAE 248
Cdd:PRK11248 242 YVLSRVFEQREAF 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-223 |
2.32e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 172.58 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-------AGTTPLSTIQDDTRMMFQDA 89
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvnDPKVDERLIRQEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVGLG---LKGSWREDARQA----LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK09493 87 YLFPHLTALENVMFGplrVRGASKEEAEKQarelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 163 LDALTRIE----MQDLIEtlwqtHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD-----LTVDIPRPR 223
Cdd:PRK09493 167 LDPELRHEvlkvMQDLAE-----EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDgdpqvLIKNPPSQR 231
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-211 |
4.90e-53 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 171.91 E-value: 4.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGttplstiQDDTRM------ 84
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIrLNG-------QDATRVhardrk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 ---MFQDARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:TIGR00968 74 igfVFQHYALFKHLTVRDNIAFGLeirkhpKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-211 |
5.16e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 172.58 E-value: 5.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQDAR 90
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRkvgFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGLK----------GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTvlprrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-211 |
9.72e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.73 E-value: 9.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLStiQDDTRM-----MFQD 88
Cdd:COG1121 9 LENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--RARRRIgyvpqRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPwKTVMDNVGLGLKGSW----------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1121 87 DWDFP-ITVRDVVLMGRYGRRglfrrpsradREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1121 166 PFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-211 |
1.01e-51 |
|
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: 168.14 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR------ 83
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkarrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --MMFQDARLLPWKTVMDNVGLGLK-GSWREDARQA-----LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03258 84 igMIFQHFNLLSSRTVFENVALPLEiAGVPKAEIEErvlelLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-210 |
1.16e-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: 167.26 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-----MMF 86
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrkvgLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARllpWKTVMDNVG---------LGLKGSW-REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:cd03225 82 QNPD---DQFFGPTVEeevafglenLGLPEEEiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-211 |
1.38e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ-DDTRMM----F 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQvayvP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPwKTVMDNV----GLGLKGSWREDARQALAAVGLENRAGEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG4619 81 QEPALWG-GTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-241 |
1.62e-51 |
|
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: 168.13 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL--------AGTTPLSTIQDDTRM 84
Cdd:cd03256 3 VENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinkLKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNVGLGLKGSW--------------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGRRstwrslfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 151 PGLLLLDEPLGALD-ALTRIEMqDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDltvdiprprrvGSAr 229
Cdd:cd03256 163 PKLILADEPVASLDpASSRQVM-DLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD-----------GPP- 229
|
250
....*....|..
gi 1880204416 230 lAELEAEVLDRV 241
Cdd:cd03256 230 -AELTDEVLDEI 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-211 |
3.20e-51 |
|
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: 164.88 E-value: 3.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM----MFQDA 89
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrigyLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVglglkgswredarqalaavglenragewpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:cd03230 83 SLYENLTVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03230 133 EFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-211 |
3.55e-51 |
|
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: 170.67 E-value: 3.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTiLNAlDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLstiQDDTR------------M 84
Cdd:COG4148 7 FRLRRGGFT-LDV-DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL---QDSARgiflpphrrrigY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNVGLGLKGSWREDARQALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-211 |
5.46e-51 |
|
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: 167.14 E-value: 5.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-----MMFQD 88
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarriaYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLG------LKGSWRED----ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1120 84 PPAPFGLTVRELVALGryphlgLFGRPSAEdreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
1.50e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 168.33 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRY----GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD----DTR-- 83
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelrAARrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --MMFQDARLLPWKTVMDNVGLGLKGS-WREDARQA-----LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG1135 84 igMIFQHFNLLSSRTVAENVALPLEIAgVPKAEIRKrvaelLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-210 |
2.19e-50 |
|
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: 162.55 E-value: 2.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-----MMF 86
Cdd:cd03228 3 FKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniaYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPwKTVMDNVglglkgswredarqalaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03228 83 QDPFLFS-GTIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1880204416 167 TRIEMQDLIETLwqTHGFTVLLVTHDVSeAVAMADRVLLIEEGK 210
Cdd:cd03228 131 TEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-211 |
4.66e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 166.03 E-value: 4.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTI-LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDT--RMM---FQ 87
Cdd:COG1125 4 FENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIgyvIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGL--GLKGsW-----REDARQALAAVGLENR--AGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1125 84 QIGLFPHMTVAENIATvpRLLG-WdkeriRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-211 |
5.20e-50 |
|
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: 164.01 E-value: 5.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTiQDDTRM------MF 86
Cdd:cd03295 3 FENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVELrrkigyVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPWKTVMDNVGLGLKGS-W-----REDARQALAAVGLE--NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLkWpkekiRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
17-210 |
1.90e-49 |
|
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: 161.65 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD--------TRMMFQ 87
Cdd:TIGR02673 7 VSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlpllrrrIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR02673 87 DFRLLPDRTVYENVALPLevrgkkEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 162 ALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:TIGR02673 167 NLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-211 |
2.65e-49 |
|
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: 163.20 E-value: 2.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD---------DTRMMFQDARLLPWKTV 97
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelrrkKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 171
Cdd:cd03294 120 LENVAFGLevqgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1880204416 172 QDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-211 |
2.80e-49 |
|
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: 161.12 E-value: 2.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTIlnALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQDAR 90
Cdd:cd03298 3 LDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpvsMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGLKGSWREDARQ------ALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKLTAEDrqaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-211 |
1.94e-48 |
|
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: 159.59 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRY----GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR------ 83
Cdd:cd03257 4 VKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --MMFQDAR--LLPWKTVMDNVG------LGLKGSWREDARQALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:cd03257 84 iqMVFQDPMssLNPRMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-211 |
2.25e-48 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 159.00 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 19 KRYGDNTILNALDLhipAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLstiqDDTR-------------MM 85
Cdd:cd03297 8 KRLPDFTLKIDFDL---NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL----FDSRkkinlppqqrkigLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGLKG-SWRED---ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRkRNREDrisVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-241 |
2.28e-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: 160.02 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR----MMFQDA 89
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqigVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVGL--GLKGSWREDARQALAAV----GLEN----RAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG4555 84 GLYDRLTVRENIRYfaELYGLFDEELKKRIEELiellGLEEfldrRVGE----LSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 160 LGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRVgsarLAELEAEVLD 239
Cdd:COG4555 160 TNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG----EENLEDAFVA 234
|
..
gi 1880204416 240 RV 241
Cdd:COG4555 235 LI 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-221 |
6.45e-48 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 161.12 E-value: 6.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 42 VVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQDARLLPWKTVMDNVGLGLK--GSWRED---- 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhinMVFQSYALFPHMTVEENVAFGLKmrKVPRAEikpr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 113 ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHD 192
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....*....
gi 1880204416 193 VSEAVAMADRVLLIEEGKIgldLTVDIPR 221
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKI---AQIGTPE 186
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-211 |
1.06e-47 |
|
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: 167.70 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI-QDDTRMMF---- 86
Cdd:COG2274 476 LENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdPASLRRQIgvvl 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPwKTVMDNVGLGLKGSWREDARQALAAVGLEN-----------RAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG2274 556 QDVFLFS-GTIRENITLGDPDATDEEIIEAARLAGLHDfiealpmgydtVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLwqTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 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 ... |
17-211 |
3.98e-47 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 156.03 E-value: 3.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTI-LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR--------MMFQ 87
Cdd:cd03292 6 VTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylrrkigVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGLKGS------WREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTgvppreIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-250 |
4.07e-47 |
|
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: 163.54 E-value: 4.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRY--GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN---SGDILAGTTPLSTIQDDTR 83
Cdd:COG1123 2 TPLLeVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 -----MMFQD--ARLLPWkTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:COG1123 82 grrigMVFQDpmTQLNPV-TVGDQIAEALenlglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD--IPRPRRVGSA 228
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEeiLAAPQALAAV 240
|
250 260
....*....|....*....|..
gi 1880204416 229 RLAELEAEVLDRVMKRGEAEIQ 250
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPLLE 262
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-211 |
9.68e-47 |
|
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: 155.42 E-value: 9.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----EAPNSGDILAGTTPLSTIQDD-----TR 83
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --MMFQDARLLPwKTVMDNVGLGLK--GSWREDARQALAAVGLEnRAGEW--------PAALSGGQKQRVALARALIHRP 151
Cdd:cd03260 83 vgMVFQKPNPFP-GSIYDNVAYGLRlhGIKLKEELDERVEEALR-KAALWdevkdrlhALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 152 GLLLLDEPLGALDALTRIEMQDLIETLWQTHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-211 |
3.11e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 157.88 E-value: 3.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQDAR 90
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERgvgMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGLK--GSWREDARQALAAVG--------LENRagewPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK11000 86 LYPHLSVAENMSFGLKlaGAKKEEINQRVNQVAevlqlahlLDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-211 |
3.40e-46 |
|
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: 152.20 E-value: 3.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIqddtrmmfqdarllp 93
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 wktvmdnvglglkgSWREDAR------QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:cd03214 67 --------------SPKELARkiayvpQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1880204416 168 RIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-211 |
4.55e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 161.46 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 3 TARLNQGTPLLLNGVTKRYGDN-TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD 81
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 TRM-----MFQDARLLPWkTVMDNVGLGLKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALAR 145
Cdd:COG4988 408 SWRrqiawVPQNPYLFAG-TIRENLRLGRPDASDEELEAALEAAgldefvaalpdGLDTPLGEGGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 146 ALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-241 |
8.21e-46 |
|
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: 153.22 E-value: 8.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL--------AGTTPLSTIQDDT 82
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditkLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 RMMFQDARLLPWKTVMDNV---GLGLKGSWR-----------EDARQALAAVGLENRAGEWPAALSGGQKQRVALARALI 148
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWRsllgrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 149 HRPGLLLLDEPLGALD-ALTRIEMqDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDltvdiprprrvGS 227
Cdd:TIGR02315 162 QQPDLILADEPIASLDpKTSKQVM-DYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD-----------GA 229
|
250
....*....|....
gi 1880204416 228 ArlAELEAEVLDRV 241
Cdd:TIGR02315 230 P--SELDDEVLRHI 241
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
39-211 |
8.56e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 157.19 E-value: 8.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 39 FVaVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDT----R-----MMFQDARLLPWKTVMDNVGLGL---- 105
Cdd:COG4175 56 FV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelRrkkmsMVFQHFALLPHRTVLENVAFGLeiqg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 106 --KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD-LIEtLWQTH 182
Cdd:COG4175 135 vpKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDeLLE-LQAKL 213
|
170 180
....*....|....*....|....*....
gi 1880204416 183 GFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4175 214 KKTIVFITHDLDEALRLGDRIAIMKDGRI 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-210 |
1.02e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 156.92 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI---QDDTRMM 85
Cdd:PRK11607 17 TPLLeIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGLK------GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKqdklpkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 160 LGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
14-206 |
1.91e-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: 151.23 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTT--PLSTIQ------DDTRM 84
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVyLNGQEtpPLNSKKaskfrrEKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNVGLGLKGSW------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKlskkekREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 159 PLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDvSEAVAMADRVLLI 206
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-210 |
3.23e-45 |
|
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: 148.93 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQddtrmmfqdarllp 93
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 wktvmdnvglglkgswREDARQALAAVGlenragewpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD 173
Cdd:cd00267 68 ----------------LEELRRRIGYVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 1880204416 174 LIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:cd00267 122 LLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-214 |
4.04e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 151.27 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 31 DLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAG----TTPLStiQDDTRMMFQDARLLPWKTVMDNVGLG- 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGqdhtTTPPS--RRPVSMLFQENNLFSHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 105 -----LKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLW 179
Cdd:PRK10771 97 npglkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1880204416 180 QTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
12-211 |
5.22e-45 |
|
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: 150.40 E-value: 5.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVtkRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL---AGTTPLSTIQDDTRMMFQD 88
Cdd:TIGR01277 1 LALDKV--RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKvndQSHTGLAPYQRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLKGSWREDARQ------ALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLHPGLKLNAEQqekvvdAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-211 |
7.16e-45 |
|
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: 151.81 E-value: 7.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTtpLSTIQDDTR-------- 83
Cdd:TIGR04520 3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 MMFQD-------ArllpwkTVMDNVGLGL--KGSWREDARQ----ALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:TIGR04520 81 MVFQNpdnqfvgA------TVEDDVAFGLenLGVPREEMRKrvdeALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVaMADRVLLIEEGKI 211
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-211 |
1.05e-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: 149.81 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDN----TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-------- 83
Cdd:TIGR02211 6 NLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkkl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 -MMFQDARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:TIGR02211 86 gFIYQFHHLLPDFTALENVAMPLligkksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-211 |
2.51e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.39 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI--------LAGTTPLSTIQD---DT 82
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPSDKAIRElrrNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 RMMFQDARLLPWKTVMDNV------GLGL-KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLieapcrVLGLsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
3.36e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 149.01 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAG-----TTPLST-----IQDDT 82
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLnIAGhqfdfSQKPSEkairlLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 RMMFQDARLLPWKTVMDNVG------LGL-KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLIeapckvLGLsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-211 |
6.65e-44 |
|
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: 147.29 E-value: 6.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQdARLLP 93
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQ-RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WK---TVMDNVGLGL----------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03235 81 RDfpiSVRDVVLMGLyghkglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03235 161 AGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-211 |
1.26e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.32 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI-QDDTR----MMFQ 87
Cdd:COG1132 342 FENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtLESLRrqigVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPwKTVMDNVGLGLKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:COG1132 422 DTFLFS-GTIRENIRYGRPDATDEEVEEAAKAAqahefiealpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLwqTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG1132 501 DEATSALDTETEALIQEALERL--MKGRTTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-211 |
7.76e-43 |
|
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: 145.56 E-value: 7.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNaLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL---AGTTPLSTIQDDTRMMFQD 88
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLKGSWR---EDARQAL---AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVdkkEIERKVLeiaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-211 |
1.74e-42 |
|
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: 144.01 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL--------AGTTPLSTIQDDTRMMFQDARLLPWKTV 97
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvlgqelhgASKKQLVQLRRRIGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MDNVGLGL----KGSW---REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 170
Cdd:TIGR02982 100 RQNVQMALelqpNLSYqeaRERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1880204416 171 MQDLIETLWQTHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-211 |
1.79e-42 |
|
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: 151.84 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 2 NTARLNQGTPLLLNGVTKRY--GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ 79
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDTR-----MMFQDARLLPwKTVMDNVGLGLKGSWREDARQALAAVGLEN-----------RAGEWPAALSGGQKQRVAL 143
Cdd:COG4987 404 EDDLrrriaVVPQRPHLFD-TTLRENLRLARPDATDEELWAALERVGLGDwlaalpdgldtWLGEGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 144 ARALIHRPGLLLLDEPLGALDALTRiemQDLIETLWQ-THGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATE---QALLADLLEaLAGRTVLLITHR-LAGLERMDRILVLEDGRI 547
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-211 |
2.16e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 147.25 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRY--GDNTI--LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD----TR-- 83
Cdd:PRK11153 4 LKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkARrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --MMFQDARLLPWKTVMDNVGLGLK-GSWREDARQA-----LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK11153 84 igMIFQHFNLLSSRTVFDNVALPLElAGTPKAEIKArvtelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTH--DVSEAVamADRVLLIEEGKI 211
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKRI--CDRVAVIDAGRL 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-214 |
2.01e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.98 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTIL--NALD---LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTplsTIQDDTRMMFQD 88
Cdd:TIGR04521 3 LKNVSYIYQPGTPFekKALDdvsLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGR---DITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARllpwK----------------TVMDNVG-----LGL-KGSWREDARQALAAVGL-ENRAGEWPAALSGGQKQRVALAR 145
Cdd:TIGR04521 80 LR----KkvglvfqfpehqlfeeTVYKDIAfgpknLGLsEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 146 ALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
16-211 |
2.02e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.20 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG------TTPLSTIQDDTRMM---- 85
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGLIRQLrqhv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 ---FQDARLLPWKTVMDNVGLG---LKGSWREDA----RQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK11264 88 gfvFQNFNLFPHRTVLENIIEGpviVKGEPKEEAtaraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQTHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-208 |
3.66e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 140.31 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN---SGDILAGTTPLSTIQDDTR---MM 85
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRrigIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGLKGSWREDAR-----QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALPPTIGRAQRrarveQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAmADRVLLIEE 208
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-211 |
8.70e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 143.45 E-value: 8.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRY-GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---MMFQ 87
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRdiaMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGLK--GSWRE--DARQALAAVGLE-----NRAgewPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKirGMPKAeiEERVAEAARILElepllDRK---PRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-211 |
9.26e-41 |
|
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: 139.27 E-value: 9.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILA-GTTPLSTIQDDTRM--MFQDAR 90
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIgaLIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGLKGSWREDAR--QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRidEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1880204416 169 IEMQDLIeTLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03268 163 KELRELI-LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-211 |
1.80e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.54 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 7 NQGTPLLLNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS--TIQDDT 82
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeeTVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 R---MMFQ--DARLLPwKTVMDNVGLGLK--GSWRED----ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRP 151
Cdd:PRK13635 81 RqvgMVFQnpDNQFVG-ATVQDDVAFGLEniGVPREEmverVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 152 GLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-210 |
5.33e-40 |
|
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: 137.23 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR----MMFQ 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGL--GLKGSW--REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG4133 83 ADGLKPELTVRENLRFwaALYGLRadREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 164 DALTRIEMQDLIETlWQTHGFTVLLVTHDVSEAVamADRVLLIEEGK 210
Cdd:COG4133 163 DAAGVALLAELIAA-HLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-211 |
3.27e-39 |
|
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: 136.71 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 9 GTPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGttplstiQDDTRMM- 85
Cdd:COG0411 1 SDPLLeVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlFDG-------RDITGLPp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 -----------FQDARLLPWKTVMDNVGLGL----KGSW-----------------REDARQALAAVGLENRAGEWPAAL 133
Cdd:COG0411 74 hriarlgiartFQNPRLFPELTVLENVLVAAharlGRGLlaallrlprarreereaRERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 134 SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
11-211 |
4.15e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.47 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 11 PLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD--------DT 82
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpaDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 R----------MMFQDARLLPWKTVMDNVG------LGL-KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALAR 145
Cdd:COG4598 88 RqlqrirtrlgMVFQSFNLWSHMTVLENVIeapvhvLGRpKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 146 ALIHRPGLLLLDEPLGALDAltriE--------MQDLIEtlwqtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDP----ElvgevlkvMRDLAE-----EGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-211 |
5.77e-39 |
|
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: 138.71 E-value: 5.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 19 KRYGDNTIlnALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTT--------PLSTIQDDTRMMFQDA 89
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvLNGRTlfdsrkgiFLPPEKRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVGLGLKGSWREDARQALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISFERViellGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 166 LTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-211 |
7.02e-39 |
|
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: 134.80 E-value: 7.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGD-ILAGTTPLS---TIQDDTRMMFQDARL 91
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVReprEVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LPWKTVMDNVGL-----GLKGS-WREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:cd03265 85 DDELTGWENLYIharlyGVPGAeRRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 166 LTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-212 |
8.22e-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: 135.60 E-value: 8.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSG---DILAGTTPLSTIQD----- 80
Cdd:COG1119 1 DPLLeLRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGERRGGEDVWElrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 81 ---DTRMMfqdARLLPWKTVMDNVGLGLKGS---WRE-------DARQALAAVGLENRAGEWPAALSGGQKQRVALARAL 147
Cdd:COG1119 81 glvSPALQ---LRFPRDETVLDVVLSGFFDSiglYREptdeqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 148 IHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-217 |
9.14e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 134.94 E-value: 9.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLLL-NGVTKRYGDNTI----LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM 84
Cdd:PRK11629 3 KILLQcDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 M---------FQDARLLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK11629 83 ElrnqklgfiYQFHHLLPDFTALENVAMPLligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 150 RPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMaDRVLLIEEGKIGLDLTV 217
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-230 |
2.88e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 134.43 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI--------QDDTRMMFQ 87
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DA--RLLPWKTVMDNVG------LGLKGSWRED-ARQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK10419 97 DSisAVNPRKTVREIIReplrhlLSLDKAERLArASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 158 EPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI------GLDLTVDIPRPRRVGSARL 230
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetqpvGDKLTFSSPAGRVLQNAVL 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-211 |
3.13e-38 |
|
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: 133.72 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR------MM 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGL----KGSW------------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAqartGSGLllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 150 RPGLLLLDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-211 |
1.65e-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: 131.40 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR------MM 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGLKGSWREDARQALAAV-----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03224 161 EGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-211 |
3.14e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 131.43 E-value: 3.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 15 NGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-----MMFQDA 89
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrraVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RL-LPWkTVMDNVGLGL---KGSWREDAR---QALAAVGLENRAGEWPAALSGGQKQRVALARALI------HRPGLLLL 156
Cdd:PRK13548 86 SLsFPF-TVEEVVAMGRaphGLSRAEDDAlvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-209 |
4.39e-37 |
|
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: 132.87 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYG-DNTILNALD---LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN---SGDILAGTTPLSTIQDDTR--- 83
Cdd:COG0444 4 VRNLKVYFPtRRGVVKAVDgvsFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 ------MMFQD--ARLLPWKTVMDNVGLGL-------KGSWREDARQALAAVGL---ENRAGEWPAALSGGQKQRVALAR 145
Cdd:COG0444 84 rgreiqMIFQDpmTSLNPVMTVGDQIAEPLrihgglsKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 146 ALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVL------LIEEG 209
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAvmyagrIVEEG 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-211 |
6.31e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.39 E-value: 6.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT---ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST-----IQDDTRMM 85
Cdd:PRK13650 7 VKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQ--DARLLPwKTVMDNVGLGL--KGSWREDAR----QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK13650 87 FQnpDNQFVG-ATVEDDVAFGLenKGIPHEEMKervnEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 158 EPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 211
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-211 |
8.98e-37 |
|
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: 128.85 E-value: 8.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFvAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF----Q 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTV---MDNVGLgLKG--SWREDAR--QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03264 80 EFGVYPNFTVrefLDYIAW-LKGipSKEVKARvdEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
12-211 |
2.92e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.54 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNgVTKRYGDNTIlnALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM------- 84
Cdd:PRK11144 2 LELN-FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 --MFQDARLLPWKTVMDNVGLGLKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK11144 79 gyVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-211 |
3.04e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 134.42 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIlagttplsTIQDDTRMMF--QDARL 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLRIGYlpQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LPWKTVMDNVGLGLKGSWR--------------------------------------EDARQALAAVGLENRAGEWP-AA 132
Cdd:COG0488 73 DDDLTVLDTVLDGDAELRAleaeleeleaklaepdedlerlaelqeefealggweaeARAEEILSGLGFPEEDLDRPvSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIETLWQTHGFTVLLVTHDVS--EAVamADRVLLIEEGK 210
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDRYflDRV--ATRILELDRGK 226
|
.
gi 1880204416 211 I 211
Cdd:COG0488 227 L 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-211 |
6.23e-36 |
|
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: 127.01 E-value: 6.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLsTIQDDTRM--MFQDA 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIgyLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDN-VGLG-LKGSWREDARQA----LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:cd03269 80 GLYPKMKVIDQlVYLAqLKGLKKEEARRRidewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 164 DALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03269 160 DPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-211 |
1.20e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.54 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 15 NGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI--QDDTRM---MFQDA 89
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspWELARRravLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RL-LPWkTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARAL--IHR-----PGLLL 155
Cdd:COG4559 85 SLaFPF-TVEEVVALGRaphgssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEpvdggPRWLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-211 |
7.66e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.51 E-value: 7.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 25 TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR---------MMFQDARLLPWK 95
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvgFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 TVMDNVGLG--LKG----SWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:PRK10584 104 NALENVELPalLRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-211 |
2.04e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.46 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 32 LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD---------DTRMMFQDARLLPWKTVMDNVG 102
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevrrkKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 103 LGLK------GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 176
Cdd:PRK10070 129 FGMElaginaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*
gi 1880204416 177 TLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-159 |
2.70e-34 |
|
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: 120.83 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-----MMFQDARLLPWKTVMDNV 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeigYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 102 GLGL---------KGSWREDARQALAAVGLENR-AGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:pfam00005 81 RLGLllkglskreKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-211 |
2.93e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.93 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 7 NQGTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD----- 81
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 -----------TR--MMFQDARLLPWKTVMDNVG------LGL-KGSWREDARQALAAVGLENRA-GEWPAALSGGQKQR 140
Cdd:PRK10619 81 vadknqlrllrTRltMVFQHFNLWSHMTVLENVMeapiqvLGLsKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 141 VALARALIHRPGLLLLDEPLGALDA-----LTRIeMQDLIEtlwqtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPelvgeVLRI-MQQLAE-----EGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-211 |
3.50e-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: 121.17 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF--- 86
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 --QDARLLPwKTVMDNVglglkgswredarqalaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03246 81 lpQDDELFS-GSIAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLwQTHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-211 |
7.08e-34 |
|
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: 127.88 E-value: 7.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 19 KRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEaPNSGDILAGTTPLSTIQDDTR--------MMFQD-- 88
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALrplrrrmqVVFQDpf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLK-------GSWRED-ARQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLRvhgpglsAAERRArVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-212 |
7.18e-34 |
|
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: 121.21 E-value: 7.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST----------IQDDTRM 84
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerrksigyvMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDarllpwkTVMDNVGLGLKGSWR--EDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03226 84 LFTD-------SVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 163 LDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:cd03226 157 LDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-211 |
1.05e-33 |
|
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: 122.61 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRY---------GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI---- 78
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 79 ----QDDTRMMFQDA--RLLPWKTVMDNVGLGLKG--SWREDARQA-----LAAVGLENR-AGEWPAALSGGQKQRVALA 144
Cdd:TIGR02769 83 rrafRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHltSLDESEQKAriaelLDMVGLRSEdADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 145 RALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-211 |
1.18e-33 |
|
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: 121.57 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGD--NTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ-DDTRMMF---- 86
Cdd:cd03251 3 FKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPwKTVMDNVGLGLKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03251 83 QDVFLFN-DTVAENIAYGRPGATREEVEEAARAAnahefimelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQthGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKI 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-211 |
1.35e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 121.14 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRY-GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD--------DTRMMFQ 87
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNrevpflrrQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGL--KGSWREDARQ----ALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLiiAGASGDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 162 ALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
31-211 |
1.37e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 123.69 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 31 DLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR--------MMFQD--ARLLPWKTVMDN 100
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrrmqMVFQDpyASLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 VGLGL-------KGSWREDARQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltRIEMQ 172
Cdd:COG4608 118 IAEPLrihglasKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV--SIQAQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1880204416 173 --DLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4608 196 vlNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-206 |
2.36e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.65 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-AGTTPLSTIQDDTRMmfqdARLLPwKTVM 98
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRrAGGARVAYVPQRSEV----PDSLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVGLGL---KGSWREDAR-------QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:NF040873 76 DLVAMGRwarRGLWRRLTRddraavdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1880204416 169 IEMQDLIeTLWQTHGFTVLLVTHDVsEAVAMADRVLLI 206
Cdd:NF040873 156 ERIIALL-AEEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-216 |
6.71e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.58 E-value: 6.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYG-----DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMM- 85
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 ----FQD------ARLlpwkTVMDN------------VGLGLKGSWREDARQALAAV--GLENRAGEWPAALSGGQKQRV 141
Cdd:COG1101 82 igrvFQDpmmgtaPSM----TIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 142 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVS 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
10-211 |
7.01e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 120.33 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTIL------NALD---LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTiQ 79
Cdd:COG4167 2 SALLeVRNLSKTFKYRTGLfrrqqfEAVKpvsFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDT------RMMFQDArllpwKTVMD---NVG------LGLKGSWREDARQA-----LAAVGL-ENRAGEWPAALSGGQK 138
Cdd:COG4167 81 DYKyrckhiRMIFQDP-----NTSLNprlNIGqileepLRLNTDLTAEEREErifatLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 139 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-211 |
1.05e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.41 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTplstiqddTRMMF--Q 87
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------VKIGYfdQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLL-PWKTVMDNVGLGLKGSWREDARQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 165
Cdd:COG0488 386 HQEELdPDKTVLDELRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD- 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 166 ltrIEMQDLIETLWQTHGFTVLLVTHDVS--EAVamADRVLLIEEGKI 211
Cdd:COG0488 465 ---IETLEALEEALDDFPGTVLLVSHDRYflDRV--ATRILEFEDGGV 507
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
16-211 |
1.09e-32 |
|
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: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTPLSTIQDDTRMM---FQDARL 91
Cdd:TIGR03864 6 GLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQIsVAGHDLRRAPRAALARLgvvFQQPTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LPWKTVMDNV-------GLGlKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR03864 86 DLDLSVRQNLryhaalhGLS-RAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLWQTHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 211
Cdd:TIGR03864 165 PASRAAITAHVRALARDQGLSVLWATHLVDE-IEASDRLVVLHRGRV 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-214 |
1.97e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 119.35 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL----EAPNSGDILAGttplSTIQDDTRM-------- 84
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLG----RTVQREGRLardirksr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 -----MFQDARLLPWKTVMDNVGLGLKGS---WR-----------EDARQALAAVGLENRAGEWPAALSGGQKQRVALAR 145
Cdd:PRK09984 86 antgyIFQQFNLVNRLSVLENVLIGALGStpfWRtcfswftreqkQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 146 ALIHRPGLLLLDEPLGALDALT-RIEMqDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESaRIVM-DTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-214 |
2.84e-32 |
|
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: 117.69 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTI--LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM-----MF 86
Cdd:cd03245 5 FRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRrnigyVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLpWKTVMDNVGLGLKGSwrEDARqALAAV--------------GLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:cd03245 85 QDVTLF-YGTLRDNITLGAPLA--DDER-ILRAAelagvtdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 153 LLLLDEPLGALDalTRIEMQdLIETLWQ-THGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 214
Cdd:cd03245 161 ILLLDEPTSAMD--MNSEER-LKERLRQlLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-211 |
2.90e-32 |
|
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: 118.16 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF-- 86
Cdd:COG0410 1 MPMLeVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 ----QDARLLPWKTVMDNVGLGLK-GSWREDARQALAAVG-----LENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:COG0410 81 gyvpEGRRIFPSLTVEENLLLGAYaRRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-206 |
4.36e-32 |
|
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: 123.17 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 11 PLLLNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM----- 84
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPwKTVMDNVGLGLKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:TIGR02857 401 VPQHPFLFA-GTIAENIRLARPDASDAEIREALERAgldefvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 154 LLLDEPLGALDALTRIEMQDLIETLWQTHgfTVLLVTHDVsEAVAMADRVLLI 206
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRL-ALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-211 |
5.35e-32 |
|
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: 117.33 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDN-TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI-QDDTR----MMFQ 87
Cdd:cd03253 3 FENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtLDSLRraigVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPwKTVMDNVGLGLKGSWREDARQALAAVGLENRAGEWPAA-----------LSGGQKQRVALARALIHRPGLLLL 156
Cdd:cd03253 83 DTVLFN-DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLwqTHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 211
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST-IVNADKIIVLKDGRI 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-211 |
5.42e-32 |
|
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: 117.33 E-value: 5.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDT-RMMF----QDARLLPwKTVMDN 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIgvvlQDTFLFS-GTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 VGLGLKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:cd03254 97 IRLGRPNATDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLwqTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03254 177 LIQEALEKL--MKGRTSIIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-211 |
6.74e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 123.30 E-value: 6.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRY--GDNTI--LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR- 83
Cdd:PRK10535 2 TALLeLKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 --------MMFQDARLLPWKTVMDNV-------GLGlKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALI 148
Cdd:PRK10535 82 qlrrehfgFIFQRYHLLSHLTAAQNVevpavyaGLE-RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 149 HRPGLLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-211 |
6.87e-32 |
|
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: 117.26 E-value: 6.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ-DDTRMMF----QDARLLPwKTV 97
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQIglvsQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MDNVGLGLKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKAnihdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1880204416 167 TRIEMQDLIETLwqTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03249 174 SEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-211 |
1.25e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.16 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTP-----LSTIQDDTRMMFQDA-RLLPWKTVMDN 100
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKHIGIVFQNPdNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 VGLGLKG------SWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 174
Cdd:PRK13648 105 VAFGLENhavpydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1880204416 175 IETLWQTHGFTVLLVTHDVSEAVAmADRVLLIEEGKI 211
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-192 |
2.95e-31 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 120.54 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 8 QGTPLLLNGVTKRY-GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTPLSTIQDDTRMM 85
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtLDGVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 F----QDARLLPwKTVMDNVGLGLKGSWREDARQALAAVGLEN-----------RAGEWPAALSGGQKQRVALARALIHR 150
Cdd:TIGR02868 411 VsvcaQDAHLFD-TTVRENLRLARPDATDEELWAALERVGLADwlralpdgldtVLGEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMqdlIETLWQ-THGFTVLLVTHD 192
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADEL---LEDLLAaLSGRTVVLITHH 529
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-211 |
3.02e-31 |
|
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: 114.91 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGD--NTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMM---- 85
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGL--GLKGSWREDAR----QALAAVGLE----NRAGEwpaaLSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLKGLPKSEIKeeveLLLRVLGLTdkanKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIetLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-218 |
3.82e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.75 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLStiQDDTRM---MFQD 88
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRigyLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVG-LG-LKGSWREDARQALAA----VGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG4152 80 RGLYPKMKVGEQLVyLArLKGLSKAEAKRRADEwlerLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 163 LDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG4152 160 LDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-211 |
6.16e-31 |
|
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: 112.52 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLStiqddtrmmFQDARllp 93
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------FASPR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 wktvmdnvglglkgswreDARQA-LAAVglenragewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 172
Cdd:cd03216 71 ------------------DARRAgIAMV----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 1880204416 173 DLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03216 123 KVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-211 |
6.51e-31 |
|
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: 114.56 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTtplstiQDDTRM-MFQDAR 90
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG------QDITKLpMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 L----LPWK-------TVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:cd03218 75 LgigyLPQEasifrklTVEENILAVLeirglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 154 LLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-211 |
7.54e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 31 DLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTplsTIQDDTR------------MMFQ--DARLLPwKT 96
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGER---VITAGKKnkklkplrkkvgIVFQfpEHQLFE-ET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNVGLGLK--GSWREDA----RQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:PRK13634 103 VEKDICFGPMnfGVSEEDAkqkaREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-211 |
1.01e-30 |
|
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: 114.12 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILA-----GTTPLSTIQDDTRMMF 86
Cdd:cd03252 3 FEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdlALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPwKTVMDNVGLGLKGSWRED----ARQALA-------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03252 83 QENVLFN-RSIRDNIALADPGMSMERvieaAKLAGAhdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 156 LDEPLGALDALT-RIEMQDLIETLwqtHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03252 162 FDEATSALDYESeHAIMRNMHDIC---AGRTVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-211 |
1.07e-30 |
|
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: 119.97 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTI--LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPL-----STIQDDTRMMF 86
Cdd:TIGR03375 466 FRNVSFAYPGQETpaLDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqidpADLRRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLpWKTVMDNVGLGLKGSWREDARQALAAVGLENRA-----------GEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:TIGR03375 546 QDPRLF-YGTLRDNIALGAPYADDEEILRAAELAGVTEFVrrhpdgldmqiGERGRSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 156 LDEPLGALDAltRIEMQdLIETLWQ-THGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR03375 625 LDEPTSAMDN--RSEER-FKDRLKRwLAGKTLVLVTHRTS-LLDLVDRIIVMDNGRI 677
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-214 |
2.01e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 111.64 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDN--TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF--- 86
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIsvl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 -QDARLLPwKTVMDNVGlglkgswredarqalaavglenragewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:cd03247 81 nQRPYLFD-TTLRNNLG----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 166 LTRiemQDLIETLWQ-THGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 214
Cdd:cd03247 132 ITE---RQLLSLIFEvLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-204 |
3.43e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.50 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 6 LNQGTPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD--- 81
Cdd:PRK10247 1 MQENSPLLqLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 --------TRMMFQDarllpwkTVMDNvglgLKGSW--REDA------RQALAAVGLENRAGEWP-AALSGGQKQRVALA 144
Cdd:PRK10247 81 qqvsycaqTPTLFGD-------TVYDN----LIFPWqiRNQQpdpaifLDDLERFALPDTILTKNiAELSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 145 RALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEaVAMADRVL 204
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVI 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
3.89e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.82 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 1 MNTARLNQGTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLR-------LLAGLEApnSG------- 66
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGeilldge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 67 DILAGTTPLSTIqddtR----MMFQDARLLPwKTVMDNVGLGL-------KGSWREDARQALAAVGL----ENRAGEWPA 131
Cdd:COG1117 79 DIYDPDVDVVEL----RrrvgMVFQKPNPFP-KSIYDNVAYGLrlhgiksKSELDEIVEESLRKAALwdevKDRLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 132 ALSGGQKQRVALARALIHRPGLLLLDEPLGALD--ALTRIEmqDLIETLWQThgFTVLLVTHDVSEAVAMADRVL----- 204
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILELKKD--YTIVIVTHNMQQAARVSDYTAffylg 229
|
....*..
gi 1880204416 205 -LIEEGK 210
Cdd:COG1117 230 eLVEFGP 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-211 |
3.90e-30 |
|
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: 117.90 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTI--LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ-DDTRMMF----QD 88
Cdd:TIGR02203 335 NVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlASLRRQValvsQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPwKTVMDNVGLG-LKGSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:TIGR02203 415 VVLFN-DTIANNIAYGrTEQADRAEIERALAAAyaqdfvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQthGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-211 |
4.86e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 113.32 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL--------AGTTPLSTIQDDTRMMFQ 87
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipaMSRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLGLkgswREDAR-----------QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK11831 92 SGALFTDMNVFDNVAYPL----REHTQlpapllhstvmMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-211 |
5.99e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL----EAPNSGDILAGTT----PLSTIQDDTRMMFQ--DARLLPwK 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITltakTVWDIREKVGIVFQnpDNQFVG-A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 TVMDNVGLGL--KGSWRED----ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:PRK13640 101 TVGDDVAFGLenRAVPRPEmikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK13640 181 QILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-211 |
8.34e-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: 116.71 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKS----TLLRLLAGLEAPNSGDI-LAGTTPLSTIQDDTR--------MMFQD 88
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlFDGQDLLGLSERELRrirgnriaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 --ARLLPWKTVMDNVG------LGLKGS-WREDARQALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:COG4172 101 pmTSLNPLHTIGKQIAevlrlhRGLSGAaARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHD---VSEavaMADRVLLIEEGKI 211
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVMRQGEI 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
1.12e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.01 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGD--NTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTT----PLSTIQDDTRMMF 86
Cdd:PRK13632 10 VENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITiskeNLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 Q--DARLLPwKTVMDNVGLGL--KGSWREDARQ----ALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK13632 90 QnpDNQFIG-ATVEDDIAFGLenKKVPPKKMKDiiddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVaMADRVLLIEEGKI 211
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-203 |
1.90e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGT-TPLSTIQDDTR--- 83
Cdd:COG1129 2 EPLLeMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlLDGEpVRFRSPRDAQAagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 -MMFQDARLLPWKTVMDNVGLG---LKGSW------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG1129 82 aIIHQELNLVPNLSVAENIFLGrepRRGGLidwramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 154 LLLDEPlgaLDALTRIEMQ---DLIETLwQTHGFTVLLVTHDVSEAVAMADRV 203
Cdd:COG1129 162 LILDEP---TASLTEREVErlfRIIRRL-KAQGVAIIYISHRLDEVFEIADRV 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-221 |
3.18e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 115.29 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 3 TARLNQGTPLLLNGVT-KRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIlagttplsTIQDD 81
Cdd:COG4178 354 RIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 TRMMFqdarlLPWKTVMDNVGL-------GLKGSW-REDARQALAAVGLENRAG------EWPAALSGGQKQRVALARAL 147
Cdd:COG4178 426 ARVLF-----LPQRPYLPLGTLreallypATAEAFsDAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 148 IHRPGLLLLDEPLGALDALTRIEM-QDLIETLWQThgfTVLLVTHDvSEAVAMADRVLLIEEGKIGLDLTVDIPR 221
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALyQLLREELPGT---TVISVGHR-STLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-211 |
7.56e-29 |
|
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: 114.15 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI-QDDTR----------MMFQDar 90
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtQASLRaaigivpqdtVLFND-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 llpwkTVMDNVGLGLKGSWREDARQA--LAAV---------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG5265 447 -----TIAYNIAYGRPDASEEEVEAAarAAQIhdfieslpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQTHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG5265 522 TSALDSRTERAIQAALREVARGR--TTLVIAHRLS-TIVDADEILVLEAGRI 570
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-210 |
7.88e-29 |
|
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: 106.38 E-value: 7.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIlagttplstiqddtrmmfqdarllp 93
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 wkTVMDNVGLGLkgswredarqalaavgLENragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQD 173
Cdd:cd03221 58 --TWGSTVKIGY----------------FEQ--------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIE 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 1880204416 174 LIETLWQTHGFTVLLVTHDVS--EAVamADRVLLIEEGK 210
Cdd:cd03221 108 ALEEALKEYPGTVILVSHDRYflDQV--ATKIIELEDGK 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-211 |
9.75e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.33 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDdtRMMFQDA 89
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS--RQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWK-------TVMDNVGLG----------LKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:PRK11231 79 ALLPQHhltpegiTVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 153 LLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-211 |
1.09e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.02 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR-----MMFQD 88
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrlaILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ----ARLlpwkTVMDNVGLG--------LKgswREDAR---QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG4604 84 nhinSRL----TVRELVAFGrfpyskgrLT---AEDREiidEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 154 LLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-211 |
1.19e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.92 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAG--TTP------LSTIQDDTRMMFQ--DARLLPwK 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGyhITPetgnknLKKLRKKVSLVFQfpEAQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 TVMDNVGLGLKG------SWREDARQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13641 102 TVLKDVEFGPKNfgfsedEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1880204416 169 IEMQDLIETlWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13641 182 KEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-211 |
2.47e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.61 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 2 NTARLNQGTpLLLNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ 79
Cdd:PRK11160 330 STAAADQVS-LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDT--RMM---------FQDarllpwkTVMDNVGLGLKGSWREDARQALAAVGLENRA----------GEWPAALSGGQK 138
Cdd:PRK11160 409 EAAlrQAIsvvsqrvhlFSA-------TLRDNLLLAAPNASDEALIEVLQQVGLEKLLeddkglnawlGEGGRQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 139 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQthGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQI 551
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-210 |
2.96e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.12 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 11 PLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF---- 86
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLPWKTVMDNVGL-----GLK-GSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVfgryfGLSaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 161 GALDALTRIEMQDLIETLWqTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-225 |
3.36e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL------AGTTPLSTIQDDTRMMFQ--DARLLPwKTVM 98
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtSDEENLWDIRNKAGMVFQnpDNQIVA-TIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVG-----LGLKGS-WREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 172
Cdd:PRK13633 105 EDVAfgpenLGIPPEeIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 173 DLIETLWQTHGFTVLLVTHDVSEAVAmADRVLLIEEGKIGLDLTvdiprPRRV 225
Cdd:PRK13633 185 NTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT-----PKEI 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-211 |
4.38e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGttplstiQDDTRM-MFQDA 89
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfLDG-------EDITHLpMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RL----LP------WK-TVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:COG1137 77 RLgigyLPqeasifRKlTVEDNILAVLelrklsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 153 LLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-211 |
4.97e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.28 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM-----------MFQDARLLPwKTVM 98
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIkpvrkkvgvvfQFPESQLFE-ETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVGLGLK--GSWREDAR----QALAAVGLENRAGE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 171
Cdd:PRK13643 104 KDVAFGPQnfGIPKEKAEkiaaEKLEMVGLADEFWEkSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1880204416 172 QDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13643 184 MQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-211 |
7.11e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.48 E-value: 7.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeAPNSGDILAGTTPLSTIqDDTRMMFQDARL-----LPWKTVMDNVGLG 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPESWRKHLSWVgqnpqLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 105 LKGSWREDARQALA-----------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQD 173
Cdd:PRK11174 447 NPDASDEQLQQALEnawvseflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE---QL 523
|
170 180 190
....*....|....*....|....*....|....*....
gi 1880204416 174 LIETLWQ-THGFTVLLVTHDVSEAVAMaDRVLLIEEGKI 211
Cdd:PRK11174 524 VMQALNAaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-225 |
1.33e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 7 NQGTPLllngvtkrygDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSG-------DILAGTTPLSTIQ 79
Cdd:PRK13637 13 MEGTPF----------EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDTRMMFQ--DARLLPwKTVMDNVGLGLKGSWRED------ARQALAAVGL--ENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK13637 83 KKVGLVFQypEYQLFE-ETIEKDIAFGPINLGLSEeeienrVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 150 RPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTvdiprPRRV 225
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT-----PREV 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-211 |
1.82e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.08 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 21 YGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----EAPNSGDI-LAGTTPLSTIQDDTR------MMFQD 88
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVrLFGRNIYSPDVDPIEvrrevgMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLK--------GSWREDARQALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKlnglvkskKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLwqTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-211 |
1.89e-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: 105.14 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNT----ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-AGTTPLSTIQDDTRMM- 85
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvDGFDVVKEPAEARRRLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 --FQDARLLPWKTVMDNVGL-----GLKGSWREDARQALAAV-----GLENRAGEwpaaLSGGQKQRVALARALIHRPGL 153
Cdd:cd03266 82 fvSDSTGLYDRLTARENLEYfaglyGLKGDELTARLEELADRlgmeeLLDRRVGG----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 154 LLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-210 |
2.58e-27 |
|
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: 104.09 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 18 TKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQddtrmmfqdarlLPW--- 94
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQ------------EPWiqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 95 KTVMDNVGLGLKgsWREDA-RQALAAVGLEN-----------RAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03250 80 GTIRENILFGKP--FDEERyEKVIKACALEPdleilpdgdltEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 163 LDALT--RIeMQDLIETLWQtHGFTVLLVTHDVsEAVAMADRVLLIEEGK 210
Cdd:cd03250 158 VDAHVgrHI-FENCILGLLL-NNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
3.04e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS-------TIQDDTRMMFQDA-R 90
Cdd:PRK13636 14 NYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmKLRESVGMVFQDPdN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGL------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:PRK13636 94 QLFSASVYQDVSFGAvnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-211 |
5.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST---------IQDDTRMMFQ--DARLLPwKTVM 98
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdikqIRKKVGLVFQfpESQLFE-ETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVGLGLK--GSWREDA----RQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 171
Cdd:PRK13649 105 KDVAFGPQnfGVSQEEAealaREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1880204416 172 QDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13649 185 MTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-211 |
6.57e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.87 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 1 MNTARLNQGTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIqd 80
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 81 DTRMMFQDARLLPWK-------TVMDNVGLGlKGSW-----------REDARQALAAVGLENRAGEWPAALSGGQKQRVA 142
Cdd:PRK10575 79 SSKAFARKVAYLPQQlpaaegmTVRELVAIG-RYPWhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 143 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-211 |
7.64e-27 |
|
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: 108.30 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF-----QDARLLPwKT 96
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHigylpQDVELFD-GT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNVGlglkgswR---EDARQALAAV--------------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG4618 422 IAENIA-------RfgdADPEKVVAAAklagvhemilrlpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 160 LGALDAltRIEmQDLIETLWQ--THGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG4618 495 NSNLDD--EGE-AALAAAIRAlkARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-211 |
1.67e-26 |
|
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: 102.60 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR----MMF- 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaragIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 -QDARLLPWKTVMDNVGLGLKGSWREDAR---------QALAAVgLENRAGEwpaaLSGGQKQRVALARALIHRPGLLLL 156
Cdd:TIGR03410 81 pQGREIFPRLTVEENLLTGLAALPRRSRKipdeiyelfPVLKEM-LGRRGGD----LSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-211 |
1.81e-26 |
|
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: 102.55 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD-----TRMMFQDARLLPwKTV 97
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylhskVSLVGQEPVLFA-RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MDNVGLGLKG----SWREDARQALA-------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03248 105 QDNIAYGLQScsfeCVKEAAQKAHAhsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1880204416 167 TRIEMQDLIETLWQTHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03248 185 SEQQVQQALYDWPERR--TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-211 |
2.19e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 21 YGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----EAPNSGDILAG-----TTPLSTIQDDTRMMFQDAR 90
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDgqdifKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGLK--------GSWREDARQALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK14247 93 PIPNLSIFENVALGLKlnrlvkskKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQThgFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-191 |
3.30e-26 |
|
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: 101.28 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD-TRMMF---- 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDArLLPWKTVMDNVGL--GLKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR01189 81 LPG-LKPELSALENLHFwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|
gi 1880204416 165 AltriEMQDLIETLWQTH---GFTVLLVTH 191
Cdd:TIGR01189 160 K----AGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-210 |
3.57e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.53 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF----QDA 89
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIgvvpQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVgLGLKGSWREDARQALAAVG-------LENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK13536 124 NLDLEFTVRENL-LVFGRYFGMSTREIEAVIPsllefarLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 163 LDALTRIEMQDLIETLWqTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13536 203 LDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-213 |
4.83e-26 |
|
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: 101.32 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLStiQDDTR---MMFQD 88
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT--RKDLHkigSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVG-----LGLKGSWREdarQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:TIGR03740 79 PPLYENLTARENLKvhttlLGLPDSRID---EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 164 DALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 213
Cdd:TIGR03740 156 DPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGY 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-211 |
6.53e-26 |
|
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: 105.98 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIqdDTRMMFQDAR 90
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWK------TVMDNVGLGLK-GSWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:TIGR01193 552 YLPQEpyifsgSILENLLLGAKeNVSQDEIWAACEIAeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 153 LLLLDEPLGALDALTRiemQDLIETLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:TIGR01193 632 VLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKI 686
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-204 |
7.45e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.12 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL--------AGTTPLSTIQDDTRMMFQD--ARLLPWKT 96
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdllkADPEAQKLLRQKIQIVFQNpyGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMD--------NVGLGlKGSWREDARQALAAVGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK11308 111 VGQileeplliNTSLS-AAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1880204416 168 RIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVL 204
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-233 |
2.26e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 9 GTPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLsTIQD--DTR-- 83
Cdd:COG3845 2 MPPALeLRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSprDAIal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 ---MMFQDARLLPWKTVMDNVGLGLKGSW-----REDARQALAAV----GLE----NRAGEwpaaLSGGQKQRVALARAL 147
Cdd:COG3845 81 gigMVHQHFMLVPNLTVAENIVLGLEPTKggrldRKAARARIRELseryGLDvdpdAKVED----LSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 148 IHRPGLLLLDEPLGaldALTRIEMQDLIETLWQ--THGFTVLLVTHDVSEAVAMADRVLLIEEGKigldlTVDIPRPRRV 225
Cdd:COG3845 157 YRGARILILDEPTA---VLTPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGK-----VVGTVDTAET 228
|
....*...
gi 1880204416 226 GSARLAEL 233
Cdd:COG3845 229 SEEELAEL 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-204 |
3.18e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.71 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALD---LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL--------AGTTPLSTIQDDTRMMFQD--ARLLP 93
Cdd:PRK15079 34 LKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgMKDDEWRAVRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WKTVMDNVGLGL--------KGSWREDARQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:PRK15079 114 RMTIGEIIAEPLrtyhpklsRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1880204416 165 ALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVL 204
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-221 |
3.22e-25 |
|
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: 99.90 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 11 PLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIqDDTRMMFQDA 89
Cdd:TIGR02323 2 PLLqVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAEL-ELYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLL---PWKTVMDNVGLGLK---------------------GSWREDARQALAAVGLE-NRAGEWPAALSGGQKQRVALA 144
Cdd:TIGR02323 81 RRLmrtEWGFVHQNPRDGLRmrvsaganigerlmaigarhyGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 145 RALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GL-DLTVDIP 220
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesGLtDQVLDDP 240
|
.
gi 1880204416 221 R 221
Cdd:TIGR02323 241 Q 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
36-211 |
3.37e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 36 AGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPL-----STIQDDTRMMFQDA--RLLPWKTV---MD---NVG 102
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySYRSQRIRMIFQDPstSLNPRQRIsqiLDfplRLN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 103 LGLKGSWREDA-RQALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQ 180
Cdd:PRK15112 118 TDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE 197
|
170 180 190
....*....|....*....|....*....|.
gi 1880204416 181 THGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK15112 198 KQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
5.00e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS-------TIQDDTRMMFQ---D 88
Cdd:PRK13639 10 SYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQnpdD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPwkTVMDNVG-----LGL-KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK13639 90 QLFAP--TVEEDVAfgplnLGLsKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1880204416 163 LDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13639 168 LDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-221 |
5.36e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-----AGTTPLSTI-QDDT 82
Cdd:PRK11701 4 QPLLsVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdGQLRDLYALsEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 RMMF--------QDAR--LLPWKTVMDNVG-----LGLK--GSWREDARQALAAVGLE-NRAGEWPAALSGGQKQRVALA 144
Cdd:PRK11701 84 RRLLrtewgfvhQHPRdgLRMQVSAGGNIGerlmaVGARhyGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 145 RALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GL-DLTVDIP 220
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesGLtDQVLDDP 243
|
.
gi 1880204416 221 R 221
Cdd:PRK11701 244 Q 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-210 |
6.67e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI--QDDTRM-- 84
Cdd:PRK11300 3 QPLLsVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIARMgv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 --MFQDARLLPWKTVMDNV--------------GLGLKGSWREDARQAL--AAVGLE--------NR-AGEwpaaLSGGQ 137
Cdd:PRK11300 83 vrTFQHVRLFREMTVIENLlvaqhqqlktglfsGLLKTPAFRRAESEALdrAATWLErvgllehaNRqAGN----LAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 138 KQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-214 |
7.11e-25 |
|
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: 98.56 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 5 RLNQGTPLLLNGVT----KRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTP----- 74
Cdd:cd03267 11 RVYSKEPGLIGSLKslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPwkrrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 75 --LSTIqddTRMMFQDARL---LPwktVMDNVGLgLKGSWREDARQALAAVG-------LENRAGEWPAALSGGQKQRVA 142
Cdd:cd03267 91 kfLRRI---GVVFGQKTQLwwdLP---VIDSFYL-LAAIYDLPPARFKKRLDelselldLEELLDTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 143 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-245 |
8.04e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.40 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAP-----NSGDILAGTTPLSTIQD------DTRMM 85
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDvlefrrRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPwKTVMDNVGLGLKG-------SWREDARQALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK14271 107 FQRPNPFP-MSIMDNVLAGVRAhklvprkEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 155 LLDEPLGALDALTRIEMQDLIETLwqTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD--IPRPRRVGSAR-LA 231
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEqlFSSPKHAETARyVA 263
|
250
....*....|....
gi 1880204416 232 ELEAEVLDrvMKRG 245
Cdd:PRK14271 264 GLSGDVKD--AKRG 275
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
27-209 |
9.78e-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: 97.89 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL----AGTTPLSTIQDDTRMMF---------QDARLLP 93
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdGGWVDLAQASPREILALrrrtigyvsQFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WKTVMDNVGLGL------KGSWREDARQALAAVGLENRAgeW---PAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:COG4778 107 RVSALDVVAEPLlergvdREEARARARELLARLNLPERL--WdlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLwQTHGFTVLLVTHD--VSEAVamADRVLLIEEG 209
Cdd:COG4778 185 AANRAVVVELIEEA-KARGTAIIGIFHDeeVREAV--ADRVVDVTPF 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-212 |
1.35e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLStiQDDTRMMFQDARL------LPWKT 96
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV--QYDHHYLHRQVALvgqepvLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNVGLGLKGSWREDARQALAAVGLENRAGEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 166 ltriEMQDLIETLWQTHGFTVLLVTHDVSeAVAMADRVLLIEEGKIG 212
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVV 692
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-211 |
1.94e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 101.63 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTT-----PLSTIQDDTRMMFQDARLLPwKTV 97
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVALVSQNVHLFN-DTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MDNVGLGLKGSW-RED----ARQALAA-------VGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK11176 434 ANNIAYARTEQYsREQieeaARMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 166 LTRIEMQDLIETLWQTHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PRK11176 514 ESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEI 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-211 |
2.16e-24 |
|
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: 96.08 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 25 TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--EAPNSGDILAGTTPLS--TIQDDTRMMFQDARLLPWKTVmdn 100
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDkrSFRKIIGYVPQDDILHPTLTV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 vglglkgswredaRQALA-AVGLENragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLW 179
Cdd:cd03213 100 -------------RETLMfAAKLRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA 158
|
170 180 190
....*....|....*....|....*....|...
gi 1880204416 180 QThGFTVLLVTHDVS-EAVAMADRVLLIEEGKI 211
Cdd:cd03213 159 DT-GRTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
36-211 |
3.29e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.81 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 36 AGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIqddTR--------MMFQDARLLPwKTVMDNVGLGLKG 107
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRaslrrniaVVFQDAGLFN-RSIEDNIRVGRPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 108 SWREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 176
Cdd:PRK13657 436 ATDEEMRAAAERAqahdfierkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD 515
|
170 180 190
....*....|....*....|....*....|....*
gi 1880204416 177 TLwqTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PRK13657 516 EL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-225 |
3.40e-24 |
|
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: 100.65 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 8 QGTPLL-LNGVTKRYG--DNTILNALD---LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGD--ILAGT--TPLST 77
Cdd:TIGR03269 275 VGEPIIkVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 78 IQDDTR--------MMFQDARLLPWKTVMDN----VGLGLKGSW-REDARQALAAVGLENRAGE-----WPAALSGGQKQ 139
Cdd:TIGR03269 355 PGPDGRgrakryigILHQEYDLYPHRTVLDNlteaIGLELPDELaRMKAVITLKMVGFDEEKAEeildkYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 140 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDI 219
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI-----VKI 509
|
....*.
gi 1880204416 220 PRPRRV 225
Cdd:TIGR03269 510 GDPEEI 515
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-232 |
3.52e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.36 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS-----TIQDDTRMMFQDARL 91
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaskEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LPWKTVMDNVGLG------LKGSWR---EDA-RQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK10253 93 PGDITVQELVARGryphqpLFTRWRkedEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDIPRPRRVGSARLAE 232
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI-----VAQGAPKEIVTAELIE 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-211 |
4.02e-24 |
|
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: 96.45 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 19 KRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGT-TPLSTIQddtrmmfqdARLLPWKT 96
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtVRGRvSSLLGLG---------GGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNV--GLGLKGSWREDARQALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 170
Cdd:cd03220 101 GRENIylNGRLLGLSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1880204416 171 MQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03220 181 CQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-191 |
5.72e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 95.26 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDtrmMFQD-----------AR 90
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---YHQDllylghqpgikTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 LLPWKTVMDNVGLGLKGSwREDARQALAAVGLENRAgEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltri 169
Cdd:PRK13538 89 LTALENLRFYQRLHGPGD-DEALWEALAQVGLAGFE-DVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK---- 162
|
170 180
....*....|....*....|....*
gi 1880204416 170 EMQDLIETLWQTH---GFTVLLVTH 191
Cdd:PRK13538 163 QGVARLEALLAQHaeqGGMVILTTH 187
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-211 |
1.17e-23 |
|
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: 95.13 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN----SGDILAGTTPL---STIQDDTRMMFQDAR--LLPWKTVMDN 100
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLlplSIRGRHIATIMQNPRtaFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 V--GLGLKGSWREDAR----QALAAVGLENRA---GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 171
Cdd:TIGR02770 85 AieTLRSLGKLSKQARalilEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1880204416 172 QDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
1.51e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.96 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTPLSTIQDDTR----MMFQDAR-LL 92
Cdd:PRK13647 13 RYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRskvgLVFQDPDdQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PWKTVMDNVG-----LGLKGS-WREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:PRK13647 93 FSSTVWDDVAfgpvnMGLDKDeVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 167 TRiemQDLIETLWQTH--GFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13647 173 GQ---ETLMEILDRLHnqGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-211 |
2.93e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 19 KRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST-----IQDDTRMMFQDA-RLL 92
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnLRRKIGMVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PWKTVMDNVGLGL--KGSWRED----ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:PRK13642 95 VGATVEDDVAFGMenQGIPREEmikrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1880204416 167 TRIEMQDLIETLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-211 |
5.91e-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: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 15 NGVTKRYGDN--TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ-DDTRMMF----Q 87
Cdd:cd03244 6 KNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSRIsiipQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPwKTVMDNvgLGLKGSWREDA-RQALAAVGLENRAGEWPAAL-----------SGGQKQRVALARALIHRPGLLL 155
Cdd:cd03244 86 DPVLFS-GTIRSN--LDPFGEYSDEElWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETlwQTHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:cd03244 163 LDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRL-DTIIDSDRILVLDKGRV 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-216 |
6.23e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.40 E-value: 6.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDdTRMMFQDARL 91
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT-AKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LP-------WKTVMDNVGLGLKGSWREDARQALAAV-----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11614 85 VPegrrvfsRMTVEENLAMGGFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 160 LGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-211 |
9.69e-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: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRY-GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST-----IQDDTRMMFQ 87
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPwKTVMDNVGLGLKGSwREDARQALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK10790 423 DPVVLA-DTFLANVTLGRDIS-EEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHgfTVLLVTHDVSEAVAmADRVLLIEEGKI 211
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-201 |
1.11e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 21 YGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLR-------LLAGLEAPNS-----GDILAGTTPLSTIQDDTRMMFQD 88
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVEGKvtfhgKNLYAPDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPwKTVMDNVG-----LGLKGSWRE----DARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK14243 100 PNPFP-KSIYDNIAygariNGYKGDMDElverSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQThgFTVLLVTHDVSEAVAMAD 201
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-191 |
1.79e-22 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 90.29 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIlagttplsTIQDDTRMMFqdarlLPWKTVMDNVG 102
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLF-----LPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 103 LglkgswredaRQALAAvglenragEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIETLWQTH 182
Cdd:cd03223 80 L----------REQLIY--------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKEL 137
|
....*....
gi 1880204416 183 GFTVLLVTH 191
Cdd:cd03223 138 GITVISVGH 146
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-230 |
2.48e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLST-----IQDDTRMMFQ---DARLLP 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenireVRKFVGLVFQnpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 wkTVMDNVG-----LGL-KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK13652 95 --TVEQDIAfgpinLGLdEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 168 RIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD--IPRPRRVGSARL 230
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEeiFLQPDLLARVHL 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-214 |
3.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNT-ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL------AGTTPLSTIQDDTRMMF 86
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidtGDFSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARL-LPWKTVMDNVGLGLKG------SWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK13644 84 QNPETqFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 160 LGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEaVAMADRVLLIEEGKIGLD 214
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-204 |
3.85e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI--LAGttplstiqdDTRmmfqDAR- 90
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGG---------DMA----DARh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 91 ------------------LLPWKTVMDNVGL-----GLKGSWREdARQA--LAAVGLE---NRagewPAA-LSGGQKQRV 141
Cdd:NF033858 71 rravcpriaympqglgknLYPTLSVFENLDFfgrlfGQDAAERR-RRIDelLRATGLApfaDR----PAGkLSGGMKQKL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 142 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTH-GFTVLLVTHDVSEA------VAM-ADRVL 204
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAerfdwlVAMdAGRVL 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-211 |
5.53e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKR-YGDNTILNALDLHIPAGQFVAVVGRSGGGKST----LLRLLAgleapNSGDILAGTTPLST--------IQDDT 82
Cdd:PRK15134 290 GILKRtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNlnrrqllpVRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 RMMFQD--ARLLPWKTVMDNVGLGLK-------GSWREDA-RQALAAVGL--ENRAgEWPAALSGGQKQRVALARALIHR 150
Cdd:PRK15134 365 QVVFQDpnSSLNPRLNVLQIIEEGLRvhqptlsAAQREQQvIAVMEEVGLdpETRH-RYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-225 |
9.83e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 9 GTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS-----TIQDDTR 83
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsarAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 MMFQDARLLPWKTVMDNVGLGLK------GSWREDAR----QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTphrsrfDTWTETDRaaveRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 154 LLLDEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDIPRPRRV 225
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV-----RAAGPPADV 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-211 |
1.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.30 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 7 NQGTPLLLNgvtkrygdntILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSG-------------------- 66
Cdd:PRK13651 13 NKKLPTELK----------ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 67 ---DILAGTTPLSTIQD--DTR----MMFQDARLLPWKTVMDN------VGLGL-KGSWREDARQALAAVGL-ENRAGEW 129
Cdd:PRK13651 83 vleKLVIQKTRFKKIKKikEIRrrvgVVFQFAEYQLFEQTIEKdiifgpVSMGVsKEEAKKRAAKYIELVGLdESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 130 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 1880204416 210 KI 211
Cdd:PRK13651 242 KI 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-191 |
1.28e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMF---QDArLLPWKTVM 98
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghRNA-MKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVGL--GLKGSWREDARQALAAVGLeNRAGEWPAA-LSGGQKQRVALARALI-HRPgLLLLDEPLGALDALTriemQDL 174
Cdd:PRK13539 92 ENLEFwaAFLGGEELDIAAALEAVGL-APLAHLPFGyLSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAA----VAL 165
|
170 180
....*....|....*....|
gi 1880204416 175 IETLWQTH---GFTVLLVTH 191
Cdd:PRK13539 166 FAELIRAHlaqGGIVIAATH 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-211 |
1.50e-21 |
|
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: 89.64 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--EAPN-SGDILAGTTPLS--TIQDDTRMMFQDARLLPWKTVMDN 100
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTtSGQILFNGQPRKpdQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 ----VGLGLKGSWREDARQALAAVGLENRAGEWPAA------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIe 170
Cdd:cd03234 102 ltytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1880204416 171 mqDLIETLWQT--HGFTVLLVTHD-VSEAVAMADRVLLIEEGKI 211
Cdd:cd03234 181 --NLVSTLSQLarRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-191 |
3.13e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.48 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGlEAPNSGDILAGTTPLSTIQDDtrmmfqdarllpwK 95
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-ALKGTPVAGCVDVPDNQFGRE-------------A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 TVMDNVglGLKGSwREDARQALAAVGLeNRAGEW---PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 172
Cdd:COG2401 101 SLIDAI--GRKGD-FKDAVELLNAVGL-SDAVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*....
gi 1880204416 173 DLIETLWQTHGFTVLLVTH 191
Cdd:COG2401 177 RNLQKLARRAGITLVVATH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-204 |
3.37e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.02 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI----------------LAGTTPLST 77
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrngklrigyvpqklyLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 78 iqddTRMMfqdaRLLPwktvmdnvglglkGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK09544 87 ----NRFL----RLRP-------------GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 158 EPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVL 204
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-214 |
4.02e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-AGTTP------------------------LSTIqdDTRM 84
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPfkrrkefarrigvvfgqrsqlwwdLPAI--DSFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 MFQDARLLPWKTVMDNVG-----LGLKGSWREDARQalaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG4586 119 LLKAIYRIPDAEYKKRLDelvelLDLGELLDTPVRQ-----------------LSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 160 -LGaLDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:COG4586 182 tIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-202 |
8.74e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 8.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 21 YGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLL------------AGLEAPNSGDILAGTTPLSTIQDDTRMMFQD 88
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWkTVMDNVGLGLKGSWREDARQALAAVG-----------LENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK14239 95 PNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEkslkgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 158 EPLGALDALT--RIEmqdliETLWQ-THGFTVLLVTHDVSEAVAMADR 202
Cdd:PRK14239 174 EPTSALDPISagKIE-----ETLLGlKDDYTMLLVTRSMQQASRISDR 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-211 |
1.32e-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: 90.48 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDT-----RMMFQDARLLPwKT 96
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkhiGYLPQDVELFP-GT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNVGlglkgSWRE--DARQALAAV--------------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:TIGR01842 408 VAENIA-----RFGEnaDPEKIIEAAklagvhelilrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-210 |
1.54e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 90.27 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--EAPNSGDILAGTTPL--STIQDDTR---- 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERagiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 MMFQDARLLPWKTVMDNVGLG----LKGSWREDARQALAAVGL--ENRAGEWPAA-----LSGGQKQRVALARALIHRPG 152
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLlrELQLDADNVTrpvgdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 153 LLLLDEPLGaldALTRIEMQ---DLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:TIGR02633 162 LLILDEPSS---SLTEKETEillDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-210 |
2.36e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKS-TLLRLLAGLEAP----NSGDIL-AGTTPLSTIQDDTR--------MMFQD 88
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRfHGESLLHASEQTLRgvrgnkiaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 --ARLLPWKTVMDNVG--LGL-KGSWREDAR----QALAAVGLEN---RAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK15134 101 pmVSLNPLHTLEKQLYevLSLhRGMRREAARgeilNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-192 |
3.52e-20 |
|
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: 89.22 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDN-TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGttPLSTIQddtrMMFQDARLL 92
Cdd:TIGR03719 7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--PGIKVG----YLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PWKTVMDNVGLGLK----------------------------------------GSWREDARQALAAVGLENRAGEWPAA 132
Cdd:TIGR03719 81 PTKTVRENVEEGVAeikdaldrfneisakyaepdadfdklaaeqaelqeiidaaDAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 133 -LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIETLWQTHGFTVLLVTHD 192
Cdd:TIGR03719 161 kLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-211 |
4.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-EAPNS-----GDILAGTTPLSTI-----QDDTRMMFQDARL 91
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIdaiklRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 92 LPWKTVMDNVGLGLKGSWREDARQ-------ALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREikkiveeCLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 161 GALDALTRIEMQDLIETLwqTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-233 |
5.88e-20 |
|
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: 85.92 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 37 GQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS----TIQDDTRMMFQDarLLPWKTVmdnvGLGLKGSWRED 112
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD--LLSSITK----DFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 113 ARQALAAVGL-ENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTH 191
Cdd:cd03237 99 IAKPLQIEQIlDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1880204416 192 DVSEAVAMADRVLLIeEGKIGLDLTVDIPRPRRVGSAR-LAEL 233
Cdd:cd03237 175 DIIMIDYLADRLIVF-EGEPSVNGVANPPQSLRSGMNRfLKNL 216
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
7.66e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 85.55 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 1 MNTARLNqGTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD 80
Cdd:COG4674 1 MSLDTMH-GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 81 D--TRMM----FQDARLLPWKTVMDNVGLGLKG--------SWREDARQ------ALAAVGLENRAGEWPAALSGGQKQR 140
Cdd:COG4674 80 HeiARLGigrkFQKPTVFEELTVFENLELALKGdrgvfaslFARLTAEErdrieeVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 141 VALARALIHRPGLLLLDEPLGaldALTRIEMQ---DLIETLWQTHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVA---GMTDAETErtaELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-211 |
1.57e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.36 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILA-GTTP----LSTIqddtrmmF 86
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGRVSalleLGAG-------F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 qDARLlpwkTVMDNVGLG--LKGSWREDARQALAAV----GLEnRAGEWPA-ALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1134 100 -HPEL----TGRENIYLNgrLLGLSRKEIDEKFDEIvefaELG-DFIDQPVkTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-211 |
1.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNT-----ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGD-------ILAGTTPLSTIQ 79
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDTR---MMFQDARL-LPWKTVMDNVGLGL--KGSWREDARQA----LAAVGL-ENRAGEWPAALSGGQKQRVALARALI 148
Cdd:PRK13645 87 RLRKeigLVFQFPEYqLFQETIEKDIAFGPvnLGENKQEAYKKvpelLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 149 HRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-192 |
1.91e-19 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 86.91 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 15 NGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRmmfqDArLLPW 94
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR----DA-LDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 95 KTVMDNVGLGLK----GSWREDARQALAAVGL-----ENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:TIGR03719 401 KTVWEEISGGLDiiklGKREIPSRAYVGRFNFkgsdqQKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
170 180
....*....|....*....|....*..
gi 1880204416 166 LTrieMQDLIETLWQTHGfTVLLVTHD 192
Cdd:TIGR03719 477 ET---LRALEEALLNFAG-CAVVISHD 499
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-201 |
1.98e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNS------------GDILAGTTPLSTIQDD 81
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrvegrveffnQNIYERRVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 TRMMFQDARLLPwKTVMDNVGLGLK-GSWRED------ARQALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:PRK14258 90 VSMVHPKPNLFP-MSVYDNVAYGVKiVGWRPKleiddiVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMAD 201
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-211 |
2.51e-19 |
|
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: 86.78 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEA--PNSGDIL-----------------AGT-- 72
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskVGEpc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 73 ---------------TPLSTIQDDTR----MMFQDA-RLLPWKTVMDNV-----GLGLKGSWRED-ARQALAAVGLENRA 126
Cdd:TIGR03269 83 pvcggtlepeevdfwNLSDKLRRRIRkriaIMLQRTfALYGDDTVLDNVlealeEIGYEGKEAVGrAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 127 GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLI 206
Cdd:TIGR03269 163 THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
....*
gi 1880204416 207 EEGKI 211
Cdd:TIGR03269 243 ENGEI 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-211 |
2.54e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 86.93 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRllagleapnsgdILAGTTPLstiqDDTRMMF-QD---A 89
Cdd:PRK11147 6 IHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK------------ILNGEVLL----DDGRIIYeQDlivA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLL--PWK----TVMDNVGLGLK--------------------------------------GSWREDAR--QALAAVGLE 123
Cdd:PRK11147 70 RLQqdPPRnvegTVYDFVAEGIEeqaeylkryhdishlvetdpseknlnelaklqeqldhhNLWQLENRinEVLAQLGLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 124 nraGEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADR 202
Cdd:PRK11147 150 ---PDAAlSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATR 222
|
....*....
gi 1880204416 203 VLLIEEGKI 211
Cdd:PRK11147 223 IVDLDRGKL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-223 |
2.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.83 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSG-------DILAGTTP--LSTIQDDTRMMFQ--DARLLPwK 95
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvddiTITHKTKDkyIRPVRKRIGMVFQfpESQLFE-D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 TVMDNVGLGLKG------SWREDARQALAAVGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13646 102 TVEREIIFGPKNfkmnldEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 169 IEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDIPRPR 223
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI-----VSQTSPK 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-210 |
2.83e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.16 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSgdILAGTTPLSTIQ--------------DDTRMMFQ 87
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG--RIGGSATFNGREilnlpekelnklraEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 D--ARLLPWKTVMDNV--------GLGLKGSWREDARQaLAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK09473 105 DpmTSLNPYMRVGEQLmevlmlhkGMSKAEAFEESVRM-LDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 155 LLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-211 |
5.07e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 25 TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG--------TTPLSTIQDDTR------------- 83
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPYSKkiknfkelrrrvs 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 MMFQDARLLPWKTVMDN------VGLGL-KGSWREDARQALAAVGLENRAGEW-PAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK13631 120 MVFQFPEYQLFKDTIEKdimfgpVALGVkKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-211 |
5.31e-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: 81.71 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGttplstiQDDTRMMFQDAR---------------LLP 93
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEItLDG-------KPVTRRSPRDAIragiayvpedrkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WKTVMDNVGLglkgswredarqalaavglenragewPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD 173
Cdd:cd03215 92 DLSVAENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1880204416 174 LIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03215 146 LIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-211 |
5.74e-19 |
|
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: 86.22 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTR----MMFQDARLLPWKTVMDNVG 102
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqslgMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 103 L--GLKGSWREDARQALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIe 176
Cdd:TIGR01257 1026 FyaQLKGRSWEEAQLEMEAMledtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104
|
170 180 190
....*....|....*....|....*....|....*
gi 1880204416 177 tLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR01257 1105 -LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-191 |
7.56e-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: 81.77 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDD-TRMMFQDARLLPWKT---V 97
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTtlsV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MDNVGLGLKGSWREDARQALAAVGLeNRAGEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriemQDLIE 176
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGL-NGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG----VARFA 165
|
170
....*....|....*...
gi 1880204416 177 TLWQTH---GFTVLLVTH 191
Cdd:cd03231 166 EAMAGHcarGGMVVLTTH 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-212 |
1.15e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.76 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQ-DDTRMMFQDARLLPW---KTVM 98
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAVVSQTPFlfsDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVGLGLKGSWREDARQA--LAAV---------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAlt 167
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVarLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG-- 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1880204416 168 RIEMQDLIETLWQTHGFTVLLVTHDVSeAVAMADRVLLIEEGKIG 212
Cdd:PRK10789 485 RTEHQILHNLRQWGEGRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-211 |
1.24e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKS-----TLLRLLAGLEApNSGDILAGTTPL----------STIQDDTRMMFQdarllPW 94
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVapcalrgrkiATIMQNPRSAFN-----PL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 95 KTVMDNVGLGLK--GSWREDAR--QALAAVGLENRA---GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK10418 96 HTMHTHARETCLalGKPADDATltAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1880204416 168 RIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-211 |
3.83e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS-------TIQDDTRMMFQDARLL 92
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PWKTVMD-NVGLGLKG---SWREDARQ---ALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK13638 90 IFYTDIDsDIAFSLRNlgvPEAEITRRvdeALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 166 LTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13638 170 AGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-211 |
7.62e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 82.53 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LA--------GTTPLSTIQ 79
Cdd:PRK10636 310 NPLLkMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAkgiklgyfAQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDTRMMFQDARLLPWKTvmdnvglglkgswREDARQALAAVGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10636 390 ADESPLQHLARLAPQEL-------------EQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRiemQDLIETLWQTHGFTVlLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10636 457 PTNHLDLDMR---QALTEALIDFEGALV-VVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-213 |
7.84e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 7 NQGTPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI------LAGTTPLSTIQ 79
Cdd:PRK15439 6 TTAPPLLcARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 80 DDTRMMFQDARLLPWKTVMDNVGLGLKGSWREDAR--QALAAVG----LENRAGewpaALSGGQKQRVALARALIHRPGL 153
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKmkQLLAALGcqldLDSSAG----SLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 154 LLLDEPLGaldALTRIEMQDL---IETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 213
Cdd:PRK15439 162 LILDEPTA---SLTPAETERLfsrIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-210 |
8.97e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 11 PLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeAPN---SGDILAGTTPL--STIQDDTR- 83
Cdd:PRK13549 4 YLLeMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRDTERa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 ---MMFQDARLLPWKTVMDNVGLG---LKG---SWRE---DARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRP 151
Cdd:PRK13549 83 giaIIHQELALVKELSVLENIFLGneiTPGgimDYDAmylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 152 GLLLLDEPLGAL-DALTRIEMqDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13549 163 RLLILDEPTASLtESETAVLL-DIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-211 |
1.41e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM------M 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgigyL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDN------VGLGLKGSWRED-ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNlmavlqIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 159 PLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-192 |
2.18e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDN-TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAgtTPLSTIQddtrMMFQDARLL 92
Cdd:PRK11819 9 MNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIKVG----YLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PWKTVMDNVGLGL----------------------------------------KGSWREDARQALAAVGLENRAGEWPAA 132
Cdd:PRK11819 83 PEKTVRENVEEGVaevkaaldrfneiyaayaepdadfdalaaeqgelqeiidaADAWDLDSQLEIAMDALRCPPWDAKVT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 133 -LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIETLWQTHGFTVLLVTHD 192
Cdd:PRK11819 163 kLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-210 |
2.84e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.69 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 9 GTPLLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAG-LEAPN-SGDILA-GTTPLSTIQDDTRMM 85
Cdd:PLN03211 66 GHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILAnNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVG----LGLKGSWRED-----ARQALAAVGL---ENR--AGEWPAALSGGQKQRVALARALIHRP 151
Cdd:PLN03211 146 TQDDILYPHLTVRETLVfcslLRLPKSLTKQekilvAESVISELGLtkcENTiiGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 152 GLLLLDEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAV-AMADRVLLIEEGK 210
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGR 284
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-192 |
3.05e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRmmfqdARLLP 93
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-----AELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WKTVMDNVGlglkgswreDARQALAAVGLEN--------------RAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11147 397 EKTVMDNLA---------EGKQEVMVNGRPRhvlgylqdflfhpkRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 1880204416 160 LGALDaltrIEMQDLIETLWQTHGFTVLLVTHD 192
Cdd:PRK11147 468 TNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-211 |
6.01e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 76.68 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDN--TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL-----AGTTPLSTIQDDTRMMF 86
Cdd:cd03369 9 VENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidISTIPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 87 QDARLLpwktvMDNVGLGLKGSWREDARQALAAVglenRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03369 89 QDPTLF-----SGTIRSNLDPFDEYSDEEIYGAL----RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1880204416 167 TRIEMQDLIETLWQthGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03369 160 TDALIQKTIREEFT--NSTILTIAHRLR-TIIDYDKILVMDAGEV 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-166 |
1.07e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.01 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 15 NGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG-TTPLSTIqDDTRmmfqDArLLP 93
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGeTVKLAYV-DQSR----DA-LDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WKTVMDNVGLGLK----GSWREDARQALAAVGL-----ENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEP----- 159
Cdd:PRK11819 402 NKTVWEEISGGLDiikvGNREIPSRAYVGRFNFkggdqQKKVGV----LSGGERNRLHLAKTLKQGGNVLLLDEPtndld 477
|
170
....*....|.
gi 1880204416 160 ---LGAL-DAL 166
Cdd:PRK11819 478 vetLRALeEAL 488
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-191 |
2.74e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.99 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 21 YGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDIL----AGTTPLSTIQDDTRMMFQDARLLPWKT 96
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNVGLGLKGSWREDARQALAAVGLENRAGEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 175
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*.
gi 1880204416 176 ETlWQTHGFTVLLVTH 191
Cdd:PRK13540 171 QE-HRAKGGAVLLTSH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-211 |
5.40e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 76.98 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 5 RLNQGTPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGlEAPN--SGD-ILAGTTPLS--TI 78
Cdd:PRK10938 253 ALPANEPRIvLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDlTLFGRRRGSgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 79 QDDTR-------MMFQDARL-LPWKTVM-----DNVGLGLKGSWRED--ARQALAAVGLENRAGEWP-AALSGGQkQRVA 142
Cdd:PRK10938 332 WDIKKhigyvssSLHLDYRVsTSVRNVIlsgffDSIGIYQAVSDRQQklAQQWLDILGIDKRTADAPfHSLSWGQ-QRLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 143 L-ARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLL-VTHDVSEAVA-MADRVLLIEEGKI 211
Cdd:PRK10938 411 LiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL-ISEGETQLLfVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-207 |
5.46e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 3 TARLNQGTPLLL-NGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTiQDD 81
Cdd:PRK13543 2 IEPLHTAPPLLAaHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 82 TRMMFQDARLLPWK---TVMDNVGL--GLKGSW-REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK13543 81 SRFMAYLGHLPGLKadlSTLENLHFlcGLHGRRaKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 156 LDEPLGALDALTRIEMQDLIETLWQTHGFTvLLVTHDVSEAVAMADRVLLIE 207
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISAHLRGGGAA-LVTTHGAYAAPPVRTRMLTLE 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-211 |
5.70e-16 |
|
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: 77.29 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLR-LLAGLEAPNSGDILAGTTPL----STIQDDTrmmfqdarllpwkt 96
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKGSVAYvpqqAWIQNDS-------------- 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 VMDNV--GLGLKGSWREDARQALAAV--------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA- 165
Cdd:TIGR00957 715 LRENIlfGKALNEKYYQQVLEACALLpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAh 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 166 LTRIEMQDLIETLWQTHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKI 839
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-222 |
1.11e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 24 NTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAG----LEAPN----SGDILAGTTPLSTIqDDTRM------MFQDA 89
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAI-DAPRLarlravLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 RLLPWKTVMDNVGLG----------LKGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARAL---------IHR 150
Cdd:PRK13547 93 QPAFAFSAREIVLLGrypharragaLTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTV-DIPRP 222
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPaDVLTP 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-209 |
2.23e-15 |
|
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: 72.75 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-----LAGTTPLSTIQDDTRMMFQDARLLPW---KTVM 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWllnATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 DNVGLGLKGSwredaRQALAAV---------------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:cd03290 97 ENITFGSPFN-----KQRYKAVtdacslqpdidllpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 164 DA-LTRIEMQDLIETLWQTHGFTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:cd03290 172 DIhLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-211 |
2.50e-15 |
|
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: 72.17 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN--SGDILAGTTPLSTIQDDTR------ 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERarlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 MMFQDARLLPWKTVMD---NVGLGlkgswredarqalaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03217 81 LAFQYPPEIPGVKNADflrYVNEG----------------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 161 GALD--ALTRIEmqDLIETLwQTHGFTVLLVTH--DVSEAVAmADRVLLIEEGKI 211
Cdd:cd03217 133 SGLDidALRLVA--EVINKL-REEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRI 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-211 |
2.61e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 37 GQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQD--------DTRMMFQD--ARLLPWKTVMDNV----- 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklqalrrDIQFIFQDpyASLDPRQTVGDSImeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 --GLGLKGSWREDARQALAAVGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETL 178
Cdd:PRK10261 430 vhGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190
....*....|....*....|....*....|...
gi 1880204416 179 WQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-210 |
3.00e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKS----TLLRLL--AGLEAPNSGDILA---------GTTPLSTIQD----DTRMMFQD-- 88
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRrrsrqvielSEQSAAQMRHvrgaDMAMIFQEpm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVMDNVGLGLK---GSWRED----ARQALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10261 115 TSLNPVFTVGEQIAESIRlhqGASREEamveAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 159 PLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-194 |
3.53e-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: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 13 LLNGVTKRYGDNtilnALDLH---IPA-GQFVAVVGRSGGGKSTLLRLLAGLEAPNSG---------DIL---AGT---- 72
Cdd:cd03236 2 LEDEPVHRYGPN----SFKLHrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdefRGSelqn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 73 --TPLSTIQDDTRMMFQDARLLPwKTVMDNVGLGLKgswREDARQALAAV----GLENRAGEWPAALSGGQKQRVALARA 146
Cdd:cd03236 78 yfTKLLEGDVKVIVKPQYVDLIP-KAVKGKVGELLK---KKDERGKLDELvdqlELRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 147 LIHRPGLLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVS 194
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLA 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-209 |
3.85e-15 |
|
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: 72.97 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 24 NTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGdilagttplsTIQDDTRMMF--QDARLLPwKTVMDNV 101
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG----------KIKHSGRISFssQFSWIMP-GTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 GLGLkgSWRE-DARQALAAVGLENR-----------AGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:cd03291 119 IFGV--SYDEyRYKSVVKACQLEEDitkfpekdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1880204416 170 EM-QDLIETLWQTHgfTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:cd03291 197 EIfESCVCKLMANK--TRILVTSKM-EHLKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-211 |
5.99e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDdtrmmfqdarllPW---KTVMDNV- 101
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ------------AWimnATVRGNIl 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 ------GLGLKGSWRE---DARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT--RIe 170
Cdd:PTZ00243 743 ffdeedAARLADAVRVsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRV- 821
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1880204416 171 MQDLIetLWQTHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:PTZ00243 822 VEECF--LGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-211 |
7.78e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 37 GQFVAVVGRSGGGKS-TLLRLLAGLEAPnsGDILAGT-----TPLSTIQDDTR---------MMFQDA--RLLPWKTV-- 97
Cdd:PRK11022 33 GEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKlefngQDLQRISEKERrnlvgaevaMIFQDPmtSLNPCYTVgf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 --MDNVGL---GLKGSWREDARQALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:PRK11022 111 qiMEAIKVhqgGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11022 191 QIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-211 |
7.88e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 18 TKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN---SGDILAGTTPLstiqdDTRMM-------FQ 87
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-----DAKEMraisayvQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNV----GLGLKGSWREDARQA-----LAAVGLENRA------GEWPAALSGGQKQRVALARALIHRPG 152
Cdd:TIGR00955 107 DDLFIPTLTVREHLmfqaHLRMPRRVTKKEKRErvdevLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 153 LLLLDEPLGALDALTrieMQDLIETLWQ--THGFTVLLVTHD-VSEAVAMADRVLLIEEGKI 211
Cdd:TIGR00955 187 LLFCDEPTSGLDSFM---AYSVVQVLKGlaQKGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-211 |
1.05e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.00 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI------LAGTTPlstiQDDTRMM 85
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGYYA----QDHAYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWktvMdnvglglkGSWR--EDARQALAAVgL------ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PRK15064 396 ENDLTLFDW---M--------SQWRqeGDDEQAVRGT-LgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 158 EPLGALDaLTRIEmqDLIETLWQTHGfTVLLVTHD---VSeavAMADRVLLIEEGKI 211
Cdd:PRK15064 464 EPTNHMD-MESIE--SLNMALEKYEG-TLIFVSHDrefVS---SLATRIIEITPDGV 513
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-216 |
1.16e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRM---------------MFQDARLlPW 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLarglvylpedrqssgLYLDAPL-AW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 95 KT---VMDNVGLGLKGSwREDAR--QALAAVGLENRAGEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK15439 361 NVcalTHNRRGFWIKPA-RENAVleRYRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1880204416 169 IEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:PRK15439 440 NDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEISGALT 486
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-211 |
1.51e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGlEAPnsgdilagttPLSTIQDDTRMMFQDARLLPW---KTVMD 99
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELS----------HAETSSVVIRGSVAYVPQVSWifnATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 100 NVglgLKGSWREDAR--QALAAVGLEN-----------RAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:PLN03232 698 NI---LFGSDFESERywRAIDVTALQHdldllpgrdltEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 167 TRIEMQD--LIETLwqtHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:PLN03232 775 VAHQVFDscMKDEL---KGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-211 |
1.98e-14 |
|
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: 72.64 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 9 GTPLLLNGVTKRY--GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeAPNSGDI-LAGTTPLSTIQDDTRMM 85
Cdd:TIGR01271 1215 GGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIqIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQdarLLPWKTVMdnvglgLKGSWR-----------EDARQALAAVGLENRAGEWPA-----------ALSGGQKQRVAL 143
Cdd:TIGR01271 1294 FG---VIPQKVFI------FSGTFRknldpyeqwsdEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCL 1364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 144 ARALIHRPGLLLLDEPLGALDALTrieMQDLIETLWQTHG-FTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVT---LQIIRKTLKQSFSnCTVILSEHRV-EALLECQQFLVIEGSSV 1429
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-209 |
2.11e-14 |
|
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: 72.64 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGdilagttplsTIQDDTRMMF--QDARLLPwKTVMDNVGL 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG----------KIKHSGRISFspQTSWIMP-GTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 104 GLkgSWRE-DARQALAAVGLENRAGEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 171
Cdd:TIGR01271 510 GL--SYDEyRYTSVIKACQLEEDIALFPekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*....
gi 1880204416 172 -QDLIETLWQTHgfTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:TIGR01271 588 fESCLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-211 |
2.59e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeAPNSGDILAGTTPLSTIQDDT----RMMF-QDARLLPWKTVMDNV 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElarhRAYLsQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 GLGLKGSWREDARQAL-----AAVGLENRAGEWPAALSGGQKQRVALARAL------IHRPG-LLLLDEPLGALDALTRI 169
Cdd:COG4138 91 ALHQPAGASSEAVEQLlaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINPEGqLLLLDEPMNSLDVAQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 170 EMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4138 171 ALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-203 |
2.65e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 29 ALD---LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN-----------SGDILAgttpLST------IQDDTRMMFQD 88
Cdd:COG4170 22 AVDrvsLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwnGIDLLK----LSPrerrkiIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 AR--LLPWKTVMDNV-----GLGLKGSW-------REDARQALAAVGLEN-----RAgeWPAALSGGQKQRVALARALIH 149
Cdd:COG4170 98 PSscLDPSAKIGDQLieaipSWTFKGKWwqrfkwrKKRAIELLHRVGIKDhkdimNS--YPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 150 RPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRV 203
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-211 |
3.02e-14 |
|
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: 69.21 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 18 TKRYGDN--TILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN---SGDILAGTTPL----STIQDDTRMMFQD 88
Cdd:cd03233 12 TTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkefaEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 ARLLPWKTVmdnvglglkgswredaRQALAAVgLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:cd03233 92 DVHFPTLTV----------------RETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1880204416 169 IEMQDLIETLWQTHGFTVLLVTHDVS-EAVAMADRVLLIEEGKI 211
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQ 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-211 |
4.37e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 30 LDLHipAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTT-PLSTIQD--DTRMMF--QDAR---LLPWKTVMDN 100
Cdd:COG1129 273 FSVR--AGEILGIAGLVGAGRTELARALFGADPADSGEIrLDGKPvRIRSPRDaiRAGIAYvpEDRKgegLVLDLSIREN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 101 VGLGL-----KGSW------REDARQALAAV-----GLENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEP----- 159
Cdd:COG1129 351 ITLASldrlsRGGLldrrreRALAEEYIKRLriktpSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPtrgid 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGAldaltRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1129 427 VGA-----KAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-210 |
8.27e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPL------STIQDDTRMM 85
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVMDNVGLGL---------KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQlphkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 157 DEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-209 |
8.74e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 10 TPLL-LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGT-----TPLSTIQDDT 82
Cdd:PRK09700 3 TPYIsMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItINNInynklDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 RMMFQDARLLPWKTVMDNVGLG---LKGSW----------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGrhlTKKVCgvniidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 150 RPGLLLLDEPlgaLDALTRIEMQDLIETLWQ--THGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:PRK09700 163 DAKVIIMDEP---TSSLTNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-207 |
1.05e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGdNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS-TIQDDTRMMFQDARLLPWK 95
Cdd:PRK15056 14 VTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLVAYVPQSEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 ---TVMDNVGLGLKG--SW--------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK15056 93 fpvLVEDVVMMGRYGhmGWlrrakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1880204416 163 LDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIE 207
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-242 |
1.75e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.99 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 110 REDAR----QALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQThGFT 185
Cdd:NF000106 118 RKDARaradELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880204416 186 VLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRVG-SARLAELEAEVLDRVM 242
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGrTLQIRPAHAAELDRMV 254
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-209 |
1.86e-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: 70.04 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 7 NQGTPLLLNGVTKRYGDNT--ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGD-ILAGTTPLSTIQDdtr 83
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILTNISD--- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 mMFQDARLLPWKTVMDNVGLG---------LKGSWRED----ARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:TIGR01257 2010 -VHQNMGYCPQFDAIDDLLTGrehlylyarLRGVPAEEiekvANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-211 |
3.34e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTI-LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTI-QDDTRMMFQda 89
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFS-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 rllpwkTVMDNVGL--GLKGSWREDARQALAAVGLE------------NRAGEwpAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK10522 401 ------AVFTDFHLfdQLLGPEGKPANPALVEKWLErlkmahkleledGRISN--LKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 156 LDEplGALDA---LTRIEMQDLIETLwQTHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:PRK10522 473 LDE--WAADQdphFRREFYQVLLPLL-QEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
26-191 |
5.41e-13 |
|
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: 68.24 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeAPNSGdilagttPLSTIQDDTRMMFqdarlLPWKTVMDNvglgl 105
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYG-------GRLTKPAKGKLFY-----VPQRPYMTL----- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 106 kGSWRE-------------------DARQALAAVGLEN---RAGEWPAA------LSGGQKQRVALARALIHRPGLLLLD 157
Cdd:TIGR00954 529 -GTLRDqiiypdssedmkrrglsdkDLEQILDNVQLTHileREGGWSAVqdwmdvLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 1880204416 158 EPLGALDaltrIEMQDLIETLWQTHGFTVLLVTH 191
Cdd:TIGR00954 608 ECTSAVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-210 |
6.54e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 36 AGQFVAVVGRSGGGKSTLLRLLAGLeAPNSGDILAGTTPLSTIQDDT----RMMF-QDARLLPWKTVMDNVGLGLKGSWR 110
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarhRAYLsQQQTPPFAMPVFQYLTLHQPDKTR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 111 EDARQAL-----AAVGLENRAGEWPAALSGGQKQRVALARAL--IHRPG-----LLLLDEPLGALDALTRIEMQDLIETL 178
Cdd:PRK03695 100 TEAVASAlnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWPDInpagqLLLLDEPMNSLDVAQQAALDRLLSEL 179
|
170 180 190
....*....|....*....|....*....|..
gi 1880204416 179 WQThGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK03695 180 CQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-247 |
7.59e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.24 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEA--PNSGDI-LAGT--TPLSTiqdDTR------MMFQD-- 88
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSIlLDGEdiLELSP---DERaragifLAFQYpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 89 -------ARLLpwKTVMDNVGLGLKGS--WREDARQALAAVGLE----NR---AGewpaaLSGGQKQRVALARALIHRPG 152
Cdd:COG0396 88 eipgvsvSNFL--RTALNARRGEELSAreFLKLLKEKMKELGLDedflDRyvnEG-----FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 153 LLLLDEPLGALD--ALtRIeMQDLIETLwQTHGFTVLLVTH-----DVSEavamADRVLLIEEGKIgldltVdiprprRV 225
Cdd:COG0396 161 LAILDETDSGLDidAL-RI-VAEGVNKL-RSPDRGILIITHyqrilDYIK----PDFVHVLVDGRI-----V------KS 222
|
250 260
....*....|....*....|...
gi 1880204416 226 GSARLA-ELEAEVLDRVMKRGEA 247
Cdd:COG0396 223 GGKELAlELEEEGYDWLKEEAAA 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-246 |
8.07e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 18 TKRYGDNTiLNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTpLS----TIQDDTRMmfqdarllp 93
Cdd:PRK13409 347 TKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISykpqYIKPDYDG--------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 wkTVMD---NVGLGLKGSW-REDARQALAAVGL-ENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13409 416 --TVEDllrSITDDLGSSYyKSEIIKPLQLERLlDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 169 IEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIG------------------LDLTV----DIPRPR- 223
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFegEPGKHGhasgpmdmregmnrflkeLGITFrrdeETGRPRv 569
|
250 260
....*....|....*....|....*
gi 1880204416 224 -RVGSarlaeleaeVLDRVMK-RGE 246
Cdd:PRK13409 570 nKPGS---------YLDREQKeRGE 585
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
133-211 |
8.66e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 8.66e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-211 |
1.35e-12 |
|
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: 67.28 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTL-LRLLAGLEAPNSGDILAGTT-----------PLSTIQDDTRMMFQ 87
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEGEIIIDGLNiakiglhdlrfKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DAR--LLPWKTVMD-NVGLGLKGSWREDARQALAAvGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR00957 1375 SLRmnLDPFSQYSDeEVWWALELAHLKTFVSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 165 ALTRIEMQDLIETLWQThgFTVLLVTHDVSEAVAMAdRVLLIEEGKI 211
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
18-229 |
1.66e-12 |
|
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: 64.13 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 18 TKRYGDNTILNALDLhIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTPLSTIQDdtrmmfqdarllpwkt 96
Cdd:cd03222 7 VKRYGVFFLLVELGV-VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDeWDGITPVYKPQY---------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 vmdnvglglkgswredarqalaavglenragewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 176
Cdd:cd03222 70 ----------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 177 TLWQTHGFTVLLVTHDVSEAVAMADRVLLIeEGKIGLDLTVDIPRPRRVGSAR 229
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIASQPKGTREGINR 167
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-211 |
4.20e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.49 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRY--GDNTILNALDLHIPAGQFVAVVGRSGGGKSTL----LRLLAgleapNSGDI-LAGTTPLSTIQDDTRMMFQda 89
Cdd:cd03289 8 LTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIqIDGVSWNSVPLQKWRKAFG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 rLLPWK------TVMDNvgLGLKGSWREDARQALA-AVGLENRAGEWPA-----------ALSGGQKQRVALARALIHRP 151
Cdd:cd03289 81 -VIPQKvfifsgTFRKN--LDPYGKWSDEEIWKVAeEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 152 GLLLLDEPLGALDALTrieMQDLIETLWQTH-GFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:cd03289 158 KILLLDEPSAHLDPIT---YQVIRKTLKQAFaDCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-220 |
4.27e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 16 GVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSG------------DIlagttplstiqdDTR 83
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdagDI------------ATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 84 M----MFQDARLLPWKTVMDNVGL-----GL-KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:NF033858 339 RrvgyMSQAFSLYGELTVRQNLELharlfHLpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 154 LLLDEPLGALDALTRiEM--QDLIEtLWQTHGFTVLLVTHDVSEAvAMADRVLLIEEGKIgldLTVDIP 220
Cdd:NF033858 419 LILDEPTSGVDPVAR-DMfwRLLIE-LSREDGVTIFISTHFMNEA-ERCDRISLMHAGRV---LASDTP 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-211 |
4.54e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGD--ILAGTTP----LSTIQDdtrmmfqdarllpwK 95
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvVIRGTVAyvpqVSWIFN--------------A 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 96 TVMDNVglgLKGSWREDAR--QALAAVGLEN-----------RAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PLN03130 694 TVRDNI---LFGSPFDPERyeRAIDVTALQHdldllpggdltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 163 LDALTRIEMQD--LIETLWQThgfTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:PLN03130 771 LDAHVGRQVFDkcIKDELRGK---TRVLVTNQL-HFLSQVDRIILVHEGMI 817
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-216 |
1.01e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 32 LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS--TIQDDTR---MMFQDAR----LLPWKTVMDNV- 101
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIRagiMLCPEDRkaegIIPVHSVADNIn 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 ----------GLGLKGSW-REDARQALAAVGLENRAGEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 169
Cdd:PRK11288 354 isarrhhlraGCLINNRWeAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1880204416 170 EMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:PRK11288 434 EIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-211 |
1.20e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI------LAGTTP-------LSTIQDDtRMmfQDArLLP 93
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrldgedITGLSPrerrrlgVAYIPED-RL--GRG-LVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 94 WKTVMDNVGLGL-------KGSW------REDARQALA-----AVGLENRAGewpaALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG3845 350 DMSVAENLILGRyrrppfsRGGFldrkaiRAFAEELIEefdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 156 LDEP-----LGAldaltriemqdlIETLWQT------HGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG3845 426 AAQPtrgldVGA------------IEFIHQRllelrdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-210 |
1.42e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 12 LLLNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNS--GDIL--AGTTPLSTIQDDTRM--- 84
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILfdGEVCRFKDIRDSEALgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 85 -MFQDARLLPWKTVMDNVGLG----LKG--SWRE---DARQALAAVGLEnragEWPAALSG----GQKQRVALARALIHR 150
Cdd:NF040905 82 iIHQELALIPYLSIAENIFLGneraKRGviDWNEtnrRARELLAKVGLD----ESPDTLVTdigvGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 151 PGLLLLDEPLGAL-----DALTriemqDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:NF040905 158 VKLLILDEPTAALneedsAALL-----DLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-193 |
1.50e-11 |
|
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: 63.65 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDntilnaLDLHIPAGQF-----VAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTT----P--LSTIQDDTRMM 85
Cdd:COG1245 347 LTKSYGG------FSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykPqyISPDYDGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FqdarllpwktVMDNVGLGLKGSW-REDARQALaavGLEN----RAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG1245 421 F----------LRSANTDDFGSSYyKTEIIKPL---GLEKlldkNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190
....*....|....*....|....*....|...
gi 1880204416 161 GALDALTRIEMQDLIETLWQTHGFTVLLVTHDV 193
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-202 |
3.21e-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: 59.69 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 37 GQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTplstiqddtrmmfqdarllpwktvmdnvglglkgswrEDARQA 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------------------------------EDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 117 LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLW-----QTHGFTVLLVTH 191
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkSEKNLTVILTTN 124
|
170
....*....|.
gi 1880204416 192 DVSEAVAMADR 202
Cdd:smart00382 125 DEKDLGPALLR 135
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
131-215 |
3.26e-11 |
|
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: 62.92 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 131 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
....*
gi 1880204416 211 IGLDL 215
Cdd:TIGR02633 481 LKGDF 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
131-215 |
4.53e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 131 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
....*
gi 1880204416 211 IGLDL 215
Cdd:PRK13549 483 LKGDL 487
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-211 |
5.13e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 40 VAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDDTRMMFQDARLLPWKTVMDnvglGLKGSWREDARQALAA 119
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMR----CFPGVPEQKLRAHLGS 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 120 VGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRIEMqdLIETLWQTHGfTVLLVTHDVSEAVA 198
Cdd:PLN03073 614 FGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVEA--LIQGLVLFQG-GVLMVSHDEHLISG 689
|
170
....*....|...
gi 1880204416 199 MADRVLLIEEGKI 211
Cdd:PLN03073 690 SVDELWVVSEGKV 702
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-210 |
7.11e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 14 LNGVTKRYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLS------TIQDDTRMMFQ 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskeALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 88 DARLLPWKTVMDNVGLG---LKGSW------REDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGMFvdqdkmYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1880204416 159 PlgaLDALTRIEMQDL---IETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK10982 161 P---TSSLTEKEVNHLftiIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
64-205 |
7.96e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 64 NSGDILAGTTPLSTIQ-DDTRMMFQDARLLPW---KTVMDNVGLGLKGSWREDARQA--LAAV-----GLENR----AGE 128
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNlKDLRNLFSIVSQEPMlfnMSIYENIKFGKEDATREDVKRAckFAAIdefieSLPNKydtnVGP 1354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 129 WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSeAVAMADRVLL 205
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVV 1430
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-203 |
8.05e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAG------------------------TTPL 75
Cdd:PRK10938 12 RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlsfeqlqklvsdewqrnnTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 76 STIQDDTRmmfqdarllpwKTVMDNVGLGLKgswrEDAR-QALAAV----GLENRAGEWpaaLSGGQKQRVALARALIHR 150
Cdd:PRK10938 92 SPGEDDTG-----------RTTAEIIQDEVK----DPARcEQLAQQfgitALLDRRFKY---LSTGETRKTLLCQALMSE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1880204416 151 PGLLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRV 203
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFA 205
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
32-203 |
1.54e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 32 LHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN---------SGDI-LAGTTPLS---TIQDDTRMMFQDAR--LLPWKT 96
Cdd:PRK15093 28 MTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtadrmrFDDIdLLRLSPRErrkLVGHNVSMIFQEPQscLDPSER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 97 V----MDNV-GLGLKGSWRE-------DARQALAAVGLENRA---GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK15093 108 VgrqlMQNIpGWTYKGRWWQrfgwrkrRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEPTN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1880204416 162 ALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSEAVAMADRV 203
Cdd:PRK15093 188 AMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-209 |
2.33e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.41 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN--SGDILAGTTPL-STIQDDTRMMFQDARLLPWKTVm 98
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLdKNFQRSTGYVEQQDVHSPNLTV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 99 dnvglglkgswredaRQALaavglenRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETL 178
Cdd:cd03232 97 ---------------REAL-------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170 180 190
....*....|....*....|....*....|..
gi 1880204416 179 wQTHGFTVLLVTHDVSEAV-AMADRVLLIEEG 209
Cdd:cd03232 155 -ADSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-226 |
8.21e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNTIlnAL-DLHIP-AGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI------------LAGTTplstIQDdtrmM 85
Cdd:COG1245 82 RYGENGF--RLyGLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrFRGTE----LQD----Y 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 86 FQDARLLPWKTVM-----DNVGLGLKGSWRE-----DARQALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRP 151
Cdd:COG1245 152 FKKLANGEIKVAHkpqyvDLIPKVFKGTVREllekvDERGKLDELaeklGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 152 GLLLLDEPLGALDALTRIEMQDLIETLWQThGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLdltVDIPRPRRVG 226
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILygEPGVYGV---VSKPKSVRVG 304
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-209 |
1.49e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 5 RLNQGTPLLLNGVTKRygdntilnaldlhIPAGQFVAVVGRSGGGKSTLL----RLL---AGLEAPNSGDIlaGTTPLST 77
Cdd:PTZ00243 1317 RYREGLPLVLRGVSFR-------------IAPREKVGIVGRTGSGKSTLLltfmRMVevcGGEIRVNGREI--GAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 78 IQDDTRMMFQDARLLPwKTVMDNVGLGLKGS----W--------REdaRQALAAVGLENRAGEWPAALSGGQKQRVALAR 145
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFD-GTVRQNVDPFLEASsaevWaalelvglRE--RVASESEGIDSRVLEGGSNYSVGQRQLMCMAR 1458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880204416 146 ALIHR-PGLLLLDEPLGALD-ALTRiEMQDLIETLWQTHgfTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:PTZ00243 1459 ALLKKgSGFILMDEATANIDpALDR-QIQATVMSAFSAY--TVITIAHRL-HTVAQYDKIIVMDHG 1520
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-211 |
2.43e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAG-LEAPNSGDILAGTTPLSTIQDDTRMMFQDA--------- 89
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPGNWQLAWVNQETPALPQPAleyvidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 90 --RLLPWKTVMDNV------------GLGLKGSWREDARQA--LAAVGLENRAGEWP-AALSGGQKQRVALARALIHRPG 152
Cdd:PRK10636 90 eyRQLEAQLHDANErndghaiatihgKLDAIDAWTIRSRAAslLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 153 LLLLDEPLGALDALTRIemqdLIETLWQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVI----WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-211 |
2.70e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTplstiqDDTRMMFQDAR----LLPWKTVM--D 99
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC------DVAKFGLTDLRrvlsIIPQSPVLfsG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 100 NVGLGLK--------GSWREDARQALAAV------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PLN03232 1325 TVRFNIDpfsehndaDLWEALERAHIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1880204416 166 LTRIEMQDLIETLWQThgFTVLLVTHDVSEAVAmADRVLLIEEGKI 211
Cdd:PLN03232 1405 RTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-207 |
3.19e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.31 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 39 FVAVVGRSGGGKSTLLrllaglEAPNSGdiLAGTTPLSTIQDDtrmmfQDARLLPWKTVMDNVGLGLKGSWRED--ARQA 116
Cdd:cd03240 24 LTLIVGQNGAGKTTII------EALKYA--LTGELPPNSKGGA-----HDPKLIREGEVRAQVKLAFENANGKKytITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 117 LAAvgLEN----RAGE--WPAA-----LSGGQKQ------RVALARALIHRPGLLLLDEPLGALDAlTRIEMQ--DLIET 177
Cdd:cd03240 91 LAI--LENvifcHQGEsnWPLLdmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE-ENIEESlaEIIEE 167
|
170 180 190
....*....|....*....|....*....|
gi 1880204416 178 LWQTHGFTVLLVTHDvSEAVAMADRVLLIE 207
Cdd:cd03240 168 RKSQKNFQLIVITHD-EELVDAADHIYRVE 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-226 |
4.16e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 17 VTKRYGDNTIlnAL-DLHIP-AGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGD---------IL---AGTTplstIQDdt 82
Cdd:PRK13409 79 PVHRYGVNGF--KLyGLPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrfRGTE----LQN-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 83 rmMFQDAR--------------LLPwKTVMDNVGLGLKgswREDARQALAAV----GLENRAGEWPAALSGGQKQRVALA 144
Cdd:PRK13409 151 --YFKKLYngeikvvhkpqyvdLIP-KVFKGKVRELLK---KVDERGKLDEVverlGLENILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 145 RALIHRPGLLLLDEPLGALDALTRIEMQDLIETLwqTHGFTVLLVTHDVseAV--AMADRVLLI--EEGKIGLdltVDIP 220
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDL--AVldYLADNVHIAygEPGAYGV---VSKP 297
|
....*.
gi 1880204416 221 RPRRVG 226
Cdd:PRK13409 298 KGVRVG 303
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-211 |
4.64e-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: 55.30 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 20 RYGDN--TILNALDLHIPAGQFVAVVGRSGGGKSTL----LRLLAGLEAPNSGD-ILAGTTPLSTIQDDTRMMFQDARLL 92
Cdd:cd03288 28 RYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFDGKIVIDgIDISKLPLHTLRSRLSIILQDPILF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 93 PwKTVMDNVGLGLKGSwreDAR--QALAAVGLENRAGEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03288 108 S-GSIRFNLDPECKCT---DDRlwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQTHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03288 184 TASIDMATENILQKVVMTAFADR--TVVTIAHRVS-TILDADLVLVLSRGIL 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-194 |
5.22e-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: 54.25 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLrlLAGLEAPNSGDILAGTTPLStiqddtrmmfqdarllPWKTVMdnvglglk 106
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISFLPKFS----------------RNKLIF-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 107 gswrEDARQALAAVGLEN-RAGEWPAALSGGQKQRVALARALIHRPG--LLLLDEPLGALDALTRIEMQDLIETLWQThG 183
Cdd:cd03238 65 ----IDQLQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-G 139
|
170
....*....|.
gi 1880204416 184 FTVLLVTHDVS 194
Cdd:cd03238 140 NTVILIEHNLD 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-164 |
9.33e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 37 GQFVAVVGRSGGGKSTLLRLLAgLEA----PNSGDIL--------AGTTPLSTIQDD----TRMMFQDARL------LPW 94
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMA-MHAidgiPKNCQILhveqevvgDDTTALQCVLNTdierTQLLEEEAQLvaqqreLEF 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 95 KTVMDNVGLGLKGSWREDA-----------RQALAAVGLENRAGEWPAALS--------------GGQKQRVALARALIH 149
Cdd:PLN03073 282 ETETGKGKGANKDGVDKDAvsqrleeiykrLELIDAYTAEARAASILAGLSftpemqvkatktfsGGWRMRIALARALFI 361
|
170
....*....|....*
gi 1880204416 150 RPGLLLLDEPLGALD 164
Cdd:PLN03073 362 EPDLLLLDEPTNHLD 376
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-219 |
1.13e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 123 ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQTHGFTVLLVTHDVSeAVAMADR 202
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANT 648
|
90
....*....|....*..
gi 1880204416 203 VLLIEEGKIGLDLTVDI 219
Cdd:PTZ00265 649 IFVLSNRERGSTVDVDI 665
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-216 |
1.18e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 2 NTARLNQGTPLLLNGVTKRygDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI------LAGTTPL 75
Cdd:PRK09700 256 NVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdISPRSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 76 STIQDDTRMMFQDAR---LLPWKTVMDNVGL-------GLKGSW-----------REDARQALA--AVGLENRAGEwpaa 132
Cdd:PRK09700 334 DAVKKGMAYITESRRdngFFPNFSIAQNMAIsrslkdgGYKGAMglfhevdeqrtAENQRELLAlkCHSVNQNITE---- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
....
gi 1880204416 213 LDLT 216
Cdd:PRK09700 489 QILT 492
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-209 |
3.82e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAP---NSGDILAGTTPL-STIQDDTRMMFQDARLLPWKTV 97
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLdSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 98 MD------------NVGLGLKGSWREDARQAL-------AAVGLenrAGEwpaALSGGQKQRVALARALIHRPGLLL-LD 157
Cdd:TIGR00956 854 REslrfsaylrqpkSVSKSEKMEYVEEVIKLLemesyadAVVGV---PGE---GLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1880204416 158 EPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSeAVAMA--DRVLLIEEG 209
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPS-AILFEefDRLLLLQKG 979
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-211 |
3.66e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTplstiqDDTRMMFQDAR----LLPWKTVMdnv 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGC------DISKFGLMDLRkvlgIIPQAPVL--- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 glgLKGSWR---------EDA-------RQALAAV------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PLN03130 1325 ---FSGTVRfnldpfnehNDAdlwesleRAHLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1880204416 160 LGALDALTRIEMQDLIETLWQThgFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLN-TIIDCDRILVLDAGRV 1450
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-69 |
6.00e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 6.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1880204416 22 GDNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPN--SGDIL 69
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDIL 67
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-204 |
9.22e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 29 ALDLHIPAGQFVAVVGRSGGGKSTLLR---LLAGLEAPN---SGDILAGttplstiqddtrmmfqdarllpwktvmDNVG 102
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSAtrrRSGVKAG---------------------------CIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 103 LglkgswrEDARQALAAVGLenragewpaalSGGQKQRVALARALIH----RPGLLLLDEPLGALDALTRIEMQDLIETL 178
Cdd:cd03227 66 A-------VSAELIFTRLQL-----------SGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEH 127
|
170 180
....*....|....*....|....*.
gi 1880204416 179 WQtHGFTVLLVTHDvSEAVAMADRVL 204
Cdd:cd03227 128 LV-KGAQVIVITHL-PELAELADKLI 151
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-211 |
1.57e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTPLSTIQDDTRMMFQDARLLPWKTVMdnvgLGL 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAALIAISSGLNGQLTGIENIELKGLM----MGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 106 -KGSWREDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD-ALTRIEMQDLIEtlWQTHG 183
Cdd:PRK13545 116 tKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDKMNE--FKEQG 193
|
170 180
....*....|....*....|....*...
gi 1880204416 184 FTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13545 194 KTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
132-211 |
1.68e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 132 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQtHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-191 |
3.14e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAGTTPLSTIQDdtrmmfqdarllPWKT-VMDNV 101
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK------------PYCTyIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 102 GLGLKGS-------WRE---DARQALAAV---GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13541 80 GLKLEMTvfenlkfWSEiynSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180
....*....|....*....|...
gi 1880204416 169 IEMQDLIeTLWQTHGFTVLLVTH 191
Cdd:PRK13541 160 DLLNNLI-VMKANSGGIVLLSSH 181
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
27-204 |
4.78e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLL----------RLLAGLEAPNSGDILAGT----------------TPLST--- 77
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRIEGLehidkvividqspigrTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 78 ---IQDDTRMMFQD----ARLLP--------WKTVMDNVGLGLkgswrEDAR-------------QALAAVGLEN-RAGE 128
Cdd:cd03271 91 ytgVFDEIRELFCEvckgKRYNRetlevrykGKSIADVLDMTV-----EEALeffenipkiarklQTLCDVGLGYiKLGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 129 WPAALSGGQKQRVALARALIHR---PGLLLLDEPLGAL---DALTRIE-MQDLIETlwqthGFTVLLVTHDVsEAVAMAD 201
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEvLQRLVDK-----GNTVVVIEHNL-DVIKCAD 239
|
...
gi 1880204416 202 RVL 204
Cdd:cd03271 240 WII 242
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
27-203 |
5.30e-06 |
|
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: 46.10 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLL---------------------RLLAGLEAPNSGDI------------LAGTT 73
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIeglspaiaidqkTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 74 PLST------IQDDTRMMFQDARLLPWKTVMDNVGLGLkgswredarqalaaVGLENRAGewpaALSGGQKQRVALARAL 147
Cdd:cd03270 91 PRSTvgtvteIYDYLRLLFARVGIRERLGFLVDVGLGY--------------LTLSRSAP----TLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880204416 148 IHR-PGLL-LLDEP-LGaldaLTRIEMQDLIETL--WQTHGFTVLLVTHDvSEAVAMADRV 203
Cdd:cd03270 153 GSGlTGVLyVLDEPsIG----LHPRDNDRLIETLkrLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
132-212 |
9.88e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 132 ALSGGQKQ------RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE-TLWQTHGF-TVLLVTHDvSEAVAMADrv 203
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIpQVIMISHH-RELLSVAD-- 877
|
....*....
gi 1880204416 204 LLIEEGKIG 212
Cdd:PRK01156 878 VAYEVKKSS 886
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
30-54 |
1.12e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 1.12e-04
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
26-192 |
1.56e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 41.58 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 26 ILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEAPNSGDILAgttplstIQDDTRMMFQDARLLPWKTVMDNVGL-- 103
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIG-------LRGDALPLGANSFILPGLTGEENARMma 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 104 ---GLKGSwrEDARQALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLWQ 180
Cdd:PRK15177 75 slyGLDGD--EFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQ 152
|
170
....*....|..
gi 1880204416 181 THGFTVLlvTHD 192
Cdd:PRK15177 153 QKGLIVL--THN 162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-209 |
1.57e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 131 AALSGGQKQRVALARaliHRPGLL-----LLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDvSEAVAMADRVLL 205
Cdd:PRK00635 475 ATLSGGEQERTALAK---HLGAELigityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADRIID 549
|
....
gi 1880204416 206 IEEG 209
Cdd:PRK00635 550 IGPG 553
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-209 |
2.56e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 37 GQFVAVVGRSGGGKSTLLRLLAGLEAPN--SGDI--------------LAGT-------TPLSTIQD------------- 80
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIrisgfpkkqetfarISGYceqndihSPQVTVREsliysaflrlpke 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 81 ---DTRMMFQDarllpwkTVMDNVGLglkgswrEDARQALaaVGLENRAGewpaaLSGGQKQRVALARALIHRPGLLLLD 157
Cdd:PLN03140 986 vskEEKMMFVD-------EVMELVEL-------DNLKDAI--VGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1880204416 158 EPLGALDA-LTRIEMQDLIETLwqTHGFTVLLVTH----DVSEAVamaDRVLLIEEG 209
Cdd:PLN03140 1045 EPTSGLDArAAAIVMRTVRNTV--DTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
117-206 |
3.78e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 117 LAAVGLE----NRAGEwpaALSGGQKQRVALAR----ALIhrpGLL-LLDEP-LGaldaLTRIEMQDLIETL--WQTHGF 184
Cdd:TIGR00630 472 LIDVGLDylslSRAAG---TLSGGEAQRIRLATqigsGLT---GVLyVLDEPsIG----LHQRDNRRLINTLkrLRDLGN 541
|
90 100
....*....|....*....|..
gi 1880204416 185 TVLLVTHDvSEAVAMADRVLLI 206
Cdd:TIGR00630 542 TLIVVEHD-EDTIRAADYVIDI 562
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-61 |
4.44e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 4.44e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1880204416 23 DNTILNALDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE 61
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE 51
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-212 |
4.76e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 115 QALAAVGLENRA-GEWPAALSGGQKQRVALARALIH---RPGLLLLDEPLGALDALtriEMQDLIETLWQ-TH-GFTVLL 188
Cdd:PRK00635 791 HALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTH---DIKALIYVLQSlTHqGHTVVI 867
|
90 100
....*....|....*....|....*.
gi 1880204416 189 VTHDVsEAVAMADRVLLI--EEGKIG 212
Cdd:PRK00635 868 IEHNM-HVVKVADYVLELgpEGGNLG 892
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-211 |
1.02e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880204416 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIETLwQTHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-164 |
1.07e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 43 VGRSGGGKSTLLRLLAGLEAPNSGDI-LAGTTPLSTIQDDtRMMFQDARllpwktVMDNVGLGLKGSWR----EDARQAL 117
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQD-QFAFEEFT------VLDTVIMGHTELWEvkqeRDRIYAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 118 A--------AVG-------------LENRAGEW------P--------AALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK15064 106 PemseedgmKVAdlevkfaemdgytAEARAGELllgvgiPeeqhyglmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
..
gi 1880204416 163 LD 164
Cdd:PRK15064 186 LD 187
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
27-53 |
1.28e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 1.28e-03
10 20
....*....|....*....|....*..
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTL 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
27-54 |
2.05e-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: 39.23 E-value: 2.05e-03
10 20
....*....|....*....|....*...
gi 1880204416 27 LNALDLHIPAGQFVAVVGRSGGGKSTLL 54
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
115-159 |
6.12e-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: 6.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1880204416 115 QALAAVGLEN-RAGEWPAALSGGQKQRVALARALIHR---PGLLLLDEP 159
Cdd:TIGR00630 811 QTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEP 859
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
115-201 |
6.25e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880204416 115 QALAAVGLEN-RAGEwPAA-LSGGQKQRVALARALIHRPG---LLLLDEP------------LGALdaltriemQDLIEt 177
Cdd:COG0178 808 QTLQDVGLGYiKLGQ-PATtLSGGEAQRVKLASELSKRSTgktLYILDEPttglhfhdirklLEVL--------HRLVD- 877
|
90 100
....*....|....*....|....*.
gi 1880204416 178 lwqtHGFTVLLVTH--DVseaVAMAD 201
Cdd:COG0178 878 ----KGNTVVVIEHnlDV---IKTAD 896
|
|
| |
