|
Name |
Accession |
Description |
Interval |
E-value |
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-255 |
2.47e-175 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 482.64 E-value: 2.47e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 1 MNTARLNQGTPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQE 80
Cdd:PRK11247 2 MNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 81 DTRMMFQDARLLPWKSVIDNVGLGLKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRLGSVRLAELEAEVLQR 240
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPRPRRRGSARLAELEAEVLQR 241
|
250
....*....|....*.
gi 447013267 241 VMQRGESE-TRLRKQG 255
Cdd:PRK11247 242 VMSRGESEpTRLRWAG 257
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-248 |
2.78e-105 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 305.48 E-value: 2.78e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKN----IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMFQ 87
Cdd:COG1116 8 LELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGLKGQWRDAARRALA------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG1116 88 EPALLPWLTVLDNVALGLELRGVPKAERRERarelleLVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDIPRPRR---LGSVRLAELEAE 236
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVDLPRPRDrelRTSPEFAALRAE 247
|
250
....*....|..
gi 447013267 237 VLQRVMQRGESE 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 |
2.53e-93 |
|
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: 273.58 E-value: 2.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKN----IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMFQ 87
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGLKGQWRDAARRALA------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERaeelleLVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEE--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 |
1.31e-80 |
|
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: 241.27 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI---QEDTRMMFQD 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03259 81 YALFPHLTVAENIAFGLKlrgvpkAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-211 |
1.13e-70 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 220.74 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI---QEDTRMMFQD 88
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRGVPKAEIRArvaellELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 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 |
2.61e-70 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 213.59 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLA-------EIQEDTRM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQDARLLPWKSVIDNVGLGLkgqwrdaarralaavglenragewpaalSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 165 ALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-211 |
9.95e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 191.02 E-value: 9.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHY----AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR- 83
Cdd:COG1136 2 SPLLeLRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 --------MMFQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:COG1136 82 rlrrrhigFVFQFFNLLPELTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 150 RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 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 |
1.26e-60 |
|
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: 190.91 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQDAR 90
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpvnTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03300 83 LFPHLTVFENIAFGLRLKKLPKAEIKErvaealDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447013267 165 ALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-211 |
2.87e-60 |
|
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: 189.62 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI----VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---- 83
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 -----MMFQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:cd03255 81 rrhigFVFQSFNLLPDLTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-223 |
4.29e-60 |
|
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: 189.60 E-value: 4.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMFQDARLLPWKSVIDNVGLGL- 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 106 -------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSL 178
Cdd:TIGR01184 81 rvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 179 WQEHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTVDIPRPR 223
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVPFPRPR 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-211 |
3.74e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 191.05 E-value: 3.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQD 88
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRniaMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG3839 84 YALYPHMTVYENIAFPLklrkvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-248 |
9.11e-59 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 186.99 E-value: 9.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI----VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMFQ 87
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLrlrgvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRL---GSVR-------LA 231
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRRFlagEDARaiksdpaFI 243
|
250
....*....|....*..
gi 447013267 232 ELEAEVLQRVMQRGESE 248
Cdd:COG4525 244 ALREELLDIIFAQEEAE 260
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-211 |
1.39e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.19 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTplAEIQEDTR-----MM 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvLNGRD--LFTNLPPRerrvgFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRArveellELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447013267 160 LGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-218 |
1.58e-54 |
|
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: 175.38 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR--------MM 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlrrrmgML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLrehtrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-211 |
1.88e-54 |
|
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: 175.55 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR--------MMFQD 88
Cdd:COG1127 11 LTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrrrigMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAARRAL-------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG1127 91 GALFDSLTVFENVAFPLREHTDLSEAEIRelvleklELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1127 171 GLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-211 |
4.38e-54 |
|
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: 173.59 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG---TTPLAEIQEDTRMMFQD 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAA------RRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDeidervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-211 |
4.97e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 173.70 E-value: 4.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR--------MMFQ 87
Cdd:COG2884 7 VSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrrigVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG2884 87 DFRLLPDRTVYENVALPLrvtgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG2884 167 NLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-211 |
6.54e-54 |
|
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: 173.10 E-value: 6.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-------AGTTPLAEIQEDTRMMFQDA 89
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltDDKKNINELRQKVGMVFQQF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03262 86 NLFPHLTVLENITLAPikvkgmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-218 |
9.55e-54 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 173.40 E-value: 9.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVlnQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQD 88
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvsMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGL-------KGQWRDAARRALAaVGLENRAGEWPAALSGGQKQRVALARALI-HRPgLLLLDEPL 160
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLrpglkltAEQRAQVEQALER-VGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
12-211 |
3.59e-53 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 175.61 E-value: 3.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG---TTPLAEIQEDTRMMFQD 88
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGgrdITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAErvaellDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-211 |
2.08e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.37 E-value: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 1 MNTARLNQGTPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG--TTPLA 76
Cdd:PRK09452 3 KLNKQPSSLSPLVeLRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImLDGqdITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 77 EIQEDTRMMFQDARLLPWKSVIDNVGLGLKGQWRDAA------RRALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:PRK09452 83 AENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAeitprvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-211 |
6.97e-52 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 172.21 E-value: 6.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL---AGTTPLAEIQEDTRMMFQD 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFidgEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQrvkealELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-218 |
9.66e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 9.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDTRM---MFQDA 89
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGEDVARDPAEVRRRigyVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPWKSVIDNVGL--GLKG----QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG1131 83 ALYPDLTVRENLRFfaRLYGlprkEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 164 DALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG1131 163 DPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-211 |
2.49e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 167.48 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG-------DVLAGTTPLAEIQEDTRMMF 86
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtitvdgeDLTDSKKDINKLRRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1126 84 QQFNLFPHLTVLENVTLAPikvkkmsKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 160 LGALD-ALTRlEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1126 164 TSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-211 |
5.69e-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: 164.11 E-value: 5.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRM----MFQDA 89
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrigyLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPWKSVIDNVglglkgqwrdaarralaavglenragewpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03230 83 SLYENLTVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03230 133 EFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-209 |
3.35e-50 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 164.87 E-value: 3.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMFQDARL 91
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 LPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK11248 82 LPWRNVQDNVAFGLqlagveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447013267 166 LTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-211 |
8.37e-50 |
|
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: 163.37 E-value: 8.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKN----IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---- 83
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 -----MMFQDARLLPWKSVIDNVGLGL----KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG4181 89 arhvgFVFQSFQLLPTLTALENVMLPLelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 155 LLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRL 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-218 |
2.86e-49 |
|
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: 162.28 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAK----NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQE-----DTRMMFQ 87
Cdd:COG1124 7 LSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafrrRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DAR--LLPWKSVIDNVGLGLK----GQWRDAARRALAAVGLENR-AGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG1124 87 DPYasLHPRHTVDRILAEPLRihglPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG1124 167 SALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-211 |
7.60e-49 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 160.97 E-value: 7.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQDARLLP 93
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERnvgFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKSVIDNVGLGLKGQWRDAARRALA----------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:cd03296 88 HMTVFDNVAFGLRVKPRSERPPEAEirakvhellkLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 164 DALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
14-233 |
3.10e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 159.84 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYA-KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL--------AGTTPLAEIQEDTRM 84
Cdd:COG3638 5 LRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtaLRGRALRRLRRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQDARLLPWKSVIDNVGLGLKGQWRDAARRALA--------------AVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:COG3638 85 IFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLfppedreralealeRVGLADKAYQRADQLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 151 PGLLLLDEPLGALD-ALTRLEMqDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTvdiprPRRLGSVR 229
Cdd:COG3638 165 PKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGP-----PAELTDAV 238
|
....
gi 447013267 230 LAEL 233
Cdd:COG3638 239 LREI 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-211 |
3.34e-48 |
|
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: 159.28 E-value: 3.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYA----KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR------ 83
Cdd:cd03258 4 LKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkarrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 --MMFQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:cd03258 84 igMIFQHFNLLSSRTVFENVALPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-223 |
3.70e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 159.49 E-value: 3.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD-------VLAGTTPLAEIQEDTRMMFQDA 89
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdglkVNDPKVDERLIRQEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPWKSVIDNVGLG-------LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK09493 87 YLFPHLTALENVMFGplrvrgaSKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 163 LDALTRLE----MQDLivslwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD-----LTVDIPRPR 223
Cdd:PRK09493 167 LDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDgdpqvLIKNPPSQR 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-211 |
6.99e-48 |
|
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: 165.46 E-value: 6.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 8 QGTPLL-LNAVSKHYAKNI-----VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL--------AGTT 73
Cdd:COG1123 256 AAEPLLeVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltkLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 74 PLAEIQEDTRMMFQD--ARLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGLENRAGEW-PAALSGGQKQRVAL 143
Cdd:COG1123 336 SLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLrlhgllsRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 144 ARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-210 |
1.44e-47 |
|
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: 156.86 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-----AGTTPLAEIQEDTRMMF 86
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARL-LPWKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03225 82 QNPDDqFFGPTVEEEVAFGLEnlglpeEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 160 LGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-210 |
1.51e-47 |
|
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: 155.23 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR-----MMF 86
Cdd:cd03228 3 FKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniaYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLPwKSVIDNVglglkgqwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03228 83 QDPFLFS-GTIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447013267 167 TRLEMQDLIVSLwqEHGFTVLLVTHDVSeAVAMADRVLLIEEGK 210
Cdd:cd03228 131 TEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-211 |
2.41e-47 |
|
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: 156.72 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG-----TTPLAEIQEDTRMMFQ 87
Cdd:COG1122 3 LENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkditKKNLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DAR---LLPwkSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1122 83 NPDdqlFAP--TVEEDVAFGPENLGLPREEIRErveealELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-211 |
3.07e-47 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 156.88 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQD 88
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRkigFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKArveellELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-211 |
9.95e-47 |
|
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: 156.65 E-value: 9.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI---------QEDTRMMFQDARLLPWKSV 97
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 IDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:cd03294 120 LENVAFGLevqgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447013267 172 QDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
1.06e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 158.32 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKN----IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQE----DTR-- 83
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelrAARrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 --MMFQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG1135 84 igMIFQHFNLLSSRTVAENVALPLeiagvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-211 |
2.84e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 157.55 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQDAR 90
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRkvgFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLGLK----------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTvlprrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-211 |
8.15e-46 |
|
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: 152.66 E-value: 8.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNI----VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL----AGTTPLAEIQEDTR----M 84
Cdd:cd03257 7 LSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkDLLKLSRRLRKIRRkeiqM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQDAR--LLPWKSVIDNVG------LGLKGQWRDAARRALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:cd03257 87 VFQDPMssLNPRMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 154 LLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-211 |
8.22e-46 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 152.26 E-value: 8.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQDARLLPWKSVIDNVGLG-- 104
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpvsMLFQENNLFAHLTVEQNVGLGls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 105 ----LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQ 180
Cdd:cd03298 97 pglkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|.
gi 447013267 181 EHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-211 |
8.84e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 155.25 E-value: 8.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYA-KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDT--RMM---FQ 87
Cdd:COG1125 4 FENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIgyvIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGL--GLKGqWRDAARRALAA-----VGLENR--AGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1125 84 QIGLFPHMTVAENIATvpRLLG-WDKERIRARVDellelVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-211 |
9.43e-46 |
|
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: 152.45 E-value: 9.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 29 QLDLHIPaGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRM---------MFQDARLLPWKSVID 99
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrkiglVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NVGLGLKGQWRDAARRA----LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLI 175
Cdd:cd03297 95 NLAFGLKRKRNREDRISvdelLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 447013267 176 VSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
17-210 |
2.63e-45 |
|
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: 151.25 E-value: 2.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED--------TRMMFQ 87
Cdd:TIGR02673 7 VSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlpllrrrIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGL-----GLKGQ-WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR02673 87 DFRLLPDRTVYENVALplevrGKKEReIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 162 ALDALTRLEMQDLIVSLWQeHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:TIGR02673 167 NLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-211 |
2.87e-45 |
|
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: 155.26 E-value: 2.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 29 QLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLaeiQEDTR------------MMFQDARLLPWKS 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL---QDSARgiflpphrrrigYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVGLGLKGQWRDAARRALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 173 DLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-211 |
4.97e-45 |
|
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: 151.30 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKN-IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ--EDTRMM---FQDAR 90
Cdd:cd03295 6 VTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpvELRRKIgyvIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLGLKGQ-WRDAARRA-----LAAVGLE--NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03295 86 LFPHMTVEENIALVPKLLkWPKEKIREradelLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-211 |
5.82e-45 |
|
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: 153.42 E-value: 5.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 42 VVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQDARLLPWKSVIDNVGLGLKGQWRDAA----- 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhinMVFQSYALFPHMTVEENVAFGLKMRKVPRAeikpr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 114 -RRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHD 192
Cdd:TIGR01187 81 vLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*....
gi 447013267 193 VSEAVAMADRVLLIEEGKI 211
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKI 179
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-210 |
6.14e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.99 E-value: 6.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI---QEDTRMM 85
Cdd:PRK11607 17 TPLLeIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKqdklpkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 160 LGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-211 |
2.24e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.43 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTRMM----F 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQvayvP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLPwKSVIDNVGLGLKGQWRDAARRALAA----VGLENRAGEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQLRERKFDRERALEllerLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-241 |
1.51e-43 |
|
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: 147.31 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR----MMFQDARLL 92
Cdd:COG4555 7 LSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqigVLPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PWKSVIDNVGL--GLKGQWRDAARRALAAV----GLEN----RAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:COG4555 87 DRLTVRENIRYfaELYGLFDEELKKRIEELiellGLEEfldrRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRlgsvRLAELEAEVLQRV 241
Cdd:COG4555 163 LDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI----GEENLEDAFVALI 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-214 |
3.19e-43 |
|
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: 146.56 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKN-IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQE--------DTRM 84
Cdd:cd03256 3 VENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlrrQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQDARLLPWKSVIDNVGLGLKGQWRDAARRALA--------------AVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLfpkeekqralaaleRVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
39-211 |
4.67e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 150.25 E-value: 4.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 39 FVaVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDT----R-----MMFQDARLLPWKSVIDNVGLGL---- 105
Cdd:COG4175 56 FV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelRrkkmsMVFQHFALLPHRTVLENVAFGLeiqg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 106 --KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHG 183
Cdd:COG4175 135 vpKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLK 214
|
170 180
....*....|....*....|....*...
gi 447013267 184 FTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4175 215 KTIVFITHDLDEALRLGDRIAIMKDGRI 242
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-210 |
4.74e-43 |
|
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: 143.54 E-value: 4.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIqedtrmmfqdaRLLPWKS 96
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-----------PLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIdnvglGLKGQwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIV 176
Cdd:cd00267 74 RI-----GYVPQ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|....
gi 447013267 177 SLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:cd00267 125 EL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
26-246 |
5.17e-43 |
|
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: 152.36 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTA---GDVLAGTTPLAEIQEDTR-----MMFQD--ARLLPWk 95
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgrrigMVFQDpmTQLNPV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:COG1123 100 TVGDQIAEALenlglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 170 EMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD--IPRPRRLGSVRLAELEAEVLQRVMQRGE 246
Cdd:COG1123 180 EILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEeiLAAPQALAAVPRLGAARGRAAPAAAAAE 258
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-211 |
9.51e-43 |
|
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: 145.57 E-value: 9.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR-----MMFQD 88
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarriaYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGL---KGQWRDAARRALAAV-------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG1120 84 PPAPFGLTVRELVALGRyphLGLFGRPSAEDREAVeealertGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-211 |
1.27e-42 |
|
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: 144.09 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIV-LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE--------IQEDTRMMFQ 87
Cdd:cd03292 6 VTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraipyLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEvtgvppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03292 166 NLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-225 |
1.47e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.85 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTP------------LAEIQE 80
Cdd:COG1121 9 LENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPrrarrrigyvpqRAEVDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 81 DTRMmfqdarllpwkSVIDNVGLGLKGQWRDAARRALA----------AVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:COG1121 89 DFPI-----------TVRDVVLMGRYGRRGLFRRPSRAdreavdealeRVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRL 225
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-211 |
2.57e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 147.87 E-value: 2.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQDAR 90
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERgvgMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:PRK11000 86 LYPHLSVAENMSFGLKlagakkEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447013267 165 ALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11000 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-211 |
2.58e-42 |
|
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: 143.86 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPTAGDVLAGTTPLAEIQED-----TR 83
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 --MMFQDARLLPwKSVIDNVGLGLK--GQWRDAARRALAAVGLEnRAGEW--------PAALSGGQKQRVALARALIHRP 151
Cdd:cd03260 83 vgMVFQKPNPFP-GSIYDNVAYGLRlhGIKLKEELDERVEEALR-KAALWdevkdrlhALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 152 GLLLLDEPLGALDALTRLEMQDLIVSLWQEHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-211 |
6.12e-41 |
|
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: 140.00 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 29 QLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL---AGTTPLAEIQEDTRMMFQDARLLPWKSVIDNVGLGL 105
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKvndQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 106 K------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:TIGR01277 96 HpglklnAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|..
gi 447013267 180 QEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-211 |
6.73e-41 |
|
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: 148.83 E-value: 6.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKN--IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI-QEDTRMMF---- 86
Cdd:COG2274 476 LENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdPASLRRQIgvvl 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLPwKSVIDNVGLGLKG------QWRDAARRALAAV-----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG2274 556 QDVFLFS-GTIRENITLGDPDatdeeiIEAARLAGLHDFIealpmGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLwqEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLS-TIRLADRIIVLDKGRI 687
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-211 |
1.10e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 137.95 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRmmfqdARLLP 93
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-----ARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKS-VIDNVGLGlkgqwrdaarralaavGLENRAGEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:cd03214 77 YVPqALELLGLA----------------HLADRPFN---ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 173 DLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
25-211 |
1.52e-40 |
|
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: 139.02 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---------MMFQDARLLPWK 95
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkklgFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:TIGR02211 99 TALENVAMPLligkksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQEHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:TIGR02211 179 IIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-214 |
1.89e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 139.33 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 29 QLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG----TTPLAeiQEDTRMMFQDARLLPWKSVIDNVGL 103
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGqdhtTTPPS--RRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 104 G------LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVS 177
Cdd:PRK10771 95 GlnpglkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 178 LWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-211 |
2.93e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.86 E-value: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYA---KNIV-LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLA--------GTTPLAEIQED 81
Cdd:PRK11153 4 LKNISKVFPqggRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 TRMMFQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLelagtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTH--DVSEAVamADRVLLIEEGKI 211
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKRI--CDRVAVIDAGRL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-211 |
3.65e-40 |
|
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: 138.62 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYaKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL---AGTTPLAEIQEDTRMMFQD 88
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPWKSVIDNVGLGLKGQWRDAARRA------LAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIErkvleiAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-211 |
5.17e-39 |
|
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: 136.41 E-value: 5.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-AGTTPLAE-----IQEDTRMMFQD 88
Cdd:TIGR04520 6 VSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvDGLDTLDEenlweIRKKVGMVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 -------ArllpwkSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:TIGR04520 86 pdnqfvgA------TVEDDVAFGLenlgvpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVaMADRVLLIEEGKI 211
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-214 |
5.32e-39 |
|
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: 135.89 E-value: 5.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL--------AGTTPLAEIQEDT 82
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditkLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMFQDARLLPWKSVIDNV---GLGLKGQWR-----------DAARRALAAVGLENRAGEWPAALSGGQKQRVALARALI 148
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWRsllgrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 149 HRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
1.67e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.37 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG-------TTPLAEIQEDTR-- 83
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLnIAGhqfdfsqKPSEKAIRLLRQkv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 -MMFQDARLLPWKSVIDNVG------LGL-KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG4161 85 gMVFQQYNLWPHLTVMENLIeapckvLGLsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
17-211 |
3.25e-38 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 136.36 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYaKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG---TTPLAEIQEDTRMMFQDARLLP 93
Cdd:NF040840 7 LSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDgkdITNLPPEKRGIAYVYQNYMLFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:NF040840 86 HKTVFENIAFGLKlrkvpkEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447013267 168 RLEmqdLIVSL--W-QEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:NF040840 166 RDE---LIREMkrWhREFGFTAIHVTHNFEEALSLADRVGIMLNGRL 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-211 |
3.36e-38 |
|
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: 140.28 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 3 TARLNQGTPLLLNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED 81
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 TRM-----MFQDARLLPWkSVIDNVGLGLKG------QWRDAARRALAAV-----GLENRAGEWPAALSGGQKQRVALAR 145
Cdd:COG4988 408 SWRrqiawVPQNPYLFAG-TIRENLRLGRPDasdeelEAALEAAGLDEFVaalpdGLDTPLGEGGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 146 ALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
17-206 |
4.02e-38 |
|
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: 132.35 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTT--PLAEIQ------EDTRMMFQ 87
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVyLNGQEtpPLNSKKaskfrrEKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGLKGQWR------DAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR03608 84 NFALIENETVEENLDLGLKYKKLskkekrEKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447013267 162 ALDALTRLEMQDLIVSLwQEHGFTVLLVTHDvSEAVAMADRVLLI 206
Cdd:TIGR03608 164 SLDPKNRDEVLDLLLEL-NDEGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-245 |
8.92e-38 |
|
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: 133.35 E-value: 8.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLLLNAvskhyaknivLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDTR-- 83
Cdd:TIGR04521 11 QPGTPFEKKA----------LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVtIDGRDITAKKKKKLKdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 -----MMFQdarlLPWK-----SVIDNVGLGLKGQwrdaarralaavGL-----ENRAGEW--------------PAALS 134
Cdd:TIGR04521 81 rkkvgLVFQ----FPEHqlfeeTVYKDIAFGPKNL------------GLseeeaEERVKEAlelvgldeeylersPFELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 135 GGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:TIGR04521 145 GGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 447013267 215 ltvDIPR-----PRRLGSVRLAELEA-EVLQRVMQRG 245
Cdd:TIGR04521 225 ---GTPRevfsdVDELEKIGLDVPEItELARKLKEKG 258
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-211 |
1.30e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.97 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---MMFQ 87
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRdiaMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKirgmpkAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-211 |
1.38e-37 |
|
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: 131.29 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD--VL------AGTTPLAEIQEDTRMMFQDARLLPWKSV 97
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSlkVLgqelhgASKKQLVQLRRRIGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 IDNVGLGLK-------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:TIGR02982 100 RQNVQMALElqpnlsyQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447013267 171 MQDLIVSLWQEHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-211 |
1.71e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.36 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG------TTP----LAEIQEDT 82
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGnhfdfsKTPsdkaIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMFQDARLLPWKSVIDNV------GLGL-KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLieapcrVLGLsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-211 |
4.26e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 134.51 E-value: 4.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 2 NTARLNQGTPLLLNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ 79
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTR-----MMFQ---------------------DARLLpwkSVIDNVGLGlkgQWRDAARRalaavGLENRAGEWPAAL 133
Cdd:COG4987 404 EDDLrrriaVVPQrphlfdttlrenlrlarpdatDEELW---AALERVGLG---DWLAALPD-----GLDTWLGEGGRRL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 134 SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHgfTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHR-LAGLERMDRILVLEDGRI 547
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-211 |
2.02e-35 |
|
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: 129.46 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD-VLAGTT--------PLAEIQEDTRMMFQDARLLPWKSVIDN 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEiVLNGRTlfdsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLK----GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIV 176
Cdd:TIGR02142 96 LRYGMKrarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 447013267 177 SLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-211 |
2.71e-35 |
|
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: 125.02 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL---AGTTPLAEIQEDTRMMFQDAR 90
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgKSYQKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLG--LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:cd03268 83 FYPNLTARENLRLLarLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03268 163 KELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-211 |
7.94e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.06 E-value: 7.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI-QEDTR----MMFQ 87
Cdd:COG1132 342 FENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtLESLRrqigVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPwKSVIDNVGLGLKGqwrdaarRALAAV------------------GLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:COG1132 422 DTFLFS-GTIRENIRYGRPD-------ATDEEVeeaakaaqahefiealpdGYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 150 RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-208 |
1.62e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.98 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP---TAGDVLAGTTPLAEIQEDTR---MM 85
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRrigIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGL-----KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALpptigRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAmADRVLLIEE 208
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-211 |
3.32e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.71 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 19 KHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG------TTPLAEIQEDTRMM------- 85
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGLIRQLrqhvgfv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLG-------LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGpvivkgePKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-211 |
4.33e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.97 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 22 AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE-----IQEDTRMMFQ--DARLLPw 94
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvwdVRRQVGMVFQnpDNQFVG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 95 KSVIDNVGLGLKGQ------WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13635 97 ATVQDDVAFGLENIgvpreeMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQEHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-217 |
5.61e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.62 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLLL-NAVSKHYAK----NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRM 84
Cdd:PRK11629 3 KILLQcDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 M---------FQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK11629 83 ElrnqklgfiYQFHHLLPDFTALENVAMPLligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 150 RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMaDRVLLIEEGKIGLDLTV 217
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-225 |
7.16e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 123.26 E-value: 7.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 16 AVSKHY---------AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI-------- 78
Cdd:PRK10419 8 GLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkaf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 79 QEDTRMMFQDA--RLLPWKSVIDNVG------LGL-KGQWRDAARRALAAVGL-ENRAGEWPAALSGGQKQRVALARALI 148
Cdd:PRK10419 88 RRDIQMVFQDSisAVNPRKTVREIIReplrhlLSLdKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 149 HRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI------GLDLTVDIPRP 222
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetqpvGDKLTFSSPAG 247
|
...
gi 447013267 223 RRL 225
Cdd:PRK10419 248 RVL 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-211 |
8.10e-34 |
|
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: 121.49 E-value: 8.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMFQdARLLP 93
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQ-RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WK---SVIDNVGLGLKGQWRDAARRALA----------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03235 81 RDfpiSVRDVVLMGLYGHKGLFRRLSKAdkakvdealeRVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03235 161 AGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-210 |
8.38e-34 |
|
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: 121.05 E-value: 8.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR----MMFQ 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGL--GLKGQWRDAARRAL--AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:COG4133 83 ADGLKPELTVRENLRFwaALYGLRADREAIDEalEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447013267 164 DALTRLEMQDLIVSlWQEHGFTVLLVTHDVSEAVamADRVLLIEEGK 210
Cdd:COG4133 163 DAAGVALLAELIAA-HLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-211 |
1.25e-33 |
|
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: 119.63 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 22 AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMF-----QDARLLPwKS 96
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvgylpQDDELFS-GS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVglglkgqwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIV 176
Cdd:cd03246 92 IAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*
gi 447013267 177 SLwQEHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:cd03246 141 AL-KAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-211 |
3.99e-33 |
|
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: 120.91 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 9 GTPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV------LAGTTPlAEIqed 81
Cdd:COG0411 1 SDPLLeVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrdITGLPP-HRI--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 TRM----MFQDARLLPWKSVIDNVGLGL----KGQWRDAARRALAA-----------------VGLENRAGEWPAALSGG 136
Cdd:COG0411 77 ARLgiarTFQNPRLFPELTVLENVLVAAharlGRGLLAALLRLPRArreereareraeellerVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 137 QKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-211 |
8.28e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.22 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 32 LHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI---------QEDTRMMFQDARLLPWKSVIDNVG 102
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrevrRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 103 LGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIV 176
Cdd:PRK10070 129 FGMElaginaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*
gi 447013267 177 SLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-209 |
1.63e-32 |
|
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: 120.93 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP---TAGDVLAGTTPLAEIQEDTR---------MMFQD--ARL 91
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkirgreiqMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 LPWKSVIDNVGLGL-------KGQWRDAARRALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:COG0444 100 NPVMTVGDQIAEPLrihgglsKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVL------LIEEG 209
Cdd:COG0444 180 ALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAvmyagrIVEEG 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-211 |
5.19e-32 |
|
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: 116.52 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFvAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDTRM---MFQ 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVLKQPQKLRRRigyLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGL--GLKG----QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYiaWLKGipskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-211 |
6.15e-32 |
|
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: 117.15 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR------MMFQDAR 90
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigRTFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLGLKGQWRDAARRALAA----------------VGLENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSGLLLARARreereareraeellerVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 155 LLDEPLGALDALTRLEMQDLIVSLWqEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-159 |
7.03e-32 |
|
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: 114.28 E-value: 7.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR-----MMFQDARLLPWKSVIDNV 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeigYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 102 GLGL---------KGQWRDAARRALAAVGLENR-AGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:pfam00005 81 RLGLllkglskreKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-211 |
1.09e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.42 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---------MMFQDARLLPWKS 96
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvgFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVGLG--LKG----QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:PRK10584 105 ALENVELPalLRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447013267 171 MQDLIVSLWQEHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-211 |
1.56e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 118.82 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 29 QLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRM---------MFQDARLLPWKSVID 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekrrigyVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NVGLGLKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:PRK11144 96 NLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190
....*....|....*....|....*....|..
gi 447013267 180 QEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-211 |
1.58e-31 |
|
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: 115.61 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR------MM 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGLKGQWRDAARRALAAV-----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03224 161 EGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-211 |
1.91e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 15 NAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR-----MMFQDA 89
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrraVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RL-LPWkSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALI------HRPGLLLL 156
Cdd:PRK13548 86 SLsFPF-TVEEVVAMGRaphglsRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 157 DEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-211 |
2.28e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE-----IQEDTRMMFQ--DARLLPwKS 96
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdIRHKIGMVFQnpDNQFVG-AT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVGLGLKGQWRDAARRAL------AAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKErvnealELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447013267 171 MQDLIVSLWQEHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 211
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-211 |
6.27e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 115.29 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 13 LLNA--VSKHYAKNI---------VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI--- 78
Cdd:TIGR02769 2 LLEVrdVTHTYRTGGlfgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 79 -----QEDTRMMFQDA--RLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGLENR-AGEWPAALSGGQKQRVAL 143
Cdd:TIGR02769 82 qrrafRRDVQLVFQDSpsAVNPRMTVRQIIGEPLrhltsldESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 144 ARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-211 |
2.59e-30 |
|
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: 112.46 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 19 KHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD-VLAG---TTPLAEIQEDTRMMFQDARLLPW 94
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGhdvVREPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 95 KSVIDNVGL-----GLKGQ-WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:cd03265 88 LTGWENLYIharlyGVPGAeRRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-214 |
3.70e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.91 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-----AEIQEDTRMMF 86
Cdd:cd03245 5 FRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLpWKSVIDNVGLG--------------LKGqwrDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:cd03245 85 QDVTLF-YGTLRDNITLGapladderilraaeLAG---VTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 153 LLLLDEPLGALDalTRLEMQdLIVSLWQE-HGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 214
Cdd:cd03245 161 ILLLDEPTSAMD--MNSEER-LKERLRQLlGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-206 |
4.93e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.79 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 21 YAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-AGTTPLAEIQEDTRMmfqdARLLPwKSVID 99
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRrAGGARVAYVPQRSEV----PDSLP-LTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NVGLGL---KGQWRDAARRALAAV-------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:NF040873 77 LVAMGRwarRGLWRRLTRDDRAAVddalervGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 170 EMQDLIVSlWQEHGFTVLLVTHDVsEAVAMADRVLLI 206
Cdd:NF040873 157 RIIALLAE-EHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-211 |
1.02e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.75 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI--QEDTRM---MFQDARL 91
Cdd:COG4559 7 LSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspWELARRravLPQHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 -LPWkSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALI-------HRPGLLLLD 157
Cdd:COG4559 87 aFPF-TVEEVVALGRaphgssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 158 EPLGALD---ALTRLEmqdlIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4559 166 EPTSALDlahQHAVLR----LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-212 |
1.90e-29 |
|
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: 110.94 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLA------GTTPLAEIQE-- 80
Cdd:COG1119 1 DPLLeLRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWELRKri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 81 ---DTRMMFQ-DARLLPWKSVI----DNVGLGLKGQWRDAARRAL--AAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:COG1119 81 glvSPALQLRfPRDETVLDVVLsgffDSIGLYREPTDEQRERAREllELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-211 |
1.94e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.55 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVlagttplaEIQEDTRMMF--QDARL 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLRIGYlpQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 LPWKSVIDNVGLGLKGQWRDAARRALAAVGLEN----------------RAGEWPA-----------------------A 132
Cdd:COG0488 73 DDDLTVLDTVLDGDAELRALEAELEELEAKLAEpdedlerlaelqeefeALGGWEAearaeeilsglgfpeedldrpvsE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIvslwQEHGFTVLLVTHDVS--EAVamADRVLLIEEGK 210
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDRYflDRV--ATRILELDRGK 226
|
.
gi 447013267 211 I 211
Cdd:COG0488 227 L 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-206 |
2.41e-29 |
|
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: 115.46 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRM-----MFQDARLLPwKSVIDN 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRdqiawVPQHPFLFA-GTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:TIGR02857 416 IRLARPDASDAEIREALERAgldefvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 170 EMQDLIVSLWQEHgfTVLLVTHDVsEAVAMADRVLLI 206
Cdd:TIGR02857 496 EVLEALRALAQGR--TVLLVTHRL-ALAALADRIVVL 529
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-211 |
2.44e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.52 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 8 QGTPLL-LNAVSKHY---------AKNIV--LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL------ 69
Cdd:COG4608 3 MAEPLLeVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 70 --AGTTPLAEIQEDTRMMFQD--ARLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGL-ENRAGEWPAALSGGQ 137
Cdd:COG4608 83 tgLSGRELRPLRRRMQMVFQDpyASLNPRMTVGDIIAEPLrihglasKAERRERVAELLELVGLrPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447013267 138 KQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
2.81e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.24 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTT----PLAEIQEDTRMMF 86
Cdd:PRK13632 10 VENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITiskeNLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 Q--DARLLPwKSVIDNVGLGLK------GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK13632 90 QnpDNQFIG-ATVEDDIAFGLEnkkvppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVaMADRVLLIEEGKI 211
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-212 |
2.82e-29 |
|
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: 109.27 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 19 KHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG--TTPLAEIQEDTRMMFQDA-RLLPWK 95
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkPIKAKERRKSIGYVMQDVdYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLGLK--GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQD 173
Cdd:cd03226 88 SVREELLLGLKelDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 174 LIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:cd03226 168 LIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-226 |
4.78e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTP-----LAEIQEDTRMMFQDARLLPWKSVID-N 100
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKHIGIVFQNPDNQFVGSIVKyD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQ------WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDL 174
Cdd:PRK13648 105 VAFGLENHavpydeMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447013267 175 IVSLWQEHGFTVLLVTHDVSEAVAmADRVLLIEEGK-------------------IGLDLTVDIPRPRRLG 226
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTvykegtpteifdhaeeltrIGLDLPFPIKINQMLG 254
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
17-211 |
5.23e-29 |
|
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: 109.69 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDTRMM---FQDARLL 92
Cdd:TIGR03864 7 LSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQIsVAGHDLRRAPRAALARLgvvFQQPTLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PWKSVIDNV-------GLGlKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:TIGR03864 87 LDLSVRQNLryhaalhGLS-RAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 166 LTRLEMQDLIVSLWQEHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 211
Cdd:TIGR03864 166 ASRAAITAHVRALARDQGLSVLWATHLVDE-IEASDRLVVLHRGRV 210
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
19-211 |
8.32e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 109.50 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 19 KHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ--------EDTR------- 83
Cdd:COG4598 16 KSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpADRRqlqrirt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 ---MMFQDARLLPWKSVIDNVG------LGL-KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG4598 96 rlgMVFQSFNLWSHMTVLENVIeapvhvLGRpKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 154 LLLDEPLGALDALTRLE----MQDLivslwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4598 176 MLFDEPTSALDPELVGEvlkvMRDL-----AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-211 |
1.06e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.05 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKN----IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR- 83
Cdd:PRK10535 2 TALLeLKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 --------MMFQDARLLPWKSVIDNV-------GLGlKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALI 148
Cdd:PRK10535 82 qlrrehfgFIFQRYHLLSHLTAAQNVevpavyaGLE-RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 149 HRPGLLLLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
36-211 |
1.39e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 109.16 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 36 AGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLA--EIQ---EDTRMMFQDA------RLlpwksvidNVG-- 102
Cdd:COG4167 38 AGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKyrcKHIRMIFQDPntslnpRL--------NIGqi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 103 ----LGLKGQWRDAARRAL-----AAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:COG4167 110 leepLRLNTDLTAEEREERifatlRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQII 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 173 DLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4167 190 NLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-211 |
1.58e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.04 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHY-AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQE--------DTRMMFQ 87
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNrevpflrrQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGL-----GLKGQ-WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIpliiaGASGDdIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 162 ALDAltrlEMQDLIVSLWQEH---GFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10908 167 NLDD----ALSEGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-211 |
1.90e-28 |
|
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: 107.96 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLA-----GTTPLAEIQEDTRMMFQDARLLPwKSVIDN 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdlALADPAWLRRQVGVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrL 169
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAgahdfiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD----Y 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447013267 170 EMQDLIVSLWQE--HGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03252 172 ESEHAIMRNMHDicAGRTVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-211 |
2.24e-28 |
|
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: 112.47 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLEtPTAGDVLAGTTPLAEIQEDTR--------MMFQD--ARLLPWKS 96
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALrplrrrmqVVFQDpfGSLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVGLGL--------KGQWRDAARRALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:COG4172 381 VGQIIAEGLrvhgpglsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447013267 168 RLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4172 461 QAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-211 |
4.42e-28 |
|
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: 112.27 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-----AEIQEDTRMMF 86
Cdd:TIGR03375 466 FRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqidpADLRRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLpWKSVIDNVGLGLKGQWRDAARRALAAVGLENRA-----------GEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:TIGR03375 546 QDPRLF-YGTLRDNIALGAPYADDEEILRAAELAGVTEFVrrhpdgldmqiGERGRSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 156 LDEPLGALDAltRLEMQdLIVSLWQE-HGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR03375 625 LDEPTSAMDN--RSEER-FKDRLKRWlAGKTLVLVTHRTS-LLDLVDRIIVMDNGRI 677
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
4.80e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.43 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 1 MNTARLNQGTPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--ETPTA---G-------DV 68
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGeilldgeDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 69 LAGTTPLAEIqedtR----MMFQDARLLPwKSVIDNVGLGLKGQwrdaarralaavGLENR-------------AGEW-- 129
Cdd:COG1117 81 YDPDVDVVEL----RrrvgMVFQKPNPFP-KSIYDNVAYGLRLH------------GIKSKseldeiveeslrkAALWde 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 130 -------PA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALD--ALTRLEmqDLIVSLWQEhgFTVLLVTHDVSEAVAM 199
Cdd:COG1117 144 vkdrlkkSAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILELKKD--YTIVIVTHNMQQAARV 219
|
250
....*....|....*..
gi 447013267 200 ADRVL------LIEEGK 210
Cdd:COG1117 220 SDYTAffylgeLVEFGP 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-210 |
5.26e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 106.01 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 18 SKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAE----IQEDT-R------MM 85
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVsVPGSIAYVSqepwIQNGTiRenilfgKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLlpwKSVIDNVGLG-----LKGqwrdaarralaavGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03250 92 FDEERY---EKVIKACALEpdleiLPD-------------GDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALT-RLEMQDLIVSLWQEHGfTVLLVTHDVsEAVAMADRVLLIEEGK 210
Cdd:cd03250 156 SAVDAHVgRHIFENCILGLLLNNK-TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-211 |
8.93e-28 |
|
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: 105.44 E-value: 8.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-AEIQEDTRMMFQDAR 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDN-VGLG-LKG----QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:cd03269 81 LYPKMKVIDQlVYLAqLKGlkkeEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447013267 165 ALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-216 |
1.65e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.32 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLllnavskhyaKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGT--TPLAEIQEdTR 83
Cdd:COG1101 12 NPGTVN----------EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKdvTKLPEYKR-AK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 MM---FQD------ARLlpwkSVIDN------------VGLGLKGQWRDAARRALAAV--GLENRAGEWPAALSGGQKQR 140
Cdd:COG1101 81 YIgrvFQDpmmgtaPSM----TIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 141 VALARALIHRPGLLLLDEPLGALD---ALTRLEMQDLIVslwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKIV---EENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVS 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-211 |
1.75e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 22 AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD----VLAGTTPLA----EIQEDTRMMFQ--DARL 91
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskiTVDGITLTAktvwDIREKVGIVFQnpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 LPwKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK13640 98 VG-ATVGDDVAFGLenravpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 166 LTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-211 |
2.63e-27 |
|
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: 105.06 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV------LAGTTP-------L 75
Cdd:COG0410 1 MPMLeVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgedITGLPPhriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 76 AEIQEDtRMMFqdARLlpwkSVIDNVGLGLKGQWRDAARRALaavgLE--------------NRAGewpaALSGGQKQRV 141
Cdd:COG0410 81 GYVPEG-RRIF--PSL----TVEENLLLGAYARRDRAEVRAD----LErvyelfprlkerrrQRAG----TLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 142 ALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-211 |
2.80e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG--TTP------LAEIQEDTRMMFQ--DARLLPwK 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGyhITPetgnknLKKLRKKVSLVFQfpEAQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLGLKG-------------QWRDAarralaaVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK13641 102 TVLKDVEFGPKNfgfsedeakekalKWLKK-------VGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSlWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13641 175 GLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-211 |
2.97e-27 |
|
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: 104.61 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 23 KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDT-RMMF----QDARLLPwKSV 97
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIgvvlQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 IDNVGLGLKGQWRDAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 166
Cdd:cd03254 94 MENIRLGRPNATDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447013267 167 TRLEMQDLIVSLwqEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03254 174 TEKLIQEALEKL--MKGRTSIIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-211 |
3.01e-27 |
|
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: 104.51 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAK--NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG----TTPLAEIQEDTRMMFQDAR 90
Cdd:cd03263 6 LTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysiRTDRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGL--GLKG----QWRDAARRALAAVGLE----NRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:cd03263 86 LFDELTVREHLRFyaRLKGlpksEIKEEVELLLRVLGLTdkanKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALTRLEMQDLIvsLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03263 162 SGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-255 |
4.60e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKN------IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL------AGTTPLAEIQEDTRM 84
Cdd:PRK13633 10 VSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQ--DARL-----------------LPWKSVIDNVGLGLKgqwrdaarralaAVGLENRAGEWPAALSGGQKQRVALAR 145
Cdd:PRK13633 90 VFQnpDNQIvativeedvafgpenlgIPPEEIRERVDESLK------------KVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 146 ALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAmADRVLLIEEGKIGLDLTvdiprPRRL 225
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT-----PKEI 231
|
250 260 270
....*....|....*....|....*....|....
gi 447013267 226 GSvrlaelEAEVLQR----VMQRGESETRLRKQG 255
Cdd:PRK13633 232 FK------EVEMMKKigldVPQVTELAYELKKEG 259
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-210 |
4.76e-27 |
|
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: 101.76 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVlagttplaeiqedtrmmfqdarllp 93
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 wkSVIDNVGLGLKGQwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrLEMQD 173
Cdd:cd03221 58 --TWGSTVKIGYFEQ------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIE 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 174 LIVSLWQEHGFTVLLVTHDVS--EAVamADRVLLIEEGK 210
Cdd:cd03221 108 ALEEALKEYPGTVILVSHDRYflDQV--ATKIIELEDGK 144
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-211 |
6.26e-27 |
|
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: 102.12 E-value: 6.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL------AGTTPLAEIQEDTRMMFQdar 90
Cdd:cd03216 6 ITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILvdgkevSFASPRDARRAGIAMVYQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 llpwksvidnvglglkgqwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447013267 171 MQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03216 121 LFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-214 |
8.07e-27 |
|
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: 103.95 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 5 RLNQGTPLLLNAVS----KHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQ 79
Cdd:cd03267 11 RVYSKEPGLIGSLKslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRM---MFQDARLLPWK-SVIDNVGL-----GLK-GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:cd03267 91 KFLRRigvVFGQKTQLWWDlPVIDSFYLlaaiyDLPpARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 150 RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-211 |
2.37e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.95 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTplaEIQEDTR------------MMFQ--DARLL 92
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGER---VITAGKKnkklkplrkkvgIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PwKSVIDNVGLG------LKGQWRDAARRALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK13634 100 E-ETVEKDICFGpmnfgvSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 166 LTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-217 |
2.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPlllnavskhYAKnIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG-------DVLAGTTPLAEIQ 79
Cdd:PRK13637 13 MEGTP---------FEK-KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRMMFQDARLLPWKSVID--------NVGLGlKGQWRDAARRALAAVGL--ENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEkdiafgpiNLGLS-EEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 150 RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTV 217
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
26-211 |
6.16e-26 |
|
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: 101.54 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTRMMF----QDARLLPwKSVIDN 100
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIglvsQDVFLFN-DTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03251 96 IAYGRPGATREEVEEAARAAnahefimelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQehGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03251 176 LVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKI 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-211 |
6.31e-26 |
|
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: 101.46 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHY---AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTRMMF----QD 88
Cdd:cd03249 6 VSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQIglvsQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLPwKSVIDNVGLGLKGQWRDAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:cd03249 86 PVLFD-GTIAENIRYGKPDATDEEVEEAAKKAnihdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 158 EPLGALDALTRLEMQDLIVSLWQehGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-211 |
7.62e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.46 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 20 HYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPTAGDV-LAGTTPLA------EIQEDTRMMFQ 87
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVrLFGRNIYSpdvdpiEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSVIDNVGLGLK--------------GQWRDAARRALAAVglENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKlnglvkskkelderVEWALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 154 LLLDEPLGALDALTRLEMQDLIVSLWQEhgFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-214 |
8.34e-26 |
|
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: 99.69 E-value: 8.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMF----QDARLLPwKSVIDNV 101
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIsvlnQRPYLFD-TTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GlglkgqwrdaarralaavglenragewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQE 181
Cdd:cd03247 96 G----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD 147
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 182 HgfTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 214
Cdd:cd03247 148 K--TLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-192 |
8.52e-26 |
|
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: 105.14 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 8 QGTPLLLNAVSKHYA-KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDT---- 82
Cdd:TIGR02868 331 GKPTLELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 -RMMFQDARLLPwKSVIDNVGLGLKGQWRDAARRALAAVGLEN-----------RAGEWPAALSGGQKQRVALARALIHR 150
Cdd:TIGR02868 411 vSVCAQDAHLFD-TTVRENLRLARPDATDEELWAALERVGLADwlralpdgldtVLGEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLwqEHGFTVLLVTHD 192
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-211 |
1.04e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.58 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED----- 81
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 -----------TR--MMFQDARLLPWKSVIDNVG------LGL-KGQWRDAARRALAAVGLENRA-GEWPAALSGGQKQR 140
Cdd:PRK10619 81 vadknqlrllrTRltMVFQHFNLWSHMTVLENVMeapiqvLGLsKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447013267 141 VALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-210 |
1.19e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 11 PLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMF---- 86
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARLLPWKSVIDNVGL-----GLK-GQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVfgryfGLSaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 161 GALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-211 |
2.32e-25 |
|
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: 99.92 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLaeiqedTRM-MFQDARL---- 91
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI------TKLpMHKRARLgigy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 LPWK-------SVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:cd03218 80 LPQEasifrklTVEENILAVLeirglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-211 |
2.33e-25 |
|
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: 104.06 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 22 AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMF-----QDARLLPwKS 96
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHigylpQDVELFD-GT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVG-----------------------LGLKGqwrdaarralaavGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:COG4618 422 IAENIArfgdadpekvvaaaklagvhemiLRLPD-------------GYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 154 LLLDEPLGALD-----ALTRlemqdLIVSLwQEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG4618 489 VVLDEPNSNLDdegeaALAA-----AIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-211 |
2.84e-25 |
|
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: 103.61 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKS----TLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR---------MMFQD--AR 90
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrrirgnriaMIFQEpmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVG------LGLKG-QWRDAARRALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG4172 105 LNPLHTIGKQIAevlrlhRGLSGaAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHD---VSEavaMADRVLLIEEGKI 211
Cdd:COG4172 185 TALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVMRQGEI 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-214 |
2.89e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.47 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL----ETPTAGDVLAGTTPLAE--IQEDTR 83
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREgrLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 -------MMFQDARLLPWKSVIDNVGLGLKG---------QW-----RDAARRALAAVGLENRAGEWPAALSGGQKQRVA 142
Cdd:PRK09984 83 ksrantgYIFQQFNLVNRLSVLENVLIGALGstpfwrtcfSWftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 143 LARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
3.39e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.69 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTP-------LAEIQEDTR 83
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysrkgLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 MMFQDA-RLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK13636 86 MVFQDPdNQLFSASVYQDVSFGAvnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 157 DEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-211 |
5.30e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 98.70 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-----EDTRMMFQDARLLPwKSVIDN 100
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhSKVSLVGQEPVLFA-RSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAhahsfiselasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQEHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03248 188 QVQQALYDWPERR--TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-204 |
5.49e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 36 AGQFVAVVGRSGGGKSTLLRLLAGLETPTAG-------DVL-AGTTPLAEIQEDTRMMFQD--ARLLPWKSVID------ 99
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGelyyqgqDLLkADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQileepl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 --NVGLGlKGQWRDAARRALAAVGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIV 176
Cdd:PRK11308 120 liNTSLS-AAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMM 198
|
170 180
....*....|....*....|....*...
gi 447013267 177 SLWQEHGFTVLLVTHDVSEAVAMADRVL 204
Cdd:PRK11308 199 DLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-211 |
6.14e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.98 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 2 NTARLNQGTpLLLNAVSKHY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ 79
Cdd:PRK11160 330 STAAADQVS-LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDT--RMMfqdarllpwkSVI------------DNVGLGLKGQWRDAARRALAAVGLENRA----------GEWPAALSG 135
Cdd:PRK11160 409 EAAlrQAI----------SVVsqrvhlfsatlrDNLLLAAPNASDEALIEVLQQVGLEKLLeddkglnawlGEGGRQLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 136 GQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQehGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQI 551
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-211 |
6.51e-25 |
|
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: 98.84 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDT-R----MMFQDARLLPwKSVIDN 100
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRraigVVPQDTVLFN-DTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAVGLENRAGEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03253 95 IRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQehGFTVLLVTHDVSEaVAMADRVLLIEEGKI 211
Cdd:cd03253 175 EIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRI 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-211 |
1.13e-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: 102.19 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 8 QGTPLL-LNAVSKHYA---KNIV--LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD--VLAGT--TPLAE 77
Cdd:TIGR03269 275 VGEPIIkVRNVSKRYIsvdRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 78 IQEDTR--------MMFQDARLLPWKSVIDN----VGLGLKGQWRDAARR-ALAAVGLENRAGE-----WPAALSGGQKQ 139
Cdd:TIGR03269 355 PGPDGRgrakryigILHQEYDLYPHRTVLDNlteaIGLELPDELARMKAViTLKMVGFDEEKAEeildkYPDELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 140 RVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-211 |
1.38e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.06 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPTAGDVLAG-----TTPLAEIQEDTRMMFQDARLLPWK 95
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDgqdifKMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLGLK--------------GQWRDAARRALAAVglENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK14247 98 SIFENVALGLKlnrlvkskkelqerVRWALEKAQLWDEV--KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLWQEhgFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-211 |
1.83e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 101.72 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTRMMF----QDARLLPwKSVIDN 100
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlASLRRQValvsQDVVLFN-DTIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAV------------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:TIGR02203 426 IAYGRTEQADRAEIERALAAayaqdfvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQehGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR02203 506 RLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-211 |
1.87e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTplAEI----QEdtrmm 85
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--VKIgyfdQH----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 fQDArLLPWKSVIDNVGLGLKGqwrdaaRRALAAVGL-------ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG0488 387 -QEE-LDPDKTVLDELRDGAPG------GTEQEVRGYlgrflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 159 PLGALDaltrLEMQDLIVSLWQEHGFTVLLVTHDVS--EAVamADRVLLIEEGKI 211
Cdd:COG0488 459 PTNHLD----IETLEALEEALDDFPGTVLLVSHDRYflDRV--ATRILEFEDGGV 507
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-211 |
2.50e-24 |
|
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: 96.67 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKN----IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-AGTTPLAEIQEDTRMM- 85
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvDGFDVVKEPAEARRRLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 --FQDARLLPWKSVIDNVGL-----GLKGQWRDAARRALAAV-----GLENRAGEwpaaLSGGQKQRVALARALIHRPGL 153
Cdd:cd03266 82 fvSDSTGLYDRLTARENLEYfaglyGLKGDELTARLEELADRlgmeeLLDRRVGG----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 154 LLLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-204 |
3.72e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 98.63 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 31 DLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL--------AGTTPLAEIQEDTRMMFQD--ARLLPWKSVIDN 100
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGL--------KGQWRDAARRALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:PRK15079 121 IAEPLrtyhpklsRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 172 QDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVL 204
Cdd:PRK15079 201 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-204 |
5.90e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 6 LNQGTPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED--- 81
Cdd:PRK10247 1 MQENSPLLqLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 --------TRMMFQDarllpwkSVIDNvglgLKGQWR--------DAARRALAAVGLENRAGEWP-AALSGGQKQRVALA 144
Cdd:PRK10247 81 qqvsycaqTPTLFGD-------TVYDN----LIFPWQirnqqpdpAIFLDDLERFALPDTILTKNiAELSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 145 RALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEaVAMADRVL 204
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVI 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-211 |
7.01e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG------TTPLAEIQEDTR-----MMFQDARLLPwK 95
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvssTSKQKEIKPVRKkvgvvFQFPESQLFE-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLG------LKGQWRDAARRALAAVGLENRAGE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13643 101 TVLKDVAFGpqnfgiPKEKAEKIAAEKLEMVGLADEFWEkSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-211 |
1.22e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.32 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 21 YAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG-----DVLAGTTPL------AEIQEDTRMMFQDA 89
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrdvLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPwKSVIDNVGLGLKG-------QWRDAARRALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhklvprkEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEhgFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-211 |
2.24e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.22 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL--------AGTTPLAEIQEDTRMMFQDARLLPWKSV 97
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipaMSRSRLYTVRKRMSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 IDNVGLGLKGQ-------WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLE 170
Cdd:PRK11831 102 FDNVAYPLREHtqlpaplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447013267 171 MQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-221 |
3.43e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--------ETPTAGDVL---------AGTtpLAEI----QEDTR 83
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLflpqrpylpLGT--LREAllypATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 mmFQDARLlpwKSVIDNVGLGlkgqwrdaarralaavGLENRAGE---WPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:COG4178 455 --FSDAEL---REALEAVGLG----------------HLAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALTRLEMQDLIVSlwQEHGFTVLLVTHDvSEAVAMADRVLLIEEGKIGLDLTVDIPR 221
Cdd:COG4178 514 SALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-221 |
3.79e-23 |
|
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: 94.51 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 11 PLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIqEDTRMMFQDA 89
Cdd:TIGR02323 2 PLLqVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAEL-ELYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLL---PWKSVIDNVGLGLKGQWRDAARRALAAVGLENR--------AGEW--------------PAALSGGQKQRVALA 144
Cdd:TIGR02323 81 RRLmrtEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygniratAQDWleeveidptriddlPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 145 RALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GL-DLTVDIP 220
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesGLtDQVLDDP 240
|
.
gi 447013267 221 R 221
Cdd:TIGR02323 241 Q 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-211 |
4.61e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGttplaeiQEDTRM-MFQDARL--- 91
Cdd:COG1137 9 LVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfLDG-------EDITHLpMHKRARLgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 -LP------WK-SVIDNVGLGL------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLD 157
Cdd:COG1137 82 yLPqeasifRKlTVEDNILAVLelrklsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 158 EPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-218 |
5.02e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLaeiQEDTRMMF---QD 88
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIgylPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 AR-LLPWKSVIDNVG-LG-LKG-----------QWRDAarralaaVGLENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:COG4152 79 ERgLYPKMKVGEQLVyLArLKGlskaeakrradEWLER-------LGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447013267 155 LLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
17-218 |
5.71e-23 |
|
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: 93.23 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLaeiqedTRMMFQDARLLPWK- 95
Cdd:TIGR03740 6 LSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW------TRKDLHKIGSLIESp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 ------SVIDNVG-----LGLKGQwrdAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR03740 80 plyenlTARENLKvhttlLGLPDS---RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 165 ALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 218
Cdd:TIGR03740 157 PIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-201 |
6.84e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 16 AVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPTA---GDVLAGTTPL-------AEIQEDTR 83
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGFrveGKVTFHGKNLyapdvdpVEVRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 MMFQDARLLPwKSVIDNVG-----LGLKGQWRDAARRALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLL 154
Cdd:PRK14243 95 MVFQKPNPFP-KSIYDNIAygariNGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447013267 155 LLDEPLGALDALTRLEMQDLIVSLWQEhgFTVLLVTHDVSEAVAMAD 201
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-211 |
8.29e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.84 E-value: 8.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeTPTAGDVLAGTTPLAEIQEdtrmmfQDAR----------LLPWKSVID 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDP------ESWRkhlswvgqnpQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NVGLG------------LKGQWRDAARRALAAvGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK11174 442 NVLLGnpdasdeqlqqaLENAWVSEFLPLLPQ-GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447013267 168 -RLEMQDLIvSLWQEHgfTVLLVTHDVSEAVAMaDRVLLIEEGKI 211
Cdd:PRK11174 521 eQLVMQALN-AASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-211 |
9.94e-23 |
|
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: 91.84 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTA--GDVLAGTTPLAEIQEDTRMMF--QDARLLPWKSVIDNV 101
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKIIGYvpQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 G--LGLKGqwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:cd03213 104 MfaAKLRG-------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA 158
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 180 QEhGFTVLLVTHDVS-EAVAMADRVLLIEEGKI 211
Cdd:cd03213 159 DT-GRTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-209 |
1.16e-22 |
|
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: 92.50 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL----AGTTPLAEIQEDTRMMF---------QDARLL 92
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdGGWVDLAQASPREILALrrrtigyvsQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PWKSVIDNVGLGLKGQWRDAARRalaavglENRAGEW--------------PAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEA-------RARARELlarlnlperlwdlpPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHD--VSEAVamADRVLLIEEG 209
Cdd:COG4778 179 PTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDeeVREAV--ADRVVDVTPF 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-211 |
1.17e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.66 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLA---------EIQEDTRMMFQ--DARLLPwK 95
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikQIRKKVGLVFQfpESQLFE-E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLG------LKGQWRDAARRALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK13649 102 TVLKDVAFGpqnfgvSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13649 182 KELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-216 |
1.50e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.63 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ------EDTRMM 85
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtakimrEAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLG----LKGQWRDAARRALAAVG-LENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGgffaERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 161 GALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-230 |
2.37e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLA-----EIQEDTRMMFQDARLLPWKSVIDN 100
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkenirEVRKFVGLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 ------VGLGLKGQWRD-AARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQD 173
Cdd:PRK13652 99 diafgpINLGLDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 174 LIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD--IPRPRRLGSVRL 230
Cdd:PRK13652 179 FLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEeiFLQPDLLARVHL 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
36-211 |
2.92e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 36 AGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-----AEIQEDTRMMFQDA--RLLPWKSV--IDNVGLGLK 106
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySYRSQRIRMIFQDPstSLNPRQRIsqILDFPLRLN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 107 GQWRDAA-----RRALAAVGL-ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQ 180
Cdd:PRK15112 118 TDLEPEQrekqiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE 197
|
170 180 190
....*....|....*....|....*....|.
gi 447013267 181 EHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK15112 198 KQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-221 |
2.95e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.30 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-----AGTTPLAEIQE-DT 82
Cdd:PRK11701 4 QPLLsVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdGQLRDLYALSEaER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMF--------QDAR--LLPWKSVIDNVGLGLKGqwrdaarralaaVG------LENRAGEW--------------PAA 132
Cdd:PRK11701 84 RRLLrtewgfvhQHPRdgLRMQVSAGGNIGERLMA------------VGarhygdIRATAGDWlerveidaariddlPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI- 211
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVv 231
|
250
....*....|...
gi 447013267 212 --GL-DLTVDIPR 221
Cdd:PRK11701 232 esGLtDQVLDDPQ 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-191 |
3.09e-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: 89.91 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVlagttplaEIQEDTRMMF------------QDARL 91
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFlpqrpylplgtlREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 92 LPWKSVidnvglglkgqwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlEM 171
Cdd:cd03223 86 YPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ES 126
|
170 180
....*....|....*....|
gi 447013267 172 QDLIVSLWQEHGFTVLLVTH 191
Cdd:cd03223 127 EDRLYQLLKELGITVISVGH 146
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-211 |
3.60e-22 |
|
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: 94.89 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHY-AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI-QEDTR----------M 84
Cdd:COG5265 363 VSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtQASLRaaigivpqdtV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQD---------------------ARLlpwkSVIDNVGLGLKGqwrdaarralaavGLENRAGEWPAALSGGQKQRVAL 143
Cdd:COG5265 443 LFNDtiayniaygrpdaseeeveaaARA----AQIHDFIESLPD-------------GYDTRVGERGLKLSGGEKQRVAI 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 144 ARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLS-TIVDADEILVLEAGRI 570
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-212 |
4.00e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE-----IQEDTRMMFQDARLLPwKSVIDN 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHRQVALVGQEPVLFS-GSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQWRDAARRALAAVGLENRAGEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrl 169
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA---- 650
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 170 EMQDLIVSLWQEHGFTVLLVTHDVSeAVAMADRVLLIEEGKIG 212
Cdd:TIGR00958 651 ECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVV 692
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-211 |
4.39e-22 |
|
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: 91.05 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTR----MMF- 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaragIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 -QDARLLPWKSVIDNVGLGLKGQWRDAARRALAAVGL--------ENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLD 157
Cdd:TIGR03410 81 pQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELfpvlkemlGRRGGD----LSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 158 EPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-211 |
9.11e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLLLNAvskhyaknivLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG-------------------- 66
Cdd:PRK13651 13 NKKLPTELKA----------LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 67 ----DVLAGTTP-----LAEIQEDTRMMFQDARLLPWKSVIDN------VGLGL-KGQWRDAARRALAAVGL-ENRAGEW 129
Cdd:PRK13651 83 vlekLVIQKTRFkkikkIKEIRRRVGVVFQFAEYQLFEQTIEKdiifgpVSMGVsKEEAKKRAAKYIELVGLdESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 130 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 447013267 210 KI 211
Cdd:PRK13651 242 KI 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-210 |
1.07e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMF----QDA 89
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIgvvpQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPWKSVIDNvgLGLKGQWRDAARRALAAV--------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK13536 124 NLDLEFTVREN--LLVFGRYFGMSTREIEAVipsllefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 162 ALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-210 |
1.55e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 28 NQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEI--QEDTRM----MFQDARLLPWKSVIDNV 101
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIARMgvvrTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 ----------------------------GLGLKGQWRDAarralaaVGLENRAGEWPAALSGGQKQRVALARALIHRPGL 153
Cdd:PRK11300 102 lvaqhqqlktglfsgllktpafrraeseALDRAATWLER-------VGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 154 LLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-211 |
1.87e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQedTRMMFQDA 89
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS--SRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPWK-------SVIDNVGLG----------LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:PRK11231 79 ALLPQHhltpegiTVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-211 |
1.87e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.76 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-----AGTTPLAEI--------QE 80
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldVATTPSRELakrlailrQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 81 DTRMMfqdaRLlpwkSVIDNVGLG--------LKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:COG4604 84 NHINS----RL----TVRELVAFGrfpyskgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-191 |
1.91e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 88.57 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED-TRMMF----QDArLLPWKSVIDN 100
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILylghLPG-LKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGL--GLKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlEMQDLIVSL 178
Cdd:TIGR01189 94 LHFwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK----AGVALLAGL 169
|
170
....*....|....*.
gi 447013267 179 WQEH---GFTVLLVTH 191
Cdd:TIGR01189 170 LRAHlarGGIVLLTTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-252 |
2.42e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-AGTTPLAEIQEDTR----MMFQDARL---LPwksVI 98
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPFKRRKEFARrigvVFGQRSQLwwdLP---AI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 99 DNVGLgLK-------GQWRDAARRALAAVGLEN------RAgewpaaLSGGQKQRVALARALIHRPGLLLLDEP-LGaLD 164
Cdd:COG4586 115 DSFRL-LKaiyripdAEYKKRLDELVELLDLGElldtpvRQ------LSLGQRMRCELAAALLHRPKILFLDEPtIG-LD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 165 ALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPR----PRRLGSVRLAE-LEAEVLQ 239
Cdd:COG4586 187 VVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKerfgPYKTIVLELAEpVPPLELP 266
|
250
....*....|....*.
gi 447013267 240 R---VMQRGESETRLR 252
Cdd:COG4586 267 RggeVIEREGNRVRLE 282
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-211 |
2.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.75 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTP-------LAEIQEDTRMMFQ---DARLLPwk 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkksLLEVRKTVGIVFQnpdDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVG-----LGL-KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:PRK13639 95 TVEEDVAfgplnLGLsKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-202 |
3.15e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.45 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPTAG-------DVLAGTTPLAEIQ 79
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGsivynghNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRMMFQDARLLPWkSVIDNV--GLGLKGQWRDAARRALAAVGL---------ENRAGEWPAALSGGQKQRVALARALI 148
Cdd:PRK14239 86 KEIGMVFQQPNPFPM-SIYENVvyGLRLKGIKDKQVLDEAVEKSLkgasiwdevKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447013267 149 HRPGLLLLDEPLGALDALTRLEMQDLIVSLwqEHGFTVLLVTHDVSEAVAMADR 202
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-211 |
3.67e-21 |
|
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: 92.11 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIqeDTRMMFQDAR 90
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWK------SVIDNVGLGLKGQWRDAARRALAAV------------GLENRAGEWPAALSGGQKQRVALARALIHRPG 152
Cdd:TIGR01193 552 YLPQEpyifsgSILENLLLGAKENVSQDEIWAACEIaeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIVSLWQEhgfTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKI 686
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-211 |
7.43e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.72 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGttplaeiQEDTRMMFQDAR---------------LLP 93
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEItLDG-------KPVTRRSPRDAIragiayvpedrkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKSVIDNVGLglkgqwrdaarralaavglenragewPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQD 173
Cdd:cd03215 92 DLSVAENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 447013267 174 LIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03215 146 LIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-211 |
1.08e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 21 YAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-----AEIQEDTRMMFQDARLLPWK 95
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyasKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLG------LKGQW----RDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK10253 97 TVQELVARGryphqpLFTRWrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 166 LTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-211 |
1.65e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAE----IQEDTRMMFQDA-RLLPWKSVIDN 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkIDGELLTAEnvwnLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQ------WRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDL 174
Cdd:PRK13642 103 VAFGMENQgipreeMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 175 IVSLWQEHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 211
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-211 |
1.88e-20 |
|
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: 86.65 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHIPAGQFVAVVGRSGGGKST----LLRLLAGLETPTAGDVLAGTTPLAEI---QEDTRMMFQDAR--LLPWKSVIDN 100
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLsirGRHIATIMQNPRtaFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 V------GLGLKGQWRDAARRALAAVGLENRA---GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:TIGR02770 85 AietlrsLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447013267 172 QDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-211 |
2.69e-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: 89.33 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 22 AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGttplAEIQEDTRMMF--------QDARLL 92
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrLDG----ADLKQWDRETFgkhigylpQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PwKSVIDNV---GLGLKGQWRDAARRALAA--------VGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR01842 405 P-GTVAENIarfGENADPEKIIEAAKLAGVhelilrlpDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447013267 162 ALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR01842 484 NLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-203 |
2.70e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG-----TTPLAEIQEDT 82
Cdd:COG1129 2 EPLLeMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlLDGepvrfRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMFQDARLLPWKSVIDNVGLG---LKG---QWRDaarralaavgLENRAGEW---------PAA----LSGGQKQRVAL 143
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGrepRRGgliDWRA----------MRRRARELlarlgldidPDTpvgdLSVAQQQLVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 144 ARALIHRPGLLLLDEPLGAL-----DALTRLeMQDLivslwQEHGFTVLLVTHDVSEAVAMADRV 203
Cdd:COG1129 152 ARALSRDARVLILDEPTASLterevERLFRI-IRRL-----KAQGVAIIYISHRLDEVFEIADRV 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-211 |
5.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNI-----VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGT----TPLAEIQEDT 82
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RM------MFQDARLLPWKSVIDN------VGLGL-KGQWRDAARRALAAVGL-ENRAGEWPAALSGGQKQRVALARALI 148
Cdd:PRK13645 87 RLrkeiglVFQFPEYQLFQETIEKdiafgpVNLGEnKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 149 HRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-211 |
9.17e-20 |
|
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: 84.51 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG--DVLAGTTPLAEIQedtrmmfqdARLLPWKSVIDNV-- 101
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtvTVRGRVSSLLGLG---------GGFNPELTGRENIyl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GLGLKGQWRDAARRALAAV----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVS 177
Cdd:cd03220 108 NGRLLGLSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|....
gi 447013267 178 LWqEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:cd03220 188 LL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-211 |
1.72e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 1 MNTARLNQGTPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAeiQE 80
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE--SW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 81 DTRMMFQDARLLPWK-------SVIDNVGLGlKGQW-----------RDAARRALAAVGLENRAGEWPAALSGGQKQRVA 142
Cdd:PRK10575 79 SSKAFARKVAYLPQQlpaaegmTVRELVAIG-RYPWhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 143 LARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-191 |
2.50e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.47 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPTAGDVlagTTPLAEIQEDtrmmfqdarllpwKSVIDNVGL 103
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---DVPDNQFGRE-------------ASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 104 glkgqwrdaARRALAAVGLENRAG-----EW---PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLI 175
Cdd:COG2401 109 ---------KGDFKDAVELLNAVGlsdavLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*.
gi 447013267 176 VSLWQEHGFTVLLVTH 191
Cdd:COG2401 180 QKLARRAGITLVVATH 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-211 |
2.99e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDTR----MMFQDA-----RLLPWKS 96
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRskvgLVFQDPddqvfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VI---DNVGLGlKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQD 173
Cdd:PRK13647 101 VAfgpVNMGLD-KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 447013267 174 LIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13647 180 ILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-233 |
4.70e-19 |
|
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: 83.23 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLA----EIQEDTRMMFQDarLLpwKSVIDnvGLGLKGQWRDA 112
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD--LL--SSITK--DFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 113 ARRALAAVGL-ENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTH 191
Cdd:cd03237 99 IAKPLQIEQIlDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 192 DVSEAVAMADRVLLIeEGKIGLDLTVDIPRPRRLGSVR-LAEL 233
Cdd:cd03237 175 DIIMIDYLADRLIVF-EGEPSVNGVANPPQSLRSGMNRfLKNL 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-211 |
6.73e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL------ETPTAGDVLAGTTPLAEI-----QEDTRMMFQDARLLPW 94
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIdaiklRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 95 KSVIDNVGLGLKG-------QWRDAARRALAAVGL----ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 163
Cdd:PRK14246 105 LSIYDNIAYPLKShgikekrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 164 DALTRLEMQDLIVSLWQEhgFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-211 |
7.50e-19 |
|
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: 82.16 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTRMMF----QDARLLP------- 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSRIsiipQDPVLFSgtirsnl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 -----------WkSVIDNVGLglkgqwrdAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:cd03244 99 dpfgeysdeelW-QALERVGL--------KEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 163 LDALTRLEMQDLIVSLWQEHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:cd03244 170 VDPETDALIQKTIREAFKDC--TVLTIAHRL-DTIIDSDRILVLDKGRV 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
36-211 |
7.98e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.40 E-value: 7.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 36 AGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL-----AGTTPLAEIQEDTRMMFQDARLLPwKSVIDNVGLGLKGQWR 110
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdIRTVTRASLRRNIAVVFQDAGLFN-RSIEDNIRVGRPDATD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 111 DAARRALAAV-----------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLw 179
Cdd:PRK13657 439 EEMRAAAERAqahdfierkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL- 517
|
170 180 190
....*....|....*....|....*....|..
gi 447013267 180 qEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PRK13657 518 -MKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-191 |
8.11e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMMF---QDArLLPWKSVIDNV 101
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghRNA-MKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GL--GLKGQWRDAARRALAAVGLeNRAGEWPAA-LSGGQKQRVALARALI-HRPgLLLLDEPLGALDALTrlemQDLIVS 177
Cdd:PRK13539 95 EFwaAFLGGEELDIAAALEAVGL-APLAHLPFGyLSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAA----VALFAE 168
|
170
....*....|....*..
gi 447013267 178 LWQEH---GFTVLLVTH 191
Cdd:PRK13539 169 LIRAHlaqGGIVIAATH 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-225 |
1.12e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 8 QGTPLLLNAVSkhyaknivlnQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTP---------LAEI 78
Cdd:PRK13646 14 KGTPYEHQAIH----------DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 79 QEDTRMMFQ--DARLLP---WKSVI---DNVGLGLKgQWRDAARRALAAVGLE-NRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK13646 84 RKRIGMVFQfpESQLFEdtvEREIIfgpKNFKMNLD-EVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 150 RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDIPRPRRL 225
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI-----VSQTSPKEL 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-211 |
1.19e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.77 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE-----IQEDTRMMFQDARLLPwKSVI 98
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQGVAMVQQDPVVLA-DTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 99 DNVGLGL----KGQWRDAARRALAAV------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PRK10790 433 ANVTLGRdiseEQVWQALETVQLAELarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLwQEHGfTVLLVTHDVSEAVAmADRVLLIEEGKI 211
Cdd:PRK10790 513 QAIQQALAAV-REHT-TLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-211 |
1.25e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTT-----PLAEIQEDTRMMFQDARLLPwKSVIDNV 101
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVALVSQNVHLFN-DTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GLGLKGQWRDAARRALAAV------------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:PRK11176 438 AYARTEQYSREQIEEAARMayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQEHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PRK11176 518 AIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEI 556
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-191 |
1.25e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDtrmMFQD-----------ARLL 92
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---YHQDllylghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PWKSVIDNVGLGLKGQwRDAARRALAAVGLENRAgEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDA-----L 166
Cdd:PRK13538 91 ALENLRFYQRLHGPGD-DEALWEALAQVGLAGFE-DVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKqgvarL 168
|
170 180
....*....|....*....|....*
gi 447013267 167 TRLEMQDLivslwqEHGFTVLLVTH 191
Cdd:PRK13538 169 EALLAQHA------EQGGMVILTTH 187
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-214 |
2.93e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNI-VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL------AGTTPLAEIQEDTRMMF 86
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidtGDFSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDARL-LPWKSVIDNVGLGLKG------QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK13644 84 QNPETqFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 160 LGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEaVAMADRVLLIEEGKIGLD 214
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-211 |
3.53e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 22 AKNIVLNQLDLHIPAGQFVAVVGRSGGGKST----LLRLLAgletpTAGDVLAGTTPLAeiQEDTRMM----------FQ 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLH--NLNRRQLlpvrhriqvvFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 D--ARLLPWKSVIDNVGLGLK--------GQWRDAARRALAAVGL--ENRAgEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK15134 370 DpnSSLNPRLNVLQIIEEGLRvhqptlsaAQREQQVIAVMEEVGLdpETRH-RYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-223 |
9.62e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 9 GTPLLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTP------------LA 76
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrrVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 77 EIQEDTRMMFQ--------------DARLLPWKSVIDNVglglkgqwrdaARRALAAVGLENRAGEWPAALSGGQKQRVA 142
Cdd:PRK09536 81 SVPQDTSLSFEfdvrqvvemgrtphRSRFDTWTETDRAA-----------VERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 143 LARALIHRPGLLLLDEPLGALD---ALTRLEM-QDLIvslwqEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVD 218
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDinhQVRTLELvRRLV-----DDGKTAVAAIHDLDLAARYCDELVLLADGRV-----RA 219
|
....*
gi 447013267 219 IPRPR 223
Cdd:PRK09536 220 AGPPA 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-203 |
2.02e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 9 GTPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL------AGTTPLAEIQED 81
Cdd:COG3845 2 MPPALeLRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 TRMMFQDARLLPWKSVIDNVGLGLKGQWRDAARRALAAVGLENRAGEW-----PAA----LSGGQKQRVALARALIHRPG 152
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYgldvdPDAkvedLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 153 LLLLDEPLGaldALTRLEMQDLIVSLWQ--EHGFTVLLVTHDVSEAVAMADRV 203
Cdd:COG3845 162 ILILDEPTA---VLTPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRV 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-204 |
2.77e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.94 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG--DVLAGttPLAEIQEDTRMMFQDA-- 89
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrvEVLGG--DMADARHRRAVCPRIAym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 ------RLLPWKSVIDNV-------GLGlKGQWRDAARRALAAVGLE---NRagewPAA-LSGGQKQRVALARALIHRPG 152
Cdd:NF033858 82 pqglgkNLYPTLSVFENLdffgrlfGQD-AAERRRRIDELLRATGLApfaDR----PAGkLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIVSLWQEH-GFTVLLVTHDVSEA------VAM-ADRVL 204
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAerfdwlVAMdAGRVL 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-201 |
3.18e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL-----ETPTAGDVLAGTTPLAE-------IQED 81
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYErrvnlnrLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 TRMMFQDARLLPwKSVIDNVGLGLK-GQWRDAARRALAAVGLENRAGEWPAA----------LSGGQKQRVALARALIHR 150
Cdd:PRK14258 90 VSMVHPKPNLFP-MSVYDNVAYGVKiVGWRPKLEIDDIVESALKDADLWDEIkhkihksaldLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMAD 201
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-211 |
3.40e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.83 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG----TTPLAEIQEDTRMMFQDARLLPWKSVIDNVG 102
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgkdiETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 103 L--GLKGQ-WRDAARRALAAV---GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIv 176
Cdd:TIGR01257 1026 FyaQLKGRsWEEAQLEMEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104
|
170 180 190
....*....|....*....|....*....|....*
gi 447013267 177 sLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:TIGR01257 1105 -LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-239 |
6.93e-17 |
|
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: 79.46 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLET--PTAGDVL-----------------AGT----- 72
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskVGEpcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 73 -TPLAEIQED---------------TRMMFQDA-RLLPWKSVIDNV-----GLGLKGQWRDAARR-ALAAVGLENRAGEW 129
Cdd:TIGR03269 86 gGTLEPEEVDfwnlsdklrrrirkrIAIMLQRTfALYGDDTVLDNVlealeEIGYEGKEAVGRAVdLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 130 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
250 260 270
....*....|....*....|....*....|
gi 447013267 210 KIGLDLTVDIPRPRRLGSVRLAELEAEVLQ 239
Cdd:TIGR03269 246 EIKEEGTPDEVVAVFMEGVSEVEKECEVEV 275
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-204 |
1.10e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL------AGTTPlAEIQEDTRMMFQ 87
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklrIGYVP-QKLYLDTTLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWKSvidnvglGLKGQWRDAARRALAAVGLENRAGEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PRK09544 86 VNRFLRLRP-------GTKKEDILPALKRVQAGHLIDAPMQ---KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 168 RLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVL 204
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-211 |
1.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG--------TTPLAEIQEDTR-------------M 84
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPYSKkiknfkelrrrvsM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 85 MFQDARLLPWKSVIDN------VGLGL-KGQWRDAARRALAAVGLENRAGEW-PAALSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKdimfgpVALGVkKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447013267 157 DEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-210 |
2.10e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKS-TLLRLLAGLETP----TAGDVLAGTTPLAEIQEDT---------RMMFQD--A 89
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTlrgvrgnkiAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 90 RLLPW----KSVIDNVGL--GLKGQWRDAARRA-LAAVGLEN---RAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK15134 104 SLNPLhtleKQLYEVLSLhrGMRREAARGEILNcLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 160 LGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-191 |
2.48e-16 |
|
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: 74.84 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE----IQEDTRMMFQDARLLPWKSVIDNV 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrdsIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GLGLKGQWRDAARRALAAVGLeNRAGEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrlemQDLIVSLWQ 180
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGL-NGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG----VARFAEAMA 169
|
170
....*....|....
gi 447013267 181 EH---GFTVLLVTH 191
Cdd:cd03231 170 GHcarGGMVVLTTH 183
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-209 |
3.65e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 75.06 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-----LAGTTPLAEIQEDTRMMFQDARLLPW---KSVI 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWllnATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 99 DNVGLGL---KGQWRDAARRALAA-------VGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LT 167
Cdd:cd03290 97 ENITFGSpfnKQRYKAVTDACSLQpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 168 RLEMQDLIVSLWQEHGFTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:cd03290 177 DHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-211 |
4.35e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG--TTPLAEIQ---------- 79
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNgrVSALLELGagfhpeltgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRMMfqdARLL-----PWKSVIDNV----GLG------LKgqwrdaarralaavglenragewpaALSGGQKQRVALA 144
Cdd:COG1134 107 ENIYLN---GRLLglsrkEIDEKFDEIvefaELGdfidqpVK-------------------------TYSSGMRARLAFA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 145 RALIHRPGLLLLDEPLGALDA------LTRleMQDLIvslwqEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAafqkkcLAR--IRELR-----ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-211 |
5.02e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.12 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHIPAGQFVAVVGRSGGGKS----TLLRLLAGLETPTAGDVLAGTTPL----------AEIQEDTRMMFQDARLLPWK 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVapcalrgrkiATIMQNPRSAFNPLHTMHTH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDNVGLGLKGQwRDAARRALAAVGLENRA---GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQ 172
Cdd:PRK10418 102 ARETCLALGKPAD-DATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARIL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 173 DLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10418 181 DLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-211 |
1.76e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 73.61 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED--TRMM----FQDARLLPWKSVIDN 100
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHeiARLGigrkFQKPTVFEELTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VGLGLKGQ---WRDAARRALA-----------AVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGaldAL 166
Cdd:COG4674 106 LELALKGDrgvFASLFARLTAeerdrieevleTIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVA---GM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 167 TRLEMQ---DLIVSLWQEHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4674 183 TDAETErtaELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-211 |
4.20e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.60 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-----LAGTTPLAEIQEDT---RMMFQDARLLP-WKSV 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVhmkgsVAYVPQQAWIQNDSlreNILFGKALNEKyYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 IDNVGLglkgqwrdAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRLEMQDLIV 176
Cdd:TIGR00957 734 LEACAL--------LPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIG 805
|
170 180 190
....*....|....*....|....*....|....*
gi 447013267 177 SLWQEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR00957 806 PEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKI 839
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-211 |
4.73e-15 |
|
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: 71.92 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL---ETPTAGDVLAGTTPL--AEIQEDTRMMFQDARLLPWKSVID 99
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRkpDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NV--GLGLKGQWR--------DAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:cd03234 101 TLtyTAILRLPRKssdairkkRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447013267 170 emqDLIVSLWQ--EHGFTVLLVTHD-VSEAVAMADRVLLIEEGKI 211
Cdd:cd03234 181 ---NLVSTLSQlaRRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-211 |
6.13e-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: 71.02 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPTAGDVLAGTTPLAEIQEDTR------MMFQDARLLPWKSV 97
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlgifLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 ID---NVGLGlkgqwrdaarralaavglenragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRLEMQDL 174
Cdd:cd03217 95 ADflrYVNEG----------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVAE 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 447013267 175 IVSLWQEHGFTVLLVTH--DVSEAVAmADRVLLIEEGKI 211
Cdd:cd03217 146 VINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRI 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-192 |
7.75e-15 |
|
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: 73.43 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 14 LNAVSKHY-AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDvlagttplAEIQEDTR--MMFQDAR 90
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGIKvgYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLGLK----------------------------------------GQWRDAARRALAAVGLENRAGEWP 130
Cdd:TIGR03719 79 LDPTKTVRENVEEGVAeikdaldrfneisakyaepdadfdklaaeqaelqeiidaaDAWDLDSQLEIAMDALRCPPWDAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 131 AA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrlemqdliVSlWQEHGF-----TVLLVTHD 192
Cdd:TIGR03719 159 VTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES--------VA-WLERHLqeypgTVVAVTHD 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-212 |
1.01e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.21 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 20 HY--AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQED-----------TRMMF 86
Cdd:PRK10789 322 TYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsrlavvsqTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 QDarllpwkSVIDNVGLGLKG--QWRDAARRALAAV---------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK10789 402 SD-------TVANNIALGRPDatQQEIEHVARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 156 LDEPLGALDALTRLE-MQDLivSLWQEhGFTVLLVTHDVSeAVAMADRVLLIEEGKIG 212
Cdd:PRK10789 475 LDDALSAVDGRTEHQiLHNL--RQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-191 |
1.58e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 21 YAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVL----AGTTPLAEIQEDTRMMFQDARLLPWKS 96
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDNVGLGLKGQWRDAARRALAAVGLENRAGEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLemqdLI 175
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL----TI 166
|
170
....*....|....*....
gi 447013267 176 VSLWQEH---GFTVLLVTH 191
Cdd:PRK13540 167 ITKIQEHrakGGAVLLTSH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-211 |
1.89e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRM------M 85
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgigyL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGL-------KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLqirddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-209 |
2.57e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLLLNAVSKHYA--KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD-VLAGTTPLAEIQEdtr 83
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILTNISD--- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 mMFQDARLLPWKSVIDNVGLG---------LKG----QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHR 150
Cdd:TIGR01257 2010 -VHQNMGYCPQFDAIDDLLTGrehlylyarLRGvpaeEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 151 PGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-255 |
4.18e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG-----TTPLAEIQ---EDTRMMFQD--ARLLPWKSVIDNV----- 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridTLSPGKLQalrRDIQFIFQDpyASLDPRQTVGDSImeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 --GLGLKGQWRDAARRALAAVGLE-NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSL 178
Cdd:PRK10261 430 vhGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 179 WQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDIPrPRR--------------LGSVRLAELEAEVLQRVMQR 244
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQI-----VEIG-PRRavfenpqhpytrklMAAVPVADPSRQRPQRVLLS 583
|
250
....*....|.
gi 447013267 245 GESETRLRKQG 255
Cdd:PRK10261 584 DDLPSNIHLRG 594
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-210 |
5.10e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 28 NQLDLHIPAGQFVAVVGRSGGGKS----TLLRLLA--GLETPTA---GDVLAGttpLAEIQ------EDTRMMFQD--AR 90
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGGSAtfnGREILN---LPEKElnklraEQISMIFQDpmTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNV--------GLGlKGQWRDAARRALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:PRK09473 110 LNPYMRVGEQLmevlmlhkGMS-KAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 160 LGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-213 |
6.11e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV------LAGTTPLAEIQ 79
Cdd:PRK15439 6 TTAPPLLcARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRMMFQDARLLPWKSVIDNVGLGL------KGQWRDAARRALAAVGLENRAGewpaALSGGQKQRVALARALIHRPGL 153
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLpkrqasMQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 154 LLLDEPLGaldALTRLEMQDL---IVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 213
Cdd:PRK15439 162 LILDEPTA---SLTPAETERLfsrIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-211 |
8.05e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 30 LDLHipAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAG-----TTPLAEIQ-------EDtrmmfqdaR----LL 92
Cdd:COG1129 273 FSVR--AGEILGIAGLVGAGRTELARALFGADPADSGEIrLDGkpvriRSPRDAIRagiayvpED--------RkgegLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PWKSVIDNVGLGLKGQWRDAarralaavGLENRAGEWPAA--------------------LSGGQKQRVALARALIHRPG 152
Cdd:COG1129 343 LDLSIRENITLASLDRLSRG--------GLLDRRRERALAeeyikrlriktpspeqpvgnLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447013267 153 LLLLDEP-----LGAldaltRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG1129 415 VLILDEPtrgidVGA-----KAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-209 |
1.09e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 69.12 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGdvlagttplaEIQEDTRMMF--QDARLLPwKSVIDNVGL 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG----------KIKHSGRISFssQFSWIMP-GTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 104 GLKGQWRDAARRALAAVGLENRA----------GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQD 173
Cdd:cd03291 121 GVSYDEYRYKSVVKACQLEEDITkfpekdntvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170 180 190
....*....|....*....|....*....|....*.
gi 447013267 174 LIVSLWQEHGfTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:cd03291 201 SCVCKLMANK-TRILVTSKM-EHLKKADKILILHEG 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-211 |
1.24e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 21 YAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-------AEIQEDTRMMFQDARLLP 93
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrglLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKSVID--------NVGLGlKGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK13638 91 FYTDIDsdiafslrNLGVP-EAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 166 LTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-210 |
1.31e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--ETPTAGDVLAGTTPL--AEIQEDTR---- 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERagiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 MMFQDARLLPWKSVIDNVGLG----LKGQWRDAARRALAAVGL--ENRAGEWPAA-----LSGGQKQRVALARALIHRPG 152
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLlrELQLDADNVTrpvgdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 153 LLLLDEPLGaldALTRLEMQDL--IVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:TIGR02633 162 LLILDEPSS---SLTEKETEILldIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-207 |
1.35e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLLLNAVSKHYAKNI--VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPlAEIQEDTRMMFQ 87
Cdd:PRK13543 8 APPLLAAHALAFSRNEepVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 DARLLPWK---SVIDNVGL--GLKGQWRDAA-RRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK13543 87 LGHLPGLKadlSTLENLHFlcGLHGRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 162 ALDaLTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIE 207
Cdd:PRK13543 167 NLD-LEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-211 |
1.62e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 19 KHYAKNIvlnqlDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP---TAGDVLAGTTPL---------AEIQED----- 81
Cdd:TIGR00955 38 KHLLKNV-----SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIdakemraisAYVQQDdlfip 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 ---TR--MMFQ-----------DARLLPWKSVIDNVGLgLKGQwrdaarraLAAVGLENRAgewpAALSGGQKQRVALAR 145
Cdd:TIGR00955 113 tltVRehLMFQahlrmprrvtkKEKRERVDEVLQALGL-RKCA--------NTRIGVPGRV----KGLSGGERKRLAFAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 146 ALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHD-VSEAVAMADRVLLIEEGKI 211
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-222 |
1.71e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 13 LLNAVSKHYAK--NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAG-LETPTA-------GDVLAGTTPLAEIqeDT 82
Cdd:PRK13547 1 MLTADHLHVARrhRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAI--DA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMFQDARLLPWK-------SVIDNVGLGLKGQWRDAARRALAAVGLENRAGEWPAA----------LSGGQKQRVALAR 145
Cdd:PRK13547 79 PRLARLRAVLPQAaqpafafSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGAtalvgrdvttLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 146 AL---------IHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
....*..
gi 447013267 217 V-DIPRP 222
Cdd:PRK13547 239 PaDVLTP 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
133-211 |
1.72e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.72e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-211 |
2.50e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTpLAEIQEDTRMM----------FQDARLLPW 94
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-IAYVPQQAWIMnatvrgnilfFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 95 KSVIDNVGLglkgqwrdAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRLEMQD 173
Cdd:PTZ00243 753 ADAVRVSQL--------EADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEE 824
|
170 180 190
....*....|....*....|....*....|....*...
gi 447013267 174 LIvsLWQEHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:PTZ00243 825 CF--LGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-210 |
4.22e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--ETPTAGDVLA-GTTPLAEIQEDTRMMFQDARLLPWKSVIDN-V 101
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILAnNRKPTKQILKRTGFVTQDDILYPHLTVRETlV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GLGL--------KGQWRDAARRALAAVGL---ENR--AGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PLN03211 163 FCSLlrlpksltKQEKILVAESVISELGLtkcENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQEhGFTVLLVTHDVSEAV-AMADRVLLIEEGK 210
Cdd:PLN03211 243 YRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGR 284
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-211 |
4.48e-13 |
|
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: 66.28 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 21 YAKNI--VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAG-----DVLAGTTPLAEIQEDTRMMFQDARLLP 93
Cdd:cd03369 16 YAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGkieidGIDISTIPLEDLRSSLTIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 wKSVIDNvgLGLKGQWRDAARRALAAV--GLENragewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:cd03369 96 -GTIRSN--LDPFDEYSDEEIYGALRVseGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447013267 172 QDLIVSLWQehGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03369 165 QKTIREEFT--NSTILTIAHRLR-TIIDYDKILVMDAGEV 201
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-211 |
6.59e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.89 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAE--------IQ 79
Cdd:PRK10636 310 NPLLkMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYfaqhqlefLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRMMFQDARLLPW---KSVIDNVG-LGLKGqwrdaarralaavgleNRAGEWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK10636 390 ADESPLQHLARLAPQeleQKLRDYLGgFGFQG----------------DKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447013267 156 LDEPLGALDaltrLEM-QDLIVSLWQEHGFTVlLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10636 454 LDEPTNHLD----LDMrQALTEALIDFEGALV-VVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
127-210 |
7.71e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 127 GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLI 206
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
....
gi 447013267 207 EEGK 210
Cdd:PRK10261 243 YQGE 246
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
42-192 |
8.78e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 42 VVGRSGGGKSTLLRLLAGLETPTAGDvlagttplAEIQEDTR--MMFQDARLLPWKSVIDNVGLGL-------------- 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAPGIKvgYLPQEPQLDPEKTVRENVEEGVaevkaaldrfneiy 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 106 --------------------------KGQWRdaarralaavgLENR-----------AGEWPAA-LSGGQKQRVALARAL 147
Cdd:PRK11819 110 aayaepdadfdalaaeqgelqeiidaADAWD-----------LDSQleiamdalrcpPWDAKVTkLSGGERRRVALCRLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 148 IHRPGLLLLDEPLGALDALTrlemqdlivSLWQEH------GfTVLLVTHD 192
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLDAES---------VAWLEQflhdypG-TVVAVTHD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-212 |
9.03e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 34 IPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTT----PlAEIQEDTRMMFQDarLL----------PWKSVID 99
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykP-QYIKPDYDGTVED--LLrsitddlgssYYKSEII 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NvGLGLKGQwrdaarralaavgLENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:PRK13409 439 K-PLQLERL-------------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170 180 190
....*....|....*....|....*....|....*
gi 447013267 180 QEHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIG 212
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYISDRLMVFegEPGKHG 535
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-211 |
1.10e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 5 RLNQGTPLLLNAV-----SKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEI 78
Cdd:PRK15064 308 RFEQDKKLHRNALevenlTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 79 QEDTRMMF-QDARLLPWKSvidnvglglkgQWRDAARRALAAVGLENR-------AGEWPAALSGGQKQRVALARALIHR 150
Cdd:PRK15064 388 AQDHAYDFeNDLTLFDWMS-----------QWRQEGDDEQAVRGTLGRllfsqddIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 151 PGLLLLDEPLGALD-----AL-TRLEMQDlivslwqehGfTVLLVTHD---VSeavAMADRVLLIEEGKI 211
Cdd:PRK15064 457 PNVLVMDEPTNHMDmesieSLnMALEKYE---------G-TLIFVSHDrefVS---SLATRIIEITPDGV 513
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
122-218 |
1.49e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.30 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 122 LENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMAD 201
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAH 212
|
90
....*....|....*..
gi 447013267 202 RVLLIEEGKIGLDLTVD 218
Cdd:NF000106 213 ELTVIDRGRVIADGKVD 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-192 |
1.60e-12 |
|
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: 66.50 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 15 NAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG-TTPLAEIQEdtrmmFQDArLLP 93
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGeTVKLAYVDQ-----SRDA-LDP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKSVIDNVGLGL---------------------KGQwrdaarralaavGLENRAGEwpaaLSGGQKQRVALARALIHRPG 152
Cdd:TIGR03719 400 NKTVWEEISGGLdiiklgkreipsrayvgrfnfKGS------------DQQKKVGQ----LSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIvslwQEHGFTVLLVTHD 192
Cdd:TIGR03719 464 VLLLDEPTNDLDVETLRALEEAL----LNFAGCAVVISHD 499
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-226 |
1.61e-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: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 34 IPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVlagttplaeiqedtrmmfqdarllPWksviDNVGLGLKGQWRdaa 113
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND------------------------EW----DGITPVYKPQYI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 114 rralaavglenragewpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDV 193
Cdd:cd03222 71 ------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 194 SEAVAMADRVLLIeEGKIGLDLTVDIPRPRRLG 226
Cdd:cd03222 133 AVLDYLSDRIHVF-EGEPGVYGIASQPKGTREG 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-209 |
1.74e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.86 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGdvlagttplaEIQEDTRMMF--QDARLLPwKSVIDNVGL 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG----------KIKHSGRISFspQTSWIMP-GTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 104 GLKGQWRDAARRALAAVGLENRA----------GEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM-Q 172
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQLEEDIAlfpekdktvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfE 589
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 173 DLIVSLWQEHgfTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:TIGR01271 590 SCLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-191 |
2.03e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.31 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeTPTAGDVLA------------------GTTPLAEIQEDTRMMF 86
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTkpakgklfyvpqrpymtlGTLRDQIIYPDSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 Q-----DARLlpwKSVIDNVGLGlkgqwrdaaRRALAAVGLENRAgEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:TIGR00954 545 KrrglsDKDL---EQILDNVQLT---------HILEREGGWSAVQ-DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 447013267 162 ALDaltrLEMQDLIVSLWQEHGFTVLLVTH 191
Cdd:TIGR00954 612 AVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
37-192 |
2.28e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTplAEIQedtrmMFQDAR--LLPWKSVIDNVGLGLK-----GQW 109
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK--LEVA-----YFDQHRaeLDPEKTVMDNLAEGKQevmvnGRP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 110 RDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrLEmqdLIVSLWQEHGFTVLLV 189
Cdd:PRK11147 418 RHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-LE---LLEELLDSYQGTVLLV 493
|
...
gi 447013267 190 THD 192
Cdd:PRK11147 494 SHD 496
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-211 |
2.70e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKN-IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL-AEIQEDTRMMFQ-- 87
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSav 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 88 -------DARLLPWKSVIDNVglgLKGQWRDAARRALAAVGLENRAGEwpAALSGGQKQRVALARALIHRPGLLLLDEPL 160
Cdd:PRK10522 403 ftdfhlfDQLLGPEGKPANPA---LVEKWLERLKMAHKLELEDGRISN--LKLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 161 GALDALTRLEMQDLIVSLWQEHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 211
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-211 |
6.32e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKS-TLLRLLAGLETPtaGDVLAGT-----TPLAEIQEDTR---------MMFQDA--RLLPWKSV-- 97
Cdd:PRK11022 33 GEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKlefngQDLQRISEKERrnlvgaevaMIFQDPmtSLNPCYTVgf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 -----IDNVGLGLKGQWRDAARRALAAVGL---ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRL 169
Cdd:PRK11022 111 qimeaIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 170 EMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK11022 191 QIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
131-215 |
8.68e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 131 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
....*
gi 447013267 211 IGLDL 215
Cdd:PRK13549 483 LKGDL 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
131-215 |
1.06e-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: 64.08 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 131 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
....*
gi 447013267 211 IGLDL 215
Cdd:TIGR02633 481 LKGDF 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-211 |
1.15e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLLLNAvskhyaknivlnqlDLHIPAGQFVAVVGRSGGGKSTLLRLLAG--------------------------LETP 63
Cdd:PRK11147 16 APLLDNA--------------ELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdpprNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 64 TAGD-VLAGTTPLAEIQED-------------TRMMFQDARLlpwKSVIDNVGLglkgqWRDAARRALAAVGLENRAGEW 129
Cdd:PRK11147 82 TVYDfVAEGIEEQAEYLKRyhdishlvetdpsEKNLNELAKL---QEQLDHHNL-----WQLENRINEVLAQLGLDPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 130 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltrlemqDLIVslWQEhGF------TVLLVTHDVSEAVAMADRV 203
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIE--WLE-GFlktfqgSIIFISHDRSFIRNMATRI 223
|
....*...
gi 447013267 204 LLIEEGKI 211
Cdd:PRK11147 224 VDLDRGKL 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-211 |
2.38e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.78 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 36 AGQFVAVVGRSGGGKSTLLRLLAGLeTPTAGDVLAGTTPLAE--IQEDTR---MMFQDARLLPWKSVIDNVGLGLKGQWR 110
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwsAAELARhraYLSQQQSPPFAMPVFQYLALHQPAGAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 111 DAARRALAAV-----GLENRAGEWPAALSGGQKQRVALARAL------IHRPG-LLLLDEPLGALDALTRLEMQDLIVSL 178
Cdd:COG4138 100 SEAVEQLLAQlaealGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINPEGqLLLLDEPMNSLDVAQQAALDRLLREL 179
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 179 WQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG4138 180 CQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-211 |
2.94e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP--TAGDVLAGTTPLAEiqedtrmmfqdarLLPW---KSVI 98
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRGSVAYVP-------------QVSWifnATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 99 DNVGLGLK---GQWRDAARRALAAVGLE-------NRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PLN03232 697 ENILFGSDfesERYWRAIDVTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSlWQEHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:PLN03232 777 HQVFDSCMK-DELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-194 |
3.81e-11 |
|
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: 61.61 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 32 LHIPA-GQFVAVVGRSGGGKSTLLRLLAGLETPTAG---------DVL---AGT------TPLAEIQEDTRMMFQDARLL 92
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdefRGSelqnyfTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PwKSVIDNVGLGL-KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEM 171
Cdd:cd03236 100 P-KAVKGKVGELLkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|...
gi 447013267 172 QDLIVSLwQEHGFTVLLVTHDVS 194
Cdd:cd03236 179 ARLIREL-AEDDNYVLVVEHDLA 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
133-216 |
4.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
....
gi 447013267 213 LDLT 216
Cdd:PRK15439 483 GALT 486
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-210 |
5.95e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 23 KNIV--------LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL--------ETPTAGDVLAGTTplaeIQEDTR--- 83
Cdd:PRK13549 9 KNITktfggvkaLDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQASN----IRDTERagi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 -MMFQDARLLPWKSVIDNVGLGlkGQWRDAARRALAAVGLenRAGEW---------PAA----LSGGQKQRVALARALIH 149
Cdd:PRK13549 85 aIIHQELALVKELSVLENIFLG--NEITPGGIMDYDAMYL--RAQKLlaqlkldinPATpvgnLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 150 RPGLLLLDEPLGaldALTRLEMQDL--IVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK13549 161 QARLLILDEPTA---SLTESETAVLldIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-211 |
9.93e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTR----MMFQDARLL------ 92
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRfkitIIPQDPVLFsgslrm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 ---PWKSVIDNvglglKGQWRDAARRALAAV-----GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 164
Cdd:TIGR00957 1379 nldPFSQYSDE-----EVWWALELAHLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447013267 165 altrLEMQDLIVSL--WQEHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:TIGR00957 1454 ----LETDNLIQSTirTQFEDCTVLTIAHRLN-TIMDYTRVIVLDKGEV 1497
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-166 |
1.29e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVlagttplaEIQEDTRMMFQD---ARLLP 93
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI--------KIGETVKLAYVDqsrDALDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 94 WKSVIDNVGLGL---------------------KG--QwrdaarralaavglENRAGEwpaaLSGGQKQRVALARALIHR 150
Cdd:PRK11819 402 NKTVWEEISGGLdiikvgnreipsrayvgrfnfKGgdQ--------------QKKVGV----LSGGERNRLHLAKTLKQG 463
|
170 180
....*....|....*....|....*
gi 447013267 151 PGLLLLDEP--------LGAL-DAL 166
Cdd:PRK11819 464 GNVLLLDEPtndldvetLRALeEAL 488
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-210 |
1.83e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 36 AGQFVAVVGRSGGGKSTLLRLLAGLeTPTAGDVLAGTTPLAEIQ--EDTRM---MFQDARLLPWKSVIDNVGLGL----- 105
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSaaELARHrayLSQQQTPPFAMPVFQYLTLHQpdktr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 106 KGQWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARAL--IHRPG-----LLLLDEPLGALD-----ALtrlemqD 173
Cdd:PRK03695 100 TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWPDInpagqLLLLDEPMNSLDvaqqaAL------D 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 447013267 174 LIVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-211 |
2.26e-10 |
|
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: 58.43 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTA---GDVLAGTTPLAEIQE----DTRMMFQDARLLPWKSVID 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEkypgEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 NVGLGLKGQwrdaarralaavGLENRAGewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:cd03233 103 TLDFALRCK------------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMA 165
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 180 QEHGFTVLLVTHDVS-EAVAMADRVLLIEEGKI 211
Cdd:cd03233 166 DVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQ 198
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-202 |
2.28e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEDTRMmfqdarllpwksvidnvglglkgqwrdaarra 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 117 laavgLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW-----QEHGFTVLLVTH 191
Cdd:smart00382 50 -----LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkSEKNLTVILTTN 124
|
170
....*....|.
gi 447013267 192 DVSEAVAMADR 202
Cdd:smart00382 125 DEKDLGPALLR 135
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-230 |
2.34e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 12 LLLNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL------AEIQEDTRMM 85
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 86 FQDARLLPWKSVIDNVGLGL---KGQWRDAARRALAAVGLENRAGEW--PAA----LSGGQKQRVALARALIHRPGLLLL 156
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVDidPDTplkyLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 157 DEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGK--------------------IGLDLT 216
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRyvatfddmaqvdrdqlvqamVGREIG 243
|
250
....*....|....*.
gi 447013267 217 vDIP--RPRRLGSVRL 230
Cdd:PRK11288 244 -DIYgyRPRPLGEVRL 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-211 |
3.67e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 7 NQGTPLLLNAVSKHY-AKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETpTAGdvlagttplaEIQED---- 81
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEG----------EIQIDgvsw 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 82 TRMMFQDAR----LLPWKSVIDN----VGLGLKGQWRDAAR-RALAAVGLENRAGEWPA-----------ALSGGQKQRV 141
Cdd:TIGR01271 1283 NSVTLQTWRkafgVIPQKVFIFSgtfrKNLDPYEQWSDEEIwKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLM 1362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447013267 142 ALARALIHRPGLLLLDEPLGALDALTrleMQDLIVSLwqEHGF---TVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVT---LQIIRKTL--KQSFsncTVILSEHRV-EALLECQQFLVIEGSSV 1429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-193 |
4.08e-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: 59.41 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTT----PlAEIQEDTRMMFQDarLL-----------PWKSVIDNv 101
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykP-QYISPDYDGTVEE--FLrsantddfgssYYKTEIIK- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 GLGLKGQwrdaarralaavgLENRAGEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQE 181
Cdd:COG1245 442 PLGLEKL-------------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|..
gi 447013267 182 HGFTVLLVTHDV 193
Cdd:COG1245 505 RGKTAMVVDHDI 516
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
121-220 |
4.25e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 121 GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAvAMA 200
Cdd:NF033858 386 DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERC 464
|
90 100
....*....|....*....|
gi 447013267 201 DRVLLIEEGKIgldLTVDIP 220
Cdd:NF033858 465 DRISLMHAGRV---LASDTP 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-205 |
4.87e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 123 ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSeAVAMADR 202
Cdd:PTZ00265 1349 DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDK 1427
|
...
gi 447013267 203 VLL 205
Cdd:PTZ00265 1428 IVV 1430
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-211 |
5.78e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.88 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV------LAGTTP-------LAEIQEDtRMmfQDArLL 92
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrldgedITGLSPrerrrlgVAYIPED-RL--GRG-LV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 PWKSVIDNVGLGLKGQWRDAARRALAAVGLENRAGEW-------------PA-ALSGGQKQRVALARALIHRPGLLLLDE 158
Cdd:COG3845 349 PDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELieefdvrtpgpdtPArSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 159 PLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-203 |
6.17e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.38 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP----TA-----GDV-LAGTTPLAE---IQEDTRMMFQDAR-- 90
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTAdrfrwNGIdLLKLSPRERrkiIGREIAMIFQEPSsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNV-----GLGLKGQ-WRDAARRALAAVGLENRAG---------EWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:COG4170 102 LDPSAKIGDQLieaipSWTFKGKwWQRFKWRKKRAIELLHRVGikdhkdimnSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRV 203
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-216 |
6.25e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 32 LHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV------LAGTTPLAEIQ-------EDTRmmfQDArLLPWKSVI 98
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVyldgkpIDIRSPRDAIRagimlcpEDRK---AEG-IIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 99 DNV-----------GLGLKGQW-RDAARRALAAVGLENRAGEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK11288 350 DNInisarrhhlraGCLINNRWeAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 166 LTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 216
Cdd:PRK11288 430 GAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-194 |
9.51e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.18 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIvlNQLDLHIPAGQFVAVVGRSGGGKSTLLrlLAGLETpTAGDVLAGTTPLAEiqeDTRMMFQDArllpWKS 96
Cdd:cd03238 3 VSGANVHNL--QNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA-SGKARLISFLPKFS---RNKLIFIDQ----LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 97 VIDnVGLGLkgqwrdaarralaaVGLENRAGewpaALSGGQKQRVALARALIHRPG--LLLLDEPLGALDALTRLEMQDL 174
Cdd:cd03238 71 LID-VGLGY--------------LTLGQKLS----TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180
....*....|....*....|
gi 447013267 175 IVSLWQEhGFTVLLVTHDVS 194
Cdd:cd03238 132 IKGLIDL-GNTVILIEHNLD 150
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-211 |
1.04e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGlETPTAGD---VLAGTTPL---------AEIQEDTRM--MFQDARll 92
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRSDasvVIRGTVAYvpqvswifnATVRDNILFgsPFDPER-- 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 pWKSVIDNVGLG-----LKGqwrdaarralaavGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 167
Cdd:PLN03130 710 -YERAIDVTALQhdldlLPG-------------GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447013267 168 RLEMQDLIVSlWQEHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:PLN03130 776 GRQVFDKCIK-DELRGKTRVLVTNQL-HFLSQVDRIILVHEGMI 817
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-209 |
1.35e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 10 TPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGT-----TPLAEIQEDT 82
Cdd:PRK09700 3 TPYIsMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItINNInynklDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMFQDARLLPWKSVIDNVGLG---LKGQW----------RDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIH 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGrhlTKKVCgvniidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 150 RPGLLLLDEPlgaLDALTRLEMQDL--IVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEG 209
Cdd:PRK09700 163 DAKVIIMDEP---TSSLTNKEVDYLflIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-203 |
1.45e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP----TA-----GDV-LAGTTPLAE---IQEDTRMMFQDAR-- 90
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTAdrmrfDDIdLLRLSPRERrklVGHNVSMIFQEPQsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSV----IDNV-GLGLKGQWRDAAR-RALAAVGLENRAG---------EWPAALSGGQKQRVALARALIHRPGLLL 155
Cdd:PRK15093 102 LDPSERVgrqlMQNIpGWTYKGRWWQRFGwRKRRAIELLHRVGikdhkdamrSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447013267 156 LDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVAMADRV 203
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-211 |
1.69e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.79 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETpTAGDvlagttplaeIQED----TRMMFQDAR----LLPWK 95
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGD----------IQIDgvswNSVPLQKWRkafgVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 96 SVIDN----VGLGLKGQWRDAAR-RALAAVGLENRAGEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:cd03289 86 VFIFSgtfrKNLDPYGKWSDEEIwKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447013267 160 LGALDALTrleMQDLIVSLWQEH-GFTVLLVTHDVsEAVAMADRVLLIEEGKI 211
Cdd:cd03289 166 SAHLDPIT---YQVIRKTLKQAFaDCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-207 |
2.54e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 34 IPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAE-IQEDTRMMFQDARLLPWKS---VIDNVGLGLKGQ- 108
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVAYVPQSEEVDWSFpvlVEDVVMMGRYGHm 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 109 -WR--------DAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:PRK15056 110 gWLrrakkrdrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR 189
|
170 180
....*....|....*....|....*...
gi 447013267 180 QEhGFTVLLVTHDVSEAVAMADRVLLIE 207
Cdd:PRK15056 190 DE-GKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-209 |
8.90e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.79 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP--TAGDVLAGTTPL-AEIQEDTRMMFQDARLLPWKSVIdnvgl 103
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLdKNFQRSTGYVEQQDVHSPNLTVR----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 104 glkgqwrdaarralaaVGLENRAgeWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLwQEHG 183
Cdd:cd03232 98 ----------------EALRFSA--LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSG 158
|
170 180
....*....|....*....|....*..
gi 447013267 184 FTVLLVTHDVSEAV-AMADRVLLIEEG 209
Cdd:cd03232 159 QAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-211 |
1.93e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 5 RLNQGTPLL-LNAVSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGlETPT--AGDVL-------AGTTp 74
Cdd:PRK10938 253 ALPANEPRIvLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTlfgrrrgSGET- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 75 LAEIQED----TRMMFQDARL-LPWKSVI-----DNVGL---------GLKGQWRDAarralaaVGLENRAGEWP-AALS 134
Cdd:PRK10938 331 IWDIKKHigyvSSSLHLDYRVsTSVRNVIlsgffDSIGIyqavsdrqqKLAQQWLDI-------LGIDKRTADAPfHSLS 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 135 GGQkQRVAL-ARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSEAVA-MADRVLLIEEGKI 211
Cdd:PRK10938 404 WGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-219 |
2.09e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 123 ENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEHGFTVLLVTHDVSeAVAMADR 202
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANT 648
|
90
....*....|....*..
gi 447013267 203 VLLIEEGKIGLDLTVDI 219
Cdd:PTZ00265 649 IFVLSNRERGSTVDVDI 665
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-211 |
2.14e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 40 VAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG-------------------TTPLAeiqedtrMMFQDARLLPWKSVIDN 100
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSakvrmavfsqhhvdgldlsSNPLL-------YMMRCFPGVPEQKLRAH 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 101 VG-LGLKGqwrdaarralaavgleNRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRLEMqdLIVSLW 179
Cdd:PLN03073 611 LGsFGVTG----------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVEA--LIQGLV 671
|
170 180 190
....*....|....*....|....*....|..
gi 447013267 180 QEHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PLN03073 672 LFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-211 |
1.20e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 34 IPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDTRMMFQDArllpWKSVID------------- 99
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAWVNQETPALPQPA----LEYVIDgdreyrqleaqlh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 100 --------NVGLGLKGQ------WRDAARRALAAVGL--ENRAGEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK10636 100 danerndgHAIATIHGKldaidaWTIRSRAASLLHGLgfSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447013267 163 --LDALTRLEMqdlivslW-QEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10636 180 ldLDAVIWLEK-------WlKSYQGTLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
133-216 |
1.48e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 212
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
....
gi 447013267 213 LDLT 216
Cdd:PRK09700 489 QILT 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-210 |
2.13e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 17 VSKHYAKNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPL------AEIQEDTRMMFQDAR 90
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPWKSVIDNVGLG---LKG------QWRDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPlg 161
Cdd:PRK10982 84 LVLQRSVMDNMWLGrypTKGmfvdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447013267 162 aLDALTRLEMQDL--IVSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:PRK10982 162 -TSSLTEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
130-207 |
2.19e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 130 PAALSGGQKQ------RVALARALIHRPGLLLLDEPLGALDAlTRLEMQ--DLIVSLWQEHGFTVLLVTHDvSEAVAMAD 201
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE-ENIEESlaEIIEERKSQKNFQLIVITHD-EELVDAAD 190
|
....*.
gi 447013267 202 RVLLIE 207
Cdd:cd03240 191 HIYRVE 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-191 |
2.58e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLA--------------GLETPTAGDvlaGTTPL-----AEIqEDTRMMFQDARLLPWKSV 97
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilHVEQEVVGD---DTTALqcvlnTDI-ERTQLLEEEAQLVAQQRE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 98 IDNVGLGLKGQWRDAARRALAAVG-----------------LENRAGEWPAALS--------------GGQKQRVALARA 146
Cdd:PLN03073 279 LEFETETGKGKGANKDGVDKDAVSqrleeiykrlelidaytAEARAASILAGLSftpemqvkatktfsGGWRMRIALARA 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447013267 147 LIHRPGLLLLDEPLGALDALTRLEMQDLIVSlWQEhgfTVLLVTH 191
Cdd:PLN03073 359 LFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSH 399
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-209 |
2.68e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 5 RLNQGTPLLLNAVSkhyaknivlnqldLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLA-----GTTPLAEIQ 79
Cdd:PTZ00243 1317 RYREGLPLVLRGVS-------------FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVngreiGAYGLRELR 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 80 EDTRMMFQDARLLPwKSVIDNVG----------------LGLKGQwrdaarRALAAVGLENRAGEWPAALSGGQKQRVAL 143
Cdd:PTZ00243 1384 RQFSMIPQDPVLFD-GTVRQNVDpfleassaevwaalelVGLRER------VASESEGIDSRVLEGGSNYSVGQRQLMCM 1456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447013267 144 ARALIHR-PGLLLLDEPLGALD-ALTRlEMQDLIVSLWQEHgfTVLLVTHDVsEAVAMADRVLLIEEG 209
Cdd:PTZ00243 1457 ARALLKKgSGFILMDEATANIDpALDR-QIQATVMSAFSAY--TVITIAHRL-HTVAQYDKIIVMDHG 1520
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
132-211 |
2.88e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 132 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-209 |
3.46e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 23 KNIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETP---TAGDVLAGTTPLAEI---------QED-------TR 83
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSfqrsigyvqQQDlhlptstVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 84 MMFQ-DARL-LPWK-----------SVIDNVGLglkgqwrdaARRALAAVGLenrAGEwpaALSGGQKQRVALARALIHR 150
Cdd:TIGR00956 855 ESLRfSAYLrQPKSvsksekmeyveEVIKLLEM---------ESYADAVVGV---PGE---GLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 151 PGLLL-LDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDVSeAVAMA--DRVLLIEEG 209
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPS-AILFEefDRLLLLQKG 979
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-211 |
3.91e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQ-EDTRMMFQdarLLPWKSVI--DNVG 102
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLS---IIPQSPVLfsGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 103 LGLK--------GQWRDAARRALAAV------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 168
Cdd:PLN03232 1328 FNIDpfsehndaDLWEALERAHIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447013267 169 LEMQDLIVSLWQEhgFTVLLVTHDVSEAVAmADRVLLIEEGKI 211
Cdd:PLN03232 1408 SLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-211 |
4.26e-07 |
|
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: 49.52 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTL----LRLLAGLETPTAGD-VLAGTTPLAEIQEDTRMMFQDARLL-------- 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFDGKIVIDgIDISKLPLHTLRSRLSIILQDPILFsgsirfnl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 93 -PWKSVIDNVglglkgQWRDAARRALAAV------GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:cd03288 116 dPECKCTDDR------LWEALEIAQLKNMvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447013267 166 LTRLEMQDLIVSLWQEHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:cd03288 190 ATENILQKVVMTAFADR--TVVTIAHRVS-TILDADLVLVLSRGIL 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-204 |
6.15e-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: 48.12 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 29 QLDLHIPAGQFVAVVGRSGGGKSTLLR------LLAGLETPTAGDVLAG-TTPLAEIQedtrmmFQDARLlpwksvidnv 101
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDaiglalGGAQSATRRRSGVKAGcIVAAVSAE------LIFTRL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 102 glglkgqwrdaarralaavglenragewpaALSGGQKQRVALARALIH----RPGLLLLDEPLGALDALTRLEMQDLIVS 177
Cdd:cd03227 77 ------------------------------QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180
....*....|....*....|....*..
gi 447013267 178 LWQeHGFTVLLVTHDvSEAVAMADRVL 204
Cdd:cd03227 127 HLV-KGAQVIVITHL-PELAELADKLI 151
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-211 |
7.95e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.52 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPTAGDVLAGTTPLAEIQEDTR------MMFQD--------- 88
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaragifLAFQYpveipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 89 ARLLpwKSVIDNVGLGLKG--QWRDAARRALAAVGLE----NR---AGewpaaLSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG0396 95 SNFL--RTALNARRGEELSarEFLKLLKEKMKELGLDedflDRyvnEG-----FSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 160 -----LGALDALTRlemqdlIVSLWQEHGFTVLLVTH-----DVSEavamADRVLLIEEGKI 211
Cdd:COG0396 168 dsgldIDALRIVAE------GVNKLRSPDRGILIITHyqrilDYIK----PDFVHVLVDGRI 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-203 |
2.65e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 31 DLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAG------------------------TTPLAEIQEDT---- 82
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlsfeqlqklvsdewqrnnTDMLSPGEDDTgrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 RMMFQDarllpwkSVIDNVG-LGLKGQWRDAarralaavGLENRAGEWpaaLSGGQKQRVALARALIHRPGLLLLDEPLG 161
Cdd:PRK10938 103 AEIIQD-------EVKDPARcEQLAQQFGIT--------ALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447013267 162 ALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRV 203
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFA 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-203 |
2.99e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 37 GQFVAVVGRSGGGKSTLLRLLAGLETPTAGD---------VL---AGTtplaEIQEdtrmMFQDAR-------------- 90
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrfRGT----ELQN----YFKKLYngeikvvhkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 LLPwKSVIDNVGLGLK-----GQWRDAARRalaaVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 165
Cdd:PRK13409 171 LIP-KVFKGKVRELLKkvderGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447013267 166 LTRLEMQDLIVSLWQEHgfTVLLVTHDVseAV--AMADRV 203
Cdd:PRK13409 246 RQRLNVARLIRELAEGK--YVLVVEHDL--AVldYLADNV 281
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-192 |
3.61e-06 |
|
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: 47.47 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 32 LHIP-AGQFVAVVGRSGGGKSTLLRLLAGLETPTAGD---------VL---AGTtplaEIQEdtrmMFQDAR-------- 90
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrfRGT----ELQD----YFKKLAngeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 ------LLPwKSVIDNVGLGLK-----GQWRDAARRalaaVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEP 159
Cdd:COG1245 165 kpqyvdLIP-KVFKGTVRELLEkvderGKLDELAEK----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 447013267 160 LGALDALTRLEMQDLIVSLwQEHGFTVLLVTHD 192
Cdd:COG1245 240 SSYLDIYQRLNVARLIREL-AEEGKYVLVVEHD 271
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-210 |
3.72e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLeTPTA---GDVLAgttplaeiqEDTRMMFQDAR------------- 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILF---------DGEVCRFKDIRdsealgiviihqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 91 --LLPWKSVIDNVGLG----LKG--QWRDAARRAL---AAVGLEnragEWPAALSG----GQKQRVALARALIHRPGLLL 155
Cdd:NF040905 87 laLIPYLSIAENIFLGneraKRGviDWNETNRRARellAKVGLD----ESPDTLVTdigvGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 156 LDEPLGAL-----DALTrlemqDLIVSLwQEHGFTVLLVTHDVSEAVAMADRVLLIEEGK 210
Cdd:NF040905 163 LDEPTAALneedsAALL-----DLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-211 |
9.69e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 20 HYAknivLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQedtrmmfqdARLLPWKSVI 98
Cdd:PRK13545 37 HYA----LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAALIAIS---------SGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 99 DNVGL-----GLKGQWRDAARRALAAVGLENRAGEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALD-ALTRLEM 171
Cdd:PRK13545 104 ENIELkglmmGLTKEKIKEIIPEIIEFADIGKFIYQPVkTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447013267 172 QDLivSLWQEHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:PRK13545 184 DKM--NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
27-203 |
1.71e-05 |
|
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: 44.56 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTLL---------------------RLLAGLETPTAgDVLAGTTPLAEIQEDT--- 82
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDV-DSIEGLSPAIAIDQKTtsr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 83 ----------------RMMFQDARLLPWKSVIDNVGLGLkgqwrdaarralaaVGLENRAGewpaALSGGQKQRVALARA 146
Cdd:cd03270 90 nprstvgtvteiydylRLLFARVGIRERLGFLVDVGLGY--------------LTLSRSAP----TLSGGEAQRIRLATQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 147 LIHR-PGLL-LLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDvSEAVAMADRV 203
Cdd:cd03270 152 IGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-211 |
2.78e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 26 VLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLA--------GTTPLAE---IQEDTRMMF-------- 86
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdiskfGLMDLRKvlgIIPQAPVLFsgtvrfnl 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 87 ------QDARLlpW--------KSVIDNVGLGLKGQWRdaarralaavglenRAGEwpaALSGGQKQRVALARALIHRPG 152
Cdd:PLN03130 1334 dpfnehNDADL--WeslerahlKDVIRRNSLGLDAEVS--------------EAGE---NFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 153 LLLLDEPLGALDALTRLEMQDLIVSLWQehGFTVLLVTHDVSeAVAMADRVLLIEEGKI 211
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFK--SCTMLIIAHRLN-TIIDCDRILVLDAGRV 1450
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
5-54 |
3.21e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 3.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 447013267 5 RLNQGTPLLLNAVSKHYAKNIvlnqlDLHIPAGQFVAVVGRSGGGKSTLL 54
Cdd:PRK00349 608 RKGNGKFLKLKGARENNLKNV-----DVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
9-62 |
1.09e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 447013267 9 GTPLLLNAVSKHYAKNIvlnqlDLHIPAGQFVAVVGRSGGGKSTLLR--LLAGLET 62
Cdd:TIGR00630 611 GKFLTLKGARENNLKNI-----TVSIPLGLFTCITGVSGSGKSTLINdtLYPALAN 661
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-209 |
1.88e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 131 AALSGGQKQRVALARaliHRPGLL-----LLDEPLGALDALTRLEMQDLIVSLwQEHGFTVLLVTHDvSEAVAMADRVLL 205
Cdd:PRK00635 475 ATLSGGEQERTALAK---HLGAELigityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADRIID 549
|
....
gi 447013267 206 IEEG 209
Cdd:PRK00635 550 IGPG 553
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
44-191 |
2.05e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 44 GRSGGGKSTLLRLLAGLETPTAGDVLAGTTPLAEIQEdtrmmfqdarllPWKSVIDNvGLGLKGQ---------WRDAAR 114
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK------------PYCTYIGH-NLGLKLEmtvfenlkfWSEIYN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 115 RALAAVG------LENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVsLWQEHGFTVLL 188
Cdd:PRK13541 100 SAETLYAaihyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV-MKANSGGIVLL 178
|
...
gi 447013267 189 VTH 191
Cdd:PRK13541 179 SSH 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-211 |
3.08e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447013267 133 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 211
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-69 |
3.91e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 3.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPTAGDVL 69
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDIL 67
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
27-53 |
5.77e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 5.77e-04
10 20
....*....|....*....|....*..
gi 447013267 27 LNQLDLHIPAGQFVAVVGRSGGGKSTL 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-164 |
7.72e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 43 VGRSGGGKSTLLRLLAGLETPTAGDV-LAGTTPLAEIQEDtRMMFQDARllpwksVIDNVGLGLKGQWRDAARRAL---- 117
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQD-QFAFEEFT------VLDTVIMGHTELWEVKQERDRiyal 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 118 --------AAVG-------------LENRAGEW------P--------AALSGGQKQRVALARALIHRPGLLLLDEPLGA 162
Cdd:PRK15064 106 pemseedgMKVAdlevkfaemdgytAEARAGELllgvgiPeeqhyglmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
..
gi 447013267 163 LD 164
Cdd:PRK15064 186 LD 187
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
132-212 |
1.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 132 ALSGGQKQ------RVALARALIHRPGLLLLDEPLGALDALTRLEMQDLI-VSLWQEHGF-TVLLVTHDvSEAVAMADrv 203
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeYSLKDSSDIpQVIMISHH-RELLSVAD-- 877
|
....*....
gi 447013267 204 LLIEEGKIG 212
Cdd:PRK01156 878 VAYEVKKSS 886
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-201 |
2.83e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 133 LSGGQKQRVALARALIHRPG---LLLLDEP------------LGALDALTrlemqdlivslwqEHGFTVLLVTH--DVse 195
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPttglhfhdirklLEVLHRLV-------------DKGNTVVVIEHnlDV-- 891
|
....*.
gi 447013267 196 aVAMAD 201
Cdd:COG0178 892 -IKTAD 896
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
25-192 |
3.59e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 37.73 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 25 IVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLETPTAGDVLAgttplaeIQEDTRMMFQDARLLPWKSVIDNVGL- 103
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIG-------LRGDALPLGANSFILPGLTGEENARMm 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 104 ----GLKGQwrDAARRALAAVGLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLW 179
Cdd:PRK15177 74 aslyGLDGD--EFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQL 151
|
170
....*....|...
gi 447013267 180 QEHGFTVLlvTHD 192
Cdd:PRK15177 152 QQKGLIVL--THN 162
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-206 |
3.79e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 120 VGLE----NRAGEwpaALSGGQKQRVALAR----ALIhrpGLL-LLDEP---LGALDAL----TRLEMQDLivslwqehG 183
Cdd:TIGR00630 475 VGLDylslSRAAG---TLSGGEAQRIRLATqigsGLT---GVLyVLDEPsigLHQRDNRrlinTLKRLRDL--------G 540
|
90 100
....*....|....*....|...
gi 447013267 184 FTVLLVTHDvSEAVAMADRVLLI 206
Cdd:TIGR00630 541 NTLIVVEHD-EDTIRAADYVIDI 562
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-87 |
4.30e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 37.46 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447013267 24 NIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGLE--TPTAGDVLAGTTPLAEIQEDTR------MMFQ 87
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRagegifMAFQ 85
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
133-204 |
5.97e-03 |
|
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: 37.21 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 133 LSGGQKQRVALARALIHR---PGLLLLDEPlgaldaLTRLEMQD---LIVSLWQ--EHGFTVLLVTHDVsEAVAMADRVL 204
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEP------TTGLHFHDvkkLLEVLQRlvDKGNTVVVIEHNL-DVIKCADWII 242
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
41-73 |
6.82e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 36.16 E-value: 6.82e-03
10 20 30
....*....|....*....|....*....|...
gi 447013267 41 AVVGRSGGGKSTLLRLLAGLETPTAGDVLAGTT 73
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTR 33
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-212 |
7.38e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447013267 132 ALSGGQKQRVALARALIH---RPGLLLLDEPLGALDALTRLEMQDLIVSLWQEhGFTVLLVTHDVsEAVAMADRVLLI-- 206
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNM-HVVKVADYVLELgp 886
|
....*.
gi 447013267 207 EEGKIG 212
Cdd:PRK00635 887 EGGNLG 892
|
|
| |
