|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-231 |
4.19e-119 |
|
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: 339.26 E-value: 4.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARFLAGF 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAFRLRQ--RMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREhtDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAA--PALAAFL 231
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASddPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-223 |
7.88e-100 |
|
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: 290.17 E-value: 7.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA---GFG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAALFDSLSVWQNVAFRLRQ--RMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREhtRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDA 223
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-233 |
6.63e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 206.77 E-value: 6.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD------RAARARFl 74
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkdiNKLRRKV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 agfGMLFQGAALFDSLSVWQNVAFRLR--QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:COG1126 80 ---GMVFQQFNLFPHLTVLENVTLAPIkvKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAA 229
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQherTRA 234
|
....
gi 1608348115 230 FLGR 233
Cdd:COG1126 235 FLSK 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
2.99e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 198.00 E-value: 2.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflag 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 fGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:COG1116 83 -GVVFQEPALLPWLTVLDNVALGLElRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG--GRIVHD 215
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
1.06e-62 |
|
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: 195.05 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARflaGFGML 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGPEtADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKlRGVPKAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
5.99e-62 |
|
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: 193.88 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAG 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 ---FGMLFQ--GAALFDSLSVWQNVA--FRLRQRMSDDRARG-IALDKLARVGLGPETADLMPAELSGGMAKRAGLARAI 148
Cdd:cd03257 81 rkeIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-218 |
8.24e-62 |
|
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: 193.07 E-value: 8.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFG----ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflagf 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLElQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG--GRIVHDGPV 218
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
2.64e-61 |
|
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: 200.51 E-value: 2.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARAR 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FLAGFGMLFQG--AALFDSLSVWQNVAF--RLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAI 148
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEplRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
2.33e-60 |
|
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: 190.40 E-value: 2.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGA----TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAG 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQ--GAALFDSLSVWQNVAFRLRQRMSDDRARGIAlDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQI 154
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDREERIA-ELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 155 IFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
4.38e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 193.01 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARflaGFGM 79
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtGLPPEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRgVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
4.73e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.12 E-value: 4.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR---AARARFlagfG 78
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpaEVRRRI----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAALFDSLSVWQNVAF--RLRqRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFfaRLY-GLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
8.40e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 188.33 E-value: 8.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFG----ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARF 73
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDissLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 LAG-FGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADD 151
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLlAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMAsVARIGDRVALLQGGRIVHD 215
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
8.51e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.83 E-value: 8.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-------RAA 69
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalserelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFlagfGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAI 148
Cdd:COG1135 81 RRKI----GMIFQHFNLLSSRTVAENVALPLEiAGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-225 |
1.02e-59 |
|
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: 188.17 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATR----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-------RAA 69
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFlagfGMLFQGAALFDSLSVWQNVAFRLR---QRMSDDRARgiALDKLARVGLGpETADLMPAELSGGMAKRAGLAR 146
Cdd:cd03258 81 RRRI----GMIFQHFNLLSSRTVFENVALPLEiagVPKAEIEER--VLELLELVGLE-DKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 147 AIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
3.84e-58 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 183.50 E-value: 3.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARA--RFLAGFGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:cd03262 81 VFQQFNLFPHLTVLENItlAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-219 |
6.75e-56 |
|
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: 181.02 E-value: 6.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA---GRILWQGRPLDRAARARF 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 LA----GFGMLFQGAalFDSL----SVWQNVA--FRLRQRMSDDRARGIALDKLARVGLGP--ETADLMPAELSGGMAKR 141
Cdd:COG0444 81 RKirgrEIQMIFQDP--MTSLnpvmTVGDQIAepLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 142 AGLARAIADDPQIIFFDEPTTGLDP-IRARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVtIQAQILN-LLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
1.76e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.94 E-value: 1.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-------RAARAR 72
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgralRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FlagfGMLFQGAALFDSLSVWQNV---------AFR-LRQRMS-DDRARgiALDKLARVGLGpETADLMPAELSGGMAKR 141
Cdd:COG3638 82 I----GMIFQQFNLVPRLSVLTNVlagrlgrtsTWRsLLGLFPpEDRER--ALEALERVGLA-DKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 142 AGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGM 221
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
...
gi 1608348115 222 DAA 224
Cdd:COG3638 235 TDA 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
2.76e-54 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 182.03 E-value: 2.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF--GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA---GRILWQGRPLDRAARARFLA 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 GFGMLFQGA-ALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQ 153
Cdd:COG1123 84 RIGMVFQDPmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 154 IIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP-ALAA 229
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPqALAA 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
9.68e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 172.90 E-value: 9.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQ--GAALFDSlSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFGPENLgLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
1.24e-53 |
|
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: 172.29 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGA----TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARFL 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 A-GFGMLFQGAALFDSLSVWQNVAFRLR---QRMSDDRARGIALdkLARVGLGpETADLMPAELSGGMAKRAGLARAIAD 150
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVELPLLlagVPKKERRERAEEL--LERVGLG-DRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMaSVARIGDRVALLQGGRI 212
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-231 |
3.07e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 169.50 E-value: 3.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQG-RPLDRAARARFL-AGFG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIrQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAALFDSLSVWQNVAFRLRQ--RMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRvrGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFL 231
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPsqrLQEFL 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-240 |
3.60e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 172.25 E-value: 3.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL--DRAARARflaGFGM 79
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRpPSKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFLG--- 232
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPAtpfVARFLGcvn 238
|
....*...
gi 1608348115 233 RSPAQSAG 240
Cdd:COG1118 239 VLRGRVIG 246
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
6.22e-52 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 166.42 E-value: 6.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRaARARFLAGFGMLF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVafrlrqrmsddrargialdklarvglgpetadlmpaELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 162 TGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-225 |
1.07e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.14 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATR----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-------RAA 69
Cdd:PRK11153 1 MIELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsekelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFlagfGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAI 148
Cdd:PRK11153 81 RRQI----GMIFQHFNLLSSRTVFDNVALPLElAGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-211 |
2.19e-51 |
|
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: 165.05 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARAR--FLAGFGM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVAFRlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
4.04e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 167.17 E-value: 4.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARflaGFGM 79
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRkVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 159 EPTTGLDP-IRARAIdALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFLGrS 234
Cdd:COG3839 159 EPLSNLDAkLRVEMR-AEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAnlfVAGFIG-S 236
|
..
gi 1608348115 235 PA 236
Cdd:COG3839 237 PP 238
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
1.10e-49 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 162.14 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA---G 76
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRvTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
2.55e-49 |
|
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: 162.52 E-value: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR-AARARFLAGFGM 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVA---------------FRL-RQRMSDDRARGIALDKLARVGLGPEtADLMPAELSGGMAKRAG 143
Cdd:COG0411 84 TFQNPRLFPELTVLENVLvaaharlgrgllaalLRLpRARREEREARERAEELLERVGLADR-ADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 144 LARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDA 223
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
250
....*....|....
gi 1608348115 224 APA-LAAFLGRSPA 236
Cdd:COG0411 243 DPRvIEAYLGEEAA 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-218 |
3.22e-49 |
|
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: 161.19 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL-----EAPEAGRILWQGRPL--DRAARARFL 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 AGFGMLFQGAALFDsLSVWQNVAF--RLRQRMSDDRARGIALDKLARVGLGPETAD-LMPAELSGGMAKRAGLARAIADD 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYglRLHGIKLKEELDERVEEALRKAALWDEVKDrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVALLQGGRIVHDGPV 218
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-220 |
5.44e-49 |
|
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: 161.18 E-value: 5.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARaRFLAGFGML 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLA-RVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIeLLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAG 220
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-219 |
1.05e-48 |
|
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: 160.59 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL---DRAARARFLAgf 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslSRRELARRIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 gMLFQGAALFDSLSVWQNVAF-------RLRQRMSDDRArgIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIAD 150
Cdd:COG1120 79 -YVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDRE--AVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-211 |
1.23e-48 |
|
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: 159.17 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAAL-FDSL 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDDqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 91 SVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRA 169
Cdd:cd03225 92 TVEEEVAFGLENLgLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1608348115 170 RAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGR 211
Cdd:cd03225 171 RELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-233 |
1.56e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 159.54 E-value: 1.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVldGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflAGFGML 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQRM---SDDRARGIALdkLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLkltAEQRAQVEQA--LERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGM---DAAPALAAFLGR 233
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldgEPPPALAAYLGI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-219 |
2.60e-48 |
|
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: 159.14 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR-AARARFLAGFGML 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNV-----------AFRLRQRMSDDRARGIALDKLARVGLGPEtADLMPAELSGGMAKRAGLARAIA 149
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsgLLLARARREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 150 DDPQIIFFDEPTTGLDPIRARAIDALIRGIVtETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-216 |
6.16e-48 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 159.35 E-value: 6.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 9 KTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----GFGMLFQGA 84
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 85 ALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGPEtADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTG 163
Cdd:cd03294 112 ALLPHRTVLENVAFGLEvQGVPRAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 164 LDP-IRARAIDALIRgIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03294 191 LDPlIRREMQDELLR-LQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
6.43e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.29 E-value: 6.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSlSVWQNVA--FRLRQRmSDDRARGIALdkLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:COG4619 81 QEPALWGG-TVRDNLPfpFQLRER-KFDRERALEL--LERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-216 |
9.29e-47 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 156.08 E-value: 9.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAG---F 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAFRLRQ--RMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREhtQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-219 |
1.77e-46 |
|
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: 154.13 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATR----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR---PLDRAARARF 73
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 LAG-FGMLFQGAALFDSLSVWQNVAFRLrQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPL-ELAGRRDARARARALLERVGLG-HRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIgDRVALLQGGRIVHDGPVA 219
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAAT 231
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-233 |
3.23e-46 |
|
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: 157.12 E-value: 3.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflAGFGMLF 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK--RDYGIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:TIGR03265 83 QSYALFPNLTVADNIAYGLKnRGMGRAEVAERVAELLDLVGL-PGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 161 TTGLDpirARAIDAL---IRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG-PVAGMD--AAPALAAFLGR 233
Cdd:TIGR03265 162 LSALD---ARVREHLrteIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGtPQEIYRhpATPFVADFVGE 237
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
7.05e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 153.42 E-value: 7.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQG-------------RPLDR 67
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 68 AARARFLAGFGMLFQGAALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLA 145
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVieAPVHVLGRPKAEAIERAEALLAKVGLA-DKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 146 RAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
250
....*....|..
gi 1608348115 226 A---LAAFLGRS 234
Cdd:COG4598 246 KserLRQFLSSS 257
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
7.30e-46 |
|
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: 153.11 E-value: 7.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGA-TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-------RAARARF 73
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 lagfGMLFQGAALFDSLSVWQNV---------AFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGL 144
Cdd:cd03256 81 ----GMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 145 ARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAA 224
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.80e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 150.64 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFlaGF--- 77
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI--GYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 --GmlfqgaaLFDSLSVWQNVAF--RLRQrMSDDRARGIALDKLARVGLGPETADLMpAELSGGMAKRAGLARAIADDPQ 153
Cdd:COG4152 79 erG-------LYPKMKVGEQLVYlaRLKG-LSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 154 IIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-234 |
8.80e-44 |
|
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: 147.83 E-value: 8.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGPET-ADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKlLKWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFLGRS 234
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAndfVAEFVGAD 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-232 |
2.29e-43 |
|
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: 146.72 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARflaGFGML 80
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-----QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRvkprsERPPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRI--------VHDGPvagmdAAPAL 227
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIeqvgtpdeVYDHP-----ASPFV 233
|
....*
gi 1608348115 228 AAFLG 232
Cdd:cd03296 234 YSFLG 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
3.79e-43 |
|
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: 145.84 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARflaGFGML 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRlKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
3.04e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.69 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAA--------RAR 72
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FLAGFgmlfqgaalfdSLSVWQNVAFRLRQRMS-----DDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARA 147
Cdd:COG1121 86 VDWDF-----------PITVRDVVLMGRYGRRGlfrrpSRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 148 IADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHdGPVAGMDAAPAL 227
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENL 231
|
....*
gi 1608348115 228 AAFLG 232
Cdd:COG1121 232 SRAYG 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-232 |
3.06e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 143.63 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATrVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR------PLDRaararfla 75
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlpPEKR-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 GFGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLARVgLG-PETADLMPAELSGGMAKRAGLARAIADDPQI 154
Cdd:cd03299 72 DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEM-LGiDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 155 IFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFL 231
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKnefVAEFL 230
|
.
gi 1608348115 232 G 232
Cdd:cd03299 231 G 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
6.07e-42 |
|
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: 142.82 E-value: 6.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFG-ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLdRAARARFL----A 75
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI-TKLRGKKLrklrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 GFGMLFQGAALFDSLSVWQNV-----------AFRLRQRMSDDRARgiALDKLARVGLGpETADLMPAELSGGMAKRAGL 144
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVlhgrlgykptwRSLLGRFSEEDKER--ALSALERVGLA-DKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 145 ARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAA 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
7.78e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 7.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRI------------LWQGRPLDRA 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 69 ARARflagFGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDK--LARVGL-GPETAdlMPAELSGGMAKRAGLA 145
Cdd:PRK11264 83 LRQH----VGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARelLAKVGLaGKETS--YPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 146 RAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETgATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-213 |
8.27e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 146.40 E-value: 8.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTfGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----GFGMLFQ 82
Cdd:COG4175 34 LEKT-GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRElrrkKMSMVFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:COG4175 113 HFALLPHRTVLENVAFGLEiQGVPKAERRERAREALELVGLA-GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAF 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 162 TGLDP-IRARAIDALIRgIVTETGATALTITHDMASVARIGDRVALLQGGRIV 213
Cdd:COG4175 192 SALDPlIRREMQDELLE-LQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-232 |
1.79e-41 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 141.48 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR-AARARflaGFGML 80
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRvHARDR---KIGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 161 TTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFLG 232
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPAnpfVMSFLG 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-216 |
6.25e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 138.34 E-value: 6.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL---DRAARARFLAgfgm 79
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslSPKELARKIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 lfqgaalfdslSVWQNvafrlrqrmsddrargialdkLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03214 77 -----------YVPQA---------------------LELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-217 |
2.13e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 139.89 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 13 ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-------RAARARFlagfGMLFQGAA 85
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkklKDLRKKV----GLVFQFPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 86 --LFdSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:TIGR04521 93 hqLF-EETVYKDIAFGPKnLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 163 GLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:TIGR04521 172 GLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
3.03e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 137.61 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRaARARFLAGFGML 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAF--RLRQRMSDDRArgiALDKLARVGLGPEtADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:COG4133 81 GHADGLKPELTVRENLRFwaALYGLRADREA---IDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1608348115 159 EPTTGLDPIRARAIDALIRGiVTETGATALTITHD 193
Cdd:COG4133 157 EPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-211 |
3.78e-40 |
|
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: 135.45 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 gaalfdslsvwqnvafrlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1608348115 163 GLDPIRARAIDALIRGIVtETGATALTITHDMASVARIGDRVALLQGGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
9.36e-40 |
|
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: 136.23 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARFLAgfgML 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPKDRDIA---MV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQRMS-----DDRARGIAldKLARVGlgpETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVpkdeiDERVREVA--ELLQIE---HLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-223 |
1.64e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.51 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 6 GLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARFLAGFGMLFQ 82
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlakLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GA--ALFDSLSVWQNVAFRLRQRMSDDRARGIA--LDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRHLLSLDKAERLAraSEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDA 223
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-218 |
4.97e-39 |
|
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: 135.29 E-value: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLagfgmLFQGAALFDSLSVWQNV 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 97 AF---RLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAID 173
Cdd:TIGR01184 76 ALavdRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1608348115 174 ALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPV 218
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
8.64e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 135.37 E-value: 8.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFG----ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflag 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 fGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRlRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG--GRIVH 214
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.04e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 133.56 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflagFGMLF 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAF--RLRQrMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03269 77 EERGLYPKMKVIDQLVYlaQLKG-LKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03269 155 PFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-226 |
1.65e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.40 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF-----------GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDR 67
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 68 AARARFLAGFGMLFQG--AALFDSLSVWQNVAFRLR-QRMSDDRAR-GIALDKLARVGLGPETADLMPAELSGGMAKRAG 143
Cdd:COG4608 88 RELRPLRRRMQMVFQDpyASLNPRMTVGDIIAEPLRiHGLASKAERrERVAELLELVGLRPEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 144 LARAIADDPQIIFFDEPTTGLD-PIRARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMD 222
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDvSIQAQVLN-LLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
....
gi 1608348115 223 AAPA 226
Cdd:COG4608 247 ARPL 250
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
2.29e-38 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 133.01 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATR--VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLdRAARARFLAGFGM 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVAF--RLRqRMSDDRARGIALDKLARVGLGPEtADLMPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyaRLK-GLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIVteTGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-226 |
2.33e-38 |
|
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: 139.82 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGA----TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA----GRILWQGRPLDRA--AR 70
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLseRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 71 ARFLAG--FGMLFQ------------GAALFDSLsvwqnvafRLRQRMSDDRARGIALDKLARVGLgPETADLM---PAE 133
Cdd:COG4172 86 LRRIRGnrIAMIFQepmtslnplhtiGKQIAEVL--------RLHRGLSGAAARARALELLERVGI-PDPERRLdayPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP-IRARaIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVtVQAQ-ILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250
....*....|....
gi 1608348115 213 VHDGPVAGMDAAPA 226
Cdd:COG4172 236 VEQGPTAELFAAPQ 249
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
2.53e-38 |
|
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: 132.73 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARArfLAGFGMLF 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDklaRVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRIDEVLD---VVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 162 TGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03268 155 NGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-234 |
7.79e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.84 E-value: 7.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD----RAARArflAG 76
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrspRDAQA---AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAF----RLRQRMSDDRARGIALDKLARVGLgpetaDLMPAELSG--GMAKRAGL--ARAI 148
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLgrepRRGGLIDWRAMRRRARELLARLGL-----DIDPDTPVGdlSVAQQQLVeiARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 149 ADDPQIIFFDEPTTGLDPiraRAIDAL---IRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:COG1129 156 SRDARVLILDEPTASLTE---REVERLfriIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDE 231
|
....*....
gi 1608348115 226 ALAAFLGRS 234
Cdd:COG1129 232 LVRLMVGRE 240
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-162 |
1.13e-37 |
|
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: 128.92 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSLSVWQNV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 97 AFRLR----QRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:pfam00005 81 RLGLLlkglSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
2.93e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.25 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAA-RARFLAGFGML 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQN--VAFRLRQRMSDDRARGIALDKLARVGlgpETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:cd03224 81 PEGRRIFPELTVEENllLGAYARRRAKRKARLERVYELFPRLK---ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDA 223
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
3.66e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRA-ARARFLagfGML 80
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAENRHV---NTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRmQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-212 |
6.67e-37 |
|
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: 129.06 E-value: 6.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGA-TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARFLAGF 77
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAFRLRqrMSDDRARGIA---LDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQI 154
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALE--VTGVPPREIRkrvPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 155 IFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-213 |
8.92e-37 |
|
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: 129.01 E-value: 8.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFG----ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL------DRAA- 69
Cdd:TIGR02211 1 LLKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklssnERAKl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFLagfGMLFQGAALFDSLSVWQNVAF-RLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAI 148
Cdd:TIGR02211 81 RNKKL---GFIYQFHHLLPDFTALENVAMpLLIGKKSVKEAKERAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIgDRVALLQGGRIV 213
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
1.59e-36 |
|
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: 128.03 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAaRARFlagfGMLFQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-RKRI----GYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 gAALFDS---LSVWQNVAFRLRQRMS-------DDRARgiALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:cd03235 76 -RRSIDRdfpISVRDVVLMGLYGHKGlfrrlskADKAK--VDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGiVTETGATALTITHDMASVARIGDRVALLQGGRIVHD 215
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
3.31e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 128.69 E-value: 3.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR---AARARFLAgf 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspWELARRRA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 gMLFQGAAL-FDsLSVWQNVAF-RLRQRMSDDRARGIALDKLARVGLGPeTADLMPAELSGGMAKRAGLARAIA------ 149
Cdd:COG4559 79 -VLPQHSSLaFP-FTVEEVVALgRAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 150 -DDPQIIFFDEPTTGLDPIRARAIDALIRGiVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQ-LARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-238 |
5.04e-36 |
|
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: 130.61 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRgLQKTFGATRvLDgVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----G 76
Cdd:COG4148 2 MLEVD-FRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRLRQrmSDDRARGIALDKLARV-GLGPeTADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGRKR--APRAERRISFDEVVELlGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLGRSP 235
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEE 235
|
...
gi 1608348115 236 AQS 238
Cdd:COG4148 236 AGS 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
5.87e-36 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 130.20 E-value: 5.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRA-ARARFLagfGML 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhARDRKV---GFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDK-----LARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAkvtqlLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-232 |
7.95e-36 |
|
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: 127.02 E-value: 7.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAA---RARflAGF 77
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphrIAR--LGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQN--VAFRLRQRMSDDRARgialdkLARV-GLGPETADLM--PA-ELSGG---M-AkragLARA 147
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENllLGAYARRDRAEVRAD------LERVyELFPRLKERRrqRAgTLSGGeqqMlA----IGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 148 IADDPQIIFFDEPTTGLDPIRARAIDALIRGIVtETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPAL 227
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEV 229
|
....*.
gi 1608348115 228 -AAFLG 232
Cdd:COG0410 230 rEAYLG 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
8.97e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.46 E-value: 8.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD----RAARArflAG 76
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDAIA---LG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVA------FRLRQRMSDDRAR--------GIALDKLARVGlgpetadlmpaELSGGMAKRA 142
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVlgleptKGGRLDRKAARARirelseryGLDVDPDAKVE-----------DLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 143 GLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMD 222
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETS 229
|
..
gi 1608348115 223 AA 224
Cdd:COG3845 230 EE 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
1.78e-35 |
|
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: 125.38 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGeSLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPlDRAARARFLAGFGMLF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWlKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 161 TTGLDP---IRaraidalIRGIVTETGATALTI--THDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03264 158 TAGLDPeerIR-------FRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
2.92e-35 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 126.19 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR---PLDRA----ARARF 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqLRDLYalseAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 LA----GFgmlfqgaalfdslsVWQNVAFRLRQRMSD----------------DRARGIALDKLARVGLGPETADLMPAE 133
Cdd:PRK11701 86 LLrtewGF--------------VHQHPRDGLRMQVSAggnigerlmavgarhyGDIRATAGDWLERVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLD-PIRARAIDaLIRGIVTETGATALTITHDMAsVARI-GDRVALLQGGR 211
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvSVQARLLD-LLRGLVRELGLAVVIVTHDLA-VARLlAHRLLVMKQGR 229
|
....*
gi 1608348115 212 IVHDG 216
Cdd:PRK11701 230 VVESG 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-225 |
9.67e-35 |
|
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: 129.80 E-value: 9.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEaGRILWQGRPLDRAARARFLA---GFGMLFQG 83
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPlrrRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 84 AalFDSLS----VWQNVA--FRLRQRMSDDRAR-GIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:COG4172 371 P--FGSLSprmtVGQIIAegLRVHGPGLSAAERrARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 157 FDEPTTGLD-PIRARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:COG4172 449 LDEPTSALDvSVQAQILD-LLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-216 |
1.09e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.64 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGrpLDRAARARFLAGFGML 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQdKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 160 PTTGLD-PIRARaIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK11607 176 PMGALDkKLRDR-MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-216 |
1.30e-34 |
|
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: 123.25 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARaRFLAGFGMLF 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARlYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 161 TTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-213 |
3.86e-34 |
|
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: 122.05 E-value: 3.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGA----TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA-- 75
Cdd:TIGR02982 2 ISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 -GFGMLFQGAALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:TIGR02982 82 rRIGYIFQAHNLLGFLTARQNVqmALELQPNLSYQEARERARAMLEAVGLG-DHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDmASVARIGDRVALLQGGRIV 213
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
4.36e-34 |
|
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: 122.09 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATR----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARArFLAG 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-216 |
5.39e-34 |
|
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: 121.45 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 21 DLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflAGFGMLFQGAALFDSLSVWQNVAF-- 98
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 99 --RLRQRMSDDRARGIALdklARVGLGPETADLmPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALI 176
Cdd:cd03298 96 spGLKLTAEDRQAIEVAL---ARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1608348115 177 RGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-217 |
1.39e-33 |
|
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: 127.64 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLqkTFG----ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGF 77
Cdd:COG2274 474 IELENV--SFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFdSLSVWQNVAFRlRQRMSDDRARGIAldKLArvGLGPETADlMP-----------AELSGGMAKRAGLAR 146
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG-DPDATDEEIIEAA--RLA--GLHDFIEA-LPmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 147 AIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVteTGATALTITHDMaSVARIGDRVALLQGGRIVHDGP 217
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGT 692
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-216 |
1.67e-33 |
|
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: 120.48 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 20 VDLTVgQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----GFGMLFQGAALFDSLSVWQN 95
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLR-QRMSDDRARGIALdkLARVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDA 174
Cdd:cd03297 96 LAFGLKrKRNREDRISVDEL--LDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1608348115 175 LIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-213 |
1.76e-33 |
|
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: 120.05 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARfLAGFGMLFQGAALFDSlS 91
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK-SIGYVMQDVDYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAFRLRQrMSDD--RARGIaLDKLARVGLgpetADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRA 169
Cdd:cd03226 89 VREELLLGLKE-LDAGneQAETV-LKDLDLYAL----KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1608348115 170 RAIDALIRgIVTETGATALTITHDMASVARIGDRVALLQGGRIV 213
Cdd:cd03226 163 ERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
2.49e-33 |
|
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: 118.30 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD----RAARArflAGF 77
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfaspRDARR---AGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQgaalfdslsvwqnvafrlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFF 157
Cdd:cd03216 78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHD 215
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-234 |
3.36e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.91 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARFLAgfgML 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVtHRSIQQRDIC---MV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGL-GPEtaDLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKmLGVPKEERKQRVKEALELVDLaGFE--DRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA---LAAFLGRS 234
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAsrfMASFMGDA 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
3.44e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 120.12 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-----RAARARFLAG 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 -FGMLFQGAALFDSLSVWQN-VAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQ 153
Cdd:COG4161 83 kVGMVFQQYNLWPHLTVMENlIEAPCKvLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 154 IIFFDEPTTGLDPirarAIDALIRGIVTE---TGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:COG4161 162 VLLFDEPTAALDP----EITAQVVEIIRElsqTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
3.80e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 120.40 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCI-----LGLEAPEAGRILWQGRPLDRAARARFLAG 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRLR-QRMSDDRArgialDKLARVGLGPETADL---------MPA-ELSGGMAKRAGLA 145
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKlNRLVKSKK-----ELQERVRWALEKAQLwdevkdrldAPAgKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 146 RAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVALLQGGRIVHDGPV 218
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-221 |
4.79e-33 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 121.34 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 9 KTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARaRFLAGFGMLFQGAALFD 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPR-KVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 89 SLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPI 167
Cdd:TIGR01188 80 DLTGRENLEMMGRlYGLPKDEAEERAEELLELFELG-EAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 168 RARAIDALIRGIVtETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGM 221
Cdd:TIGR01188 159 TRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
6.29e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 119.73 E-value: 6.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAG----- 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 -FGMLFQGAALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQ 153
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNLieAPCRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 154 IIFFDEPTTGLDP-IRARAIDaLIRGIvTETGATALTITHDMaSVAR-IGDRVALLQGGRIVHDG 216
Cdd:PRK11124 162 VLLFDEPTAALDPeITAQIVS-IIREL-AETGITQVIVTHEV-EVARkTASRVVYMENGHIVEQG 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-231 |
6.60e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.07 E-value: 6.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-----------------RAA 69
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknqlRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFLagfgMLFQGAALFDSLSVWQNVAFRLRQ--RMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARA 147
Cdd:PRK10619 91 RTRLT----MVFQHFNLWSHMTVLENVMEAPIQvlGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 148 IADDPQIIFFDEPTTGLDPiraRAIDALIRGI--VTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP---VAGMD 222
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDP---ELVGEVLRIMqqLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGApeqLFGNP 243
|
....*....
gi 1608348115 223 AAPALAAFL 231
Cdd:PRK10619 244 QSPRLQQFL 252
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
7.09e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.86 E-value: 7.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAAR-ARflAGFGML 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARlAR--ARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVA-----FRLRQRMSDdrARGIALDKLARVglgPETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLvfgryFGMSTREIE--AVIPSLLEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
1.39e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.99 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL--EAPEA---GRILWQGRP-LDR-----AAR 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDiYDPdvdvvELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 71 ARFlagfGMLFQGAALFdSLSVWQNVAF--RLRQRMSDDRARGIALDKLARVGLGPETAD-L-MPA-ELSGGMAKRAGLA 145
Cdd:COG1117 92 RRV----GMVFQKPNPF-PKSIYDNVAYglRLHGIKSKSELDEIVEESLRKAALWDEVKDrLkKSAlGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 146 RAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtgataLTI---THDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-----YTIvivTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
1.51e-32 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 119.01 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAAR-ARflagfgMLFQ 82
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdTR------LMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GAALFDSLSVWQNVAFRLRQRMSDDrargiALDKLARVGLGPETADlMPAELSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLKGQWRDA-----ALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 163 GLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPV 218
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTV 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-235 |
2.43e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 117.76 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 21 DLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflAGFGMLFQGAALFDSLSVWQNVAFRL 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 101 RQRMSDDRARGIALDKLA-RVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGI 179
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIArQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 180 VTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAG-MDAAPALAAFLGRSP 235
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDElLSGKASASALLGIKS 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-217 |
5.86e-32 |
|
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: 122.22 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRIL------W----QGRPL 65
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdeWvdmtKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 66 DRAARARFLagfGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLARVGLGPETA----DLMPAELSGGMAKR 141
Cdd:TIGR03269 359 GRGRAKRYI---GILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 142 AGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
6.17e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.49 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGA-----TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR---AARAR 72
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpeYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FLagfGMLFQ----GAAlfDSLSVWQNVA--------FRLRQRMSDDRaRGIALDKLARVGLGPEtaDLMPAE---LSGG 137
Cdd:COG1101 81 YI---GRVFQdpmmGTA--PSMTIEENLAlayrrgkrRGLRRGLTKKR-RELFRELLATLGLGLE--NRLDTKvglLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 138 maKRAGLARAIA--DDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHD 215
Cdd:COG1101 153 --QRQALSLLMAtlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-219 |
8.08e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.18 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD---RAARARFLAgf 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 gMLFQGAALFDSLSVWQNVAF-RLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIA------D 150
Cdd:PRK13548 80 -VLPQHSSLSFPFTVEEVVAMgRAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-218 |
1.57e-31 |
|
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: 115.54 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 18 DGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA----GRILWQGRPLDrAARARFLAgFGMLFQG--AALFDSLS 91
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLtqtsGEILLDGRPLL-PLSIRGRH-IATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAFRLRQRMS-DDRARGIALDKLARVGLgPETADLM---PAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPI 167
Cdd:TIGR02770 81 MGNHAIETLRSLGKlSKQARALILEALEAVGL-PDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 168 RARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPV 218
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-216 |
3.50e-31 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 114.56 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR-----PLDRaaRARflAG 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMHK--RAR--LG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDK-LARVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEElLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRgIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIK-ILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-217 |
4.57e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.50 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGA-ALFDSLSVWQN 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRL------RQRMSDdRARgialDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRA 169
Cdd:PRK13635 103 VAFGLenigvpREEMVE-RVD----QALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 170 RAIDALIRGIVTETGATALTITHDMASVARiGDRVALLQGGRIVHDGP 217
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-217 |
5.06e-31 |
|
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: 119.87 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDT-TLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VafRL-RQRMSDDRARgialDKLARVGLG------PETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGL 164
Cdd:COG4987 429 L--RLaRPDATDEELW----AALERVGLGdwlaalPDGLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 165 DPIRARAIDALIRGIVteTGATALTITHDMASVARIgDRVALLQGGRIVHDGP 217
Cdd:COG4987 503 DAATEQALLADLLEAL--AGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGT 552
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-211 |
6.34e-31 |
|
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: 112.09 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLqkTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGF 77
Cdd:cd03228 1 IEFKNV--SFsypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSlSVWQNVafrlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFF 157
Cdd:cd03228 79 AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIvtETGATALTITHDMASVaRIGDRVALLQGGR 211
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-195 |
7.45e-31 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 112.90 E-value: 7.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD------RAARARFlagfGMLFQGA- 84
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkglLERRQRV----GLVFQDPd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 85 -ALFdSLSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:TIGR01166 79 dQLF-AADVDQDVAFGPLNLgLSEAEVERRVREALTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|...
gi 1608348115 163 GLDPIRARAIDALIRGIvTETGATALTITHDMA 195
Cdd:TIGR01166 157 GLDPAGREQMLAILRRL-RAEGMTVVISTHDVD 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-194 |
1.05e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.03 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARflagfGML 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAgVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDM 194
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-217 |
1.24e-30 |
|
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: 114.06 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF--GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQG-RPLDRAA----RARFl 74
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENlweiRKKV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 agfGMLFQ-------GAalfdslSVWQNVAFRL----------RQRMsdDRArgialdkLARVGLGpETADLMPAELSGG 137
Cdd:TIGR04520 80 ---GMVFQnpdnqfvGA------TVEDDVAFGLenlgvpreemRKRV--DEA-------LKLVGME-DFRDREPHLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 138 MAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARiGDRVALLQGGRIVHDGP 217
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGT 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
2.44e-30 |
|
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: 113.00 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP--------LDRAARAR 72
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FL-AGFGMLFQGAA--LFDSLSVWQNVAFRLR---QRMSDDrARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLAR 146
Cdd:TIGR02323 83 LMrTEWGFVHQNPRdgLRMRVSAGANIGERLMaigARHYGN-IRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 147 AIADDPQIIFFDEPTTGLD-PIRARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDvSVQARLLD-LLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-209 |
3.23e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.18 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFG----ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL---DRAARARF 73
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 LA-GFGMLFQGAALFDSLSVWQNVAF-RLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADD 151
Cdd:PRK10584 86 RAkHVGFVFQSFMLIPTLNALENVELpALLRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG 209
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-212 |
4.43e-30 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 110.00 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATR--VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGM 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSlSVWQNVafrlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 160 PTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIgDRVALLQGGRI 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-214 |
6.54e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.65 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA---GRILWQGRPLDR-AARARflaG 76
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTAlPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVarigdrvalLQGGRIVH 214
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA---------PAAGRVLD 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-212 |
6.77e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 111.66 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR-----PLDRaaRARflA 75
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHK--RAR--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 GFGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALDKL-ARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQI 154
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELlEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 155 IFFDEPTTGLDPIRARAIDALI-----RGI--------VTETgataLTIThdmasvarigDRVALLQGGRI 212
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIrhlkeRGIgvlitdhnVRET----LGIC----------DRAYIISEGKV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-227 |
6.92e-30 |
|
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: 114.05 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTFGATRvLDgVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----GFGMLFQ 82
Cdd:TIGR02142 5 FSKRLGDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GAALFDSLSVWQNVAFRLRQRMSDDRArgIALDKLARV-GLGPeTADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:TIGR02142 83 EARLFPHLSVRGNLRYGMKRARPSERR--ISFERVIELlGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 162 TGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPAL 227
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
1.96e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.56 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR---AARARFLAgf 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtpsRELAKRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 gMLFQGAALFDSLSVWQNVAF--------RLRQrmsDDRArgiALDK-LARVGLGPeTADLMPAELSGGMAKRAGLARAI 148
Cdd:COG4604 79 -ILRQENHINSRLTVRELVAFgrfpyskgRLTA---EDRE---IIDEaIAYLDLED-LADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-216 |
2.52e-29 |
|
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: 110.11 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF----------GATR-----------VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILW 60
Cdd:cd03267 1 IEVSNLSKSYrvyskepgliGSLKslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 61 QG-RPLDRaaRARFLAGFGMLF-QGAALFDSLSVWQnvAFRLRQRM---SDDRARGiALDKLAR-VGLGPETaDLMPAEL 134
Cdd:cd03267 81 AGlVPWKR--RKKFLRRIGVVFgQKTQLWWDLPVID--SFYLLAAIydlPPARFKK-RLDELSElLDLEELL-DTPVRQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 135 SGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVH 214
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
..
gi 1608348115 215 DG 216
Cdd:cd03267 235 DG 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
4.92e-29 |
|
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: 109.06 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-----GATR--VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRIL--WQGRPLD--RAA 69
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrHDGGWVDlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFLA------GFGMLF------QGAalfdsLSVwqnVAFRLRQR-MSDDRARGIALDKLARVGLGPETADLMPAELSG 136
Cdd:COG4778 84 PREILAlrrrtiGYVSQFlrviprVSA-----LDV---VAEPLLERgVDREEARARARELLARLNLPERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 137 GMAKRAGLARAIADDPQIIFFDEPTTGLDPI-RARAIDaLIRGIvTETGATALTITHDMASVARIGDRVALLQGGR 211
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAAnRAVVVE-LIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-222 |
6.81e-29 |
|
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: 108.64 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRaaraRFLAGFGMLF 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR----KDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAFR-LRQRMSDDRARGIaldkLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHtTLLGLPDSRIDEV----LNIVDLT-NTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 161 TTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMD 222
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINKSE 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-216 |
7.49e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.95 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 18 DGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA---GFGMLFQG--AALFDSLSV 92
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 93 WQNVAFRLRQ---RMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLD-PIR 168
Cdd:PRK15079 118 GEIIAEPLRTyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDvSIQ 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 169 ARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK15079 198 AQVVN-LLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-229 |
2.53e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 107.86 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLqkTFGATRVL-DGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAP----EAGRILWQGRPLDRAA-RARFLA 75
Cdd:PRK10418 5 IELRNI--ALQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAlRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 gfgmlfqgaalfdslSVWQN--VAFRLRQRMSDD-----RARGIA------LDKLARVGLG--PETADLMPAELSGGMAK 140
Cdd:PRK10418 83 ---------------TIMQNprSAFNPLHTMHTHaretcLALGKPaddatlTAALEAVGLEnaARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 141 RAGLARAIADDPQIIFFDEPTTGLDPI-RARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVaQARILD-LLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE 226
|
250
....*....|
gi 1608348115 220 GMDAAPALAA 229
Cdd:PRK10418 227 TLFNAPKHAV 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
3.02e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 108.74 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARflAGFGML 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHAR--QRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQ---RMSDDRARGIALDKLARVglgPETADLMPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYfglSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIVTeTGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
3.57e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.63 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGAT-----RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQ--------------- 61
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 62 -------GRPLDR------AARARFlagfGMLFQGA--ALFDSlSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGPE 125
Cdd:PRK13651 83 vleklviQKTRFKkikkikEIRRRV----GVVFQFAeyQLFEQ-TIEKDIIFGPVSMgVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 126 TADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIdALIRGIVTETGATALTITHDMASVARIGDRVA 205
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|.
gi 1608348115 206 LLQGGRIVHDG 216
Cdd:PRK13651 237 FFKDGKIIKDG 247
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-219 |
5.67e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGL-----QKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQG-RPLDRAARARFL- 74
Cdd:PRK13637 3 IKIENLthiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 AGFGMLFQ--GAALFDSlSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLGPET-ADLMPAELSGGMAKRAGLARAIAD 150
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLgLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-219 |
6.77e-28 |
|
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: 111.00 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFdSLSVWQNVAFrLRQRMSDDRARgialDKLARVGLGPETADLmP-----------AELSGGMAKRAGLARAIA 149
Cdd:COG4988 417 PQNPYLF-AGTIRENLRL-GRPDASDEELE----AALEAAGLDEFVAAL-PdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 150 DDPQIIFFDEPTTGLDPIRARAIDALIRGIVteTGATALTITHDMASVARIgDRVALLQGGRIVHDGPVA 219
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHE 556
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
6.96e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 108.25 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----------GATR-----------VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRIL 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 60 WQGR-PLDRaaRARFLAGFGMLF-QGAALFDSLSVWQNvaFRLRQRM---SDDRARGiALDKLARV-GLGpetaDLM--P 131
Cdd:COG4586 81 VLGYvPFKR--RKEFARRIGVVFgQRSQLWWDLPAIDS--FRLLKAIyriPDAEYKK-RLDELVELlDLG----ELLdtP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 132 A-ELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGG 210
Cdd:COG4586 152 VrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250
....*....|.
gi 1608348115 211 RIVHDGPVAGM 221
Cdd:COG4586 232 RIIYDGSLEEL 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
7.20e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 105.73 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARAR--FL-AG 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpFLrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDSLSVWQNVAFRL----------RQRMSddrargIALDKlarVGLgPETADLMPAELSGGMAKRAGLAR 146
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLiiagasgddiRRRVS------AALDK---VGL-LDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 147 AIADDPQIIFFDEPTTGLDpiraraiDALIRGIV------TETGATALTITHDMASVARIGDRVALLQGGRIV--HDG 216
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD-------DALSEGILrlfeefNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHggVGG 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
1.44e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.25 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL----EAPEAgRILWQGRPLDRAAR-ARFL- 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVQREGRlARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 ---AGFGMLFQGAALFDSLSVWQNV-------------AFRLRQRMSDDRArgiaLDKLARVGLGpETADLMPAELSGGM 138
Cdd:PRK09984 83 ksrANTGYIFQQFNLVNRLSVLENVligalgstpfwrtCFSWFTREQKQRA----LQALTRVGMV-HFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 139 AKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-216 |
1.60e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 13 ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----GFGMLFQ--GAAL 86
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpvrkKVGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 87 FDSlSVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:PRK13643 98 FEE-TVLKDVAFGPQNfGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 166 PiRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13643 177 P-KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
2.26e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.24 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-GATRVLDGVDLTVGQGEsLCVI-GQSGTGKSVLLKCILGLEAPEAGRILWQGR------PLDRaarar 72
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGE-FIVLvGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelePADR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 flaGFGMLFQGAALFDSLSVWQNVAFRLRQR-MS-DDRARGIAldKLAR-VGLGPeTADLMPAELSGGMAKRAGLARAIA 149
Cdd:PRK11650 77 ---DIAMVFQNYALYPHMSVRENMAYGLKIRgMPkAEIEERVA--EAARiLELEP-LLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 150 DDPQIIFFDEPTTGLDP-IRArAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAkLRV-QMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-223 |
2.78e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARA--RFLAGFGMLFQGA--ALFdS 89
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQDPdnQLF-S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 90 LSVWQNVAF-RLRQRMSDDRARGIALDKLARVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR 168
Cdd:PRK13636 98 ASVYQDVSFgAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 169 ARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDA 223
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
3.95e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.69 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARfLAGFGML 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ-IARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 --FQGAALFDSLSVWQNV--------------------AFRLRQRMSDDRArgiaLDKLARVGLGpETADLMPAELSGGM 138
Cdd:PRK11300 84 rtFQHVRLFREMTVIENLlvaqhqqlktglfsgllktpAFRRAESEALDRA----ATWLERVGLL-EHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 139 AKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
4.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLqkTFGATR----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAG 76
Cdd:PRK13632 7 MIKVENV--SFSYPNsennALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGA-ALFDSLSVWQNVAFRLRQRMSD-DRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQI 154
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKKVPpKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 155 IFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVArIGDRVALLQGGRIVHDG 216
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-217 |
4.73e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.54 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCI-----LGLEAPEAGRILWQGR----PLDRAARAR 72
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRniysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 flAGFGMLFQGAALFDSLSVWQNVAFRLR-------QRMSDDRARGiALDKLArvgLGPETADLM---PAELSGGMAKRA 142
Cdd:PRK14267 85 --REVGMVFQYPNPFPHLTIYDNVAIGVKlnglvksKKELDERVEW-ALKKAA---LWDEVKDRLndyPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 143 GLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-213 |
6.09e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFL----AGFGMLFQ--GAALFDSl 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpvrKRIGMVFQfpESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 91 SVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRA 169
Cdd:PRK13646 102 TVEREIIFGPKNfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1608348115 170 RAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIV 213
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
6.47e-27 |
|
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: 104.01 E-value: 6.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAG---RILwqGRPLDRAA----RARF 73
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDvwelRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 laGF-----GMLFQGA---------ALFDSLSVWQNVafrlrqrmsDDRARGIALDKLARVGLGpETADLMPAELSGGMA 139
Cdd:COG1119 81 --GLvspalQLRFPRDetvldvvlsGFFDSIGLYREP---------TDEQRERARELLELLGLA-HLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 140 KRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
250
....*....|...
gi 1608348115 220 GMDAAPALAAFLG 232
Cdd:COG1119 229 EVLTSENLSEAFG 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-209 |
7.48e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.36 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR---AARARFL-AGFGMLFQGAALFDS 89
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAELRnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 90 LSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR 168
Cdd:PRK11629 102 FTALENVAMPLLiGKKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1608348115 169 ARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG 209
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
1.27e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAAR--ARFLAgf 77
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRqlARRLA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 gMLFQGAALFDSLSVWQNVAF------RLRQRMS-DDRAR-GIALDKLARVGLgpetADLMPAELSGGMAKRAGLARAIA 149
Cdd:PRK11231 80 -LLPQHHLTPEGITVRELVAYgrspwlSLWGRLSaEDNARvNQAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 150 DDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
1.80e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCI-----LGLEAPEAGRILWQGRPL--DRAARARF 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 LAGFGMLFQGAALFdSLSVWQNVAFRLRQRMSDDRARgiaLDK-----LARVGLGPETADLMPAE---LSGGMAKRAGLA 145
Cdd:PRK14239 85 RKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQV---LDEaveksLKGASIWDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 146 RAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
.
gi 1608348115 226 A 226
Cdd:PRK14239 239 K 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
2.81e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRpldraARARFLAgfgmlfQG 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----LRIGYLP------QE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 84 AALFDSLSVWQNVA-------------FRLRQRMSDDRARGIALDKL-------------ARV-------GLGPETADLM 130
Cdd:COG0488 70 PPLDDDLTVLDTVLdgdaelraleaelEELEAKLAEPDEDLERLAELqeefealggweaeARAeeilsglGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 131 PAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpirARAIDALIRGIVTETGaTALTITHDMASVARIGDRVALLQGG 210
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLEEFLKNYPG-TVLVVSHDRYFLDRVATRILELDRG 225
|
..
gi 1608348115 211 RI 212
Cdd:COG0488 226 KL 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
5.17e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEA--PEAGRIL----------WQGRP----- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 65 ------------------LDRAARARFLAGFGMLFQGA-ALFDSLSVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLGP 124
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEiGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 125 ETADLmPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRV 204
Cdd:TIGR03269 161 RITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|..
gi 1608348115 205 ALLQGGRIVHDG 216
Cdd:TIGR03269 240 IWLENGEIKEEG 251
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
5.84e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL--DRAARARFLAGF 77
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGA--ALFdSLSVWQNVAF-RLRQRMSDDRARGIALDKLARVGL-GPEtaDLMPAELSGGMAKRAGLARAIADDPQ 153
Cdd:PRK13639 81 GIVFQNPddQLF-APTVEEDVAFgPLNLGLSKEEVEKRVKEALKAVGMeGFE--NKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 154 IIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
5.92e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.19 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGM 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGA--ALFdSLSVWQNVAFRLRQRMSDDRARGIALDKLAR-VGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:PRK13652 83 VFQNPddQIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHmLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAA 229
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-225 |
8.94e-26 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 100.81 E-value: 8.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRA---ARARflAGFGML 80
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmhERAR--LGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENImaVLEIRKDLDRAEREERLEALLEEFQIS-HLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 159 EPTTGLDPIRARAIDALIRgIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIK-HLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-216 |
9.81e-26 |
|
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: 100.64 E-value: 9.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFdSLSVWQN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFrlrQRMSDDRARGIALDKLAR----VGLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPI 167
Cdd:cd03252 96 IAL---ADPGMSMERVIEAAKLAGahdfISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1608348115 168 RARAIDALIRGIVteTGATALTITHDMASVaRIGDRVALLQGGRIVHDG 216
Cdd:cd03252 173 SEHAIMRNMHDIC--AGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-236 |
1.15e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAF-------RLRQRMSDDRArgiALDK-LARVGLGpETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMgrtphrsRFDTWTETDRA---AVERaMERTGVA-QFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIVtETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLG 232
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
....
gi 1608348115 233 RSPA 236
Cdd:PRK09536 238 ARTA 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-216 |
1.59e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.19 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTfGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFL----AGFGMLFQ 82
Cdd:PRK10070 35 LEKT-GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GAALFDSLSVWQNVAFRLR-QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMElAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 162 TGLDP-IRARAIDALIRgIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK10070 193 SALDPlIRTEMQDELVK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-217 |
1.99e-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: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSl 90
Cdd:COG4618 342 GSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 91 SVWQNVAfrlrqRMSD-DRARGIALDKLARV-----GLgPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:COG4618 421 TIAENIA-----RFGDaDPEKVVAAAKLAGVhemilRL-PDGYDTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 161 TTGLDpirARAIDALIRGIVT--ETGATALTITHDMaSVARIGDRVALLQGGRIVHDGP 217
Cdd:COG4618 495 NSNLD---DEGEAALAAAIRAlkARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-225 |
2.40e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.58 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 5 RGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL---DRAARARFLAGFGMLF 81
Cdd:PRK11308 19 RGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAalFDSLSVWQNVAFRLRQRM----SDDRA--RGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:PRK11308 99 QNP--YGSLNPRKKVGQILEEPLlintSLSAAerREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 156 FFDEPTTGLD-PIRARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:PRK11308 177 VADEPVSALDvSVQAQVLN-LMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-212 |
3.63e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGA-ALFDSLSVWQN 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLR-QRMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDA 174
Cdd:PRK13650 103 VAFGLEnKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1608348115 175 LIRGIVTETGATALTITHDMASVArIGDRVALLQGGRI 212
Cdd:PRK13650 182 TIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-216 |
3.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGF----GMLFQGA--ALFD 88
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIrkkvGLVFQFPesQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 89 SlSVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPI 167
Cdd:PRK13649 101 E-TVLKDVAFGPQNfGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1608348115 168 RARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13649 180 GRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-217 |
5.81e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGF----GMLFQ--GAALFDSl 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrkkvSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 91 SVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPiRA 169
Cdd:PRK13641 102 TVLKDVEFGPKNfGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP-EG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1608348115 170 RAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIV-HDGP 217
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIkHASP 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-217 |
7.03e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.55 E-value: 7.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFdSLS 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAFRlRQRMSDDRARGIAldKLARVGlgpETADLMP-----------AELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:COG1132 430 IRENIRYG-RPDATDEEVEEAA--KAAQAH---EFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 161 TTGLDP-----IRaRAIDALIRgivtetGATALTITHDMASVARiGDRVALLQGGRIVHDGP 217
Cdd:COG1132 504 TSALDTetealIQ-EALERLMK------GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-208 |
1.08e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlS 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAF--RLRQRMSDDRArgiALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRA 169
Cdd:PRK10247 97 VYDNLIFpwQIRNQQPDPAI---FLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1608348115 170 RAIDALIRGIVTETGATALTITHDMASVARiGDRVALLQ 208
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-216 |
1.18e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL------EAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDS 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 90 LSVWQNVAFRLRQRMSDDR--ARGIALDKLARVGLGPETADLM--PA-ELSGGMAKRAGLARAIADDPQIIFFDEPTTGL 164
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKreIKKIVEECLRKVGLWKEVYDRLnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 165 DPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-214 |
1.24e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWqGRPLDraararflagFGML 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFD-SLSVWQNVAfRLRQRMSDDRARGIaldkLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:COG0488 384 DQHQEELDpDKTVLDELR-DGAPGGTEQEVRGY----LGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 160 PTTGLDPiraRAIDALIRGIVTETGaTALTITHDMASVARIGDRVALLQGGRIVH 214
Cdd:COG0488 459 PTNHLDI---ETLEALEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-228 |
1.84e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.24 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 11 FGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAP-----EAGRILWQGRPL-DRAARARFLAGFGMLFQGA 84
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 85 ALFdSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLGPETADLM---PAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK14271 111 NPF-PMSIMDNVlaGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALA 228
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
3.11e-24 |
|
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: 95.07 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFG--ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAgFGM 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-ISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSlSVWQNVAFRlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03247 80 LNQRPYLFDT-TLRNNLGRR----------------------------------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLDPIRARAIDALIRGiVTEtGATALTITHDMASVARIgDRVALLQGGRIVHDG 216
Cdd:cd03247 125 PTVGLDPITERQLLSLIFE-VLK-DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-209 |
5.38e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCI-----LGLEAPEAGRILWQGRPL--DRAARARFL 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 AGFGMLFQGAALFdSLSVWQNVAFRL-----RQRMSDDrarGIALDKLARVGLGPETADLM---PAELSGGMAKRAGLAR 146
Cdd:PRK14258 88 RQVSMVHPKPNLF-PMSVYDNVAYGVkivgwRPKLEID---DIVESALKDADLWDEIKHKIhksALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 147 AIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG 209
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-217 |
6.21e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.80 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKcILG-LEAPEAGRILWQGR---PLDRAARAR 72
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGcLDKPTSGTYRVAGQdvaTLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FL-AGFGMLFQGAALFDSLSVWQNV---AFRLRQRMSDDRARGIALdkLARVGLGpETADLMPAELSGGMAKRAGLARAI 148
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVevpAVYAGLERKQRLLRAQEL--LQRLGLE-DRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDmASVARIGDRVALLQGGRIVHDGP 217
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPP 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-216 |
6.84e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.61 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 8 QKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRI------------------LWQGRPLDRAA 69
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhelitNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 RARFLAGFGMLFQGAALFDSlSVWQNVAF---RLRQrmSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLAR 146
Cdd:PRK13631 113 ELRRRVSMVFQFPEYQLFKD-TIEKDIMFgpvALGV--KKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 147 AIADDPQIIFFDEPTTGLDPIRARAIDALIRGiVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-216 |
7.21e-24 |
|
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: 95.42 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA---GRILWQGRPLDRAaraRFLAGFGMLFQGAALFDSLS 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAF----RLRQRMSDDRARGIALDK-LARVGLGPETADLMPAeLSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP 166
Cdd:cd03234 98 VRETLTYtailRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 167 IRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-216 |
1.70e-23 |
|
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: 94.19 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFdSLSVWQN 95
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAfrLRQRMSDDR-----ARGIALDKLARvgLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLD- 165
Cdd:cd03245 98 IT--LGAPLADDErilraAELAGVTDFVN--KHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDm 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 166 PIRARAIDALIRGIVTEtgaTALTITHDMaSVARIGDRVALLQGGRIVHDG 216
Cdd:cd03245 174 NSEERLKERLRQLLGDK---TLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-226 |
1.98e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL-EAPEA----GRILWQGRPLDRA--ARARFLAG--FGMLFQGAA 85
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlPSPPVvypsGDIRFHGESLLHAseQTLRGVRGnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 86 LfdSLSVWQNV------AFRLRQRMSDDRARGIALDKLARVGLGPETADL--MPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:PRK15134 103 V--SLNPLHTLekqlyeVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA 226
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-235 |
4.72e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR------PLDRaararflaGF 77
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvpPAER--------GV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAFRL---------RQRMSDDRARGIALDKLarvglgpetADLMPAELSGGMAKRAGLARAI 148
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLklagakkeeINQRVNQVAEVLQLAHL---------LDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA-- 226
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAnr 228
|
250
....*....|
gi 1608348115 227 -LAAFLGrSP 235
Cdd:PRK11000 229 fVAGFIG-SP 237
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-225 |
4.90e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.19 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL-EAP---EAGRILWQGRPL----DRAARARFLAGFGMLFQGA-- 84
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDLqrisEKERRNLVGAEVAMIFQDPmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 85 ALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLgPETA---DLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK11022 101 SLNPCYTVGFQImeAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLD-PIRARAIDALIRGIVTETGATALtITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAP 225
Cdd:PRK11022 180 PTTALDvTIQAQIIELLLELQQKENMALVL-ITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-206 |
6.07e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 11 FGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRIlwqgrpldRAARARFLAgfgMLFQGAALFDSL 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGARVA---YVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 91 --SVWQNVAF-----RLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTG 163
Cdd:NF040873 71 plTVRDLVAMgrwarRGLWRRLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1608348115 164 LDPIRARAIDALIRGIVtETGATALTITHDMASVARIGDRVAL 206
Cdd:NF040873 150 LDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-239 |
7.75e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 7.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRA--ARARFLaGFG 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpAKAHQL-GIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAALFDSLSVWQNVAFRLRQRMSDDR-------ARGIALDKLARVGLgPETADLMPAELsggmakRAGLARaiadD 151
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPKRQASMQkmkqllaALGCQLDLDSSAGS-LEVADRQIVEI------LRGLMR----D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVtETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFL 231
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAIT 237
|
....*...
gi 1608348115 232 GRSPAQSA 239
Cdd:PRK15439 238 PAAREKSL 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
8.37e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF-----------------GATR-----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrRRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 59 LWQGRpldraarARFLAGFGMLFQGaalfdSLSVWQNVAFRlrqrmsddrargialdklARV-GLGP-ETADLMP----- 131
Cdd:COG1134 84 EVNGR-------VSALLELGAGFHP-----ELTGRENIYLN------------------GRLlGLSRkEIDEKFDeivef 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 132 AEL-----------SGGMAKRAGLARAIADDPQIIFFDEPT-TGLDPIRARAIDAlIRGIVtETGATALTITHDMASVAR 199
Cdd:COG1134 134 AELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLaVGDAAFQKKCLAR-IRELR-ESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|
gi 1608348115 200 IGDRVALLQGGRIVHDGPVA 219
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPE 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.39e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGA--ALFdSLSVWQNVAF-----RLRQRMSDDRARgialDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQ 153
Cdd:PRK13647 85 FQDPddQVF-SSTVWDDVAFgpvnmGLDKDEVERRVE----EALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 154 IIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-217 |
1.54e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.69 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 27 GESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA---GFGMLFQGAalFDSLSVWQNVAF----- 98
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDP--YASLDPRQTVGDsimep 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 99 -RLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLD-PIRARAIDALI 176
Cdd:PRK10261 428 lRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1608348115 177 rGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:PRK10261 508 -DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-216 |
1.80e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.16 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 9 KTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGF----GMLFQ-- 82
Cdd:PRK13634 15 KTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLrkkvGIVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GAALFDSlSVWQNVAF-RLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:PRK13634 95 EHQLFEE-TVEKDICFgPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 162 TGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-225 |
2.25e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATR-----VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD----- 66
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 67 -RAARARflagfgMLFQGAAlfDSLSVWQ------NVAFRLRQRMS-DDRARGIaLDKLARVGLGPETADLMPAELSGGM 138
Cdd:PRK15112 84 yRSQRIR------MIFQDPS--TSLNPRQrisqilDFPLRLNTDLEpEQREKQI-IETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 139 AKRAGLARAIADDPQIIFFDEPTTGLD-PIRARAIDaLIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDmSMRSQLIN-LMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
....*...
gi 1608348115 218 VAGMDAAP 225
Cdd:PRK15112 234 TADVLASP 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-212 |
2.68e-22 |
|
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: 90.18 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQktfgATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-RAARARFLAGFGML- 80
Cdd:cd03215 6 EVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 --FQGAALFDSLSVWQNVAfrlrqrmsddrargialdklarvglgpetadlMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:cd03215 82 edRKREGLVLDLSVAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 159 EPTTGLDpIRARA-IDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:cd03215 130 EPTRGVD-VGAKAeIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
3.08e-22 |
|
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: 94.66 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTF-GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSlSVWQNVAFRLRQRMSDDRARGialdkLARVGLGPETADLM----------PAELSGGMAKRAGLARAIAD 150
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPDASDAEIREA-----LERAGLDEFVAALPqgldtpigegGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVteTGATALTITHDMASVAR 199
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL 522
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-194 |
5.53e-22 |
|
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: 89.86 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRaARARFLAGFGMLF 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAFrlrqrMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:cd03231 80 HAPGIKTTLSVLENLRF-----WHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|...
gi 1608348115 162 TGLDPIRARAIDALIRGIVTETGATALTITHDM 194
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDL 186
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-217 |
6.63e-22 |
|
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: 90.37 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFND-TIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRlRQRMSDD---RARGIAL--DKLARVglgPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP 166
Cdd:cd03253 95 IRYG-RPDATDEeviEAAKAAQihDKIMRF---PDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 167 IRARAIDALIRGIVteTGATALTITHDMASVARiGDRVALLQGGRIVHDGP 217
Cdd:cd03253 171 HTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-219 |
7.70e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARFlaGF 77
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQL--GI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAF-RLRQR-------MSDDRARGIALDKLARVGLGPETaDLMPAELSGGMAKRAGLARAIA 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIgRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 150 DDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVA 219
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-197 |
2.97e-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: 87.80 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLdraARARFLAGFGMLF 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---AEQRDEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QG--AALFDSLSVWQNVAFRLRQRMSDDRArgiALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:TIGR01189 78 LGhlPGLKPELSALENLHFWAAIHGGAQRT---IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASV 197
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-226 |
3.50e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEaGRILWQGRPLDRAARARFLA---GFGMLFQ- 82
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPvrhRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 -GAALFDSLSVWQNVAFRLR---------QRmsddRARGIALdkLARVGLGPETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:PRK15134 371 pNSSLNPRLNVLQIIEEGLRvhqptlsaaQR----EQQVIAV--MEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA 226
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-218 |
5.54e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 90.18 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTG--KSVLLKCILGleaPEAGRILWQGRP--LDRAARARFLAGF 77
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TwcANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAAlfDSLSVWQNVAFRLRQ-RMSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:NF000106 91 RPVR*GRR--ESFSGRENLYMIGR*lDLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPV 218
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-216 |
7.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRI------------LWQGRplDRAararflagfGMLFQG 83
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWDIR--NKA---------GMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 84 ------AALfdslsVWQNVAF----------RLRQRMSDdrargialdKLARVGLGpETADLMPAELSGGMAKRAGLARA 147
Cdd:PRK13633 94 pdnqivATI-----VEEDVAFgpenlgippeEIRERVDE---------SLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 148 IADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARiGDRVALLQGGRIVHDG 216
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-237 |
8.31e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 8.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLqktfGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-RAARARFLAGFGML- 80
Cdd:COG1129 258 EVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 ----FQGaaLFDSLSVWQNVA------FRLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIAD 150
Cdd:COG1129 334 edrkGEG--LVLDLSIRENITlasldrLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 151 DPQIIFFDEPTTGLDpIRARA-IDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAA 229
Cdd:COG1129 412 DPKVLILDEPTRGID-VGAKAeIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAA 489
|
....*...
gi 1608348115 230 FLGRSPAQ 237
Cdd:COG1129 490 ATGGAAAA 497
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-218 |
1.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATR--VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA---GRILWQGRPLDRAARARFLAG 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGA-ALFDSLSVWQNVAFRLRQR-MSDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQI 154
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRaVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 155 IFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASvARIGDRVALLQGGRIV-HDGPV 218
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLaQGSPV 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-206 |
2.65e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLdRAARARFLAgfGML 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-RRQRDEYHQ--DLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQG--AALFDSLSVWQNVAF--RLRQRMSDDRARgialDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:PRK13538 78 YLGhqPGIKTELTALENLRFyqRLHGPGDDEALW----EALAQVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVAL 206
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-217 |
4.93e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.88 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPE----AGRILWQGRPLDR--AAR 70
Cdd:COG4170 3 LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKlsPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 71 ARFLAG--FGMLFQ------------GAALFDSLSVWQnVAFRLRQRMSDDRARGIALdkLARVGLgPETADLM---PAE 133
Cdd:COG4170 83 RRKIIGreIAMIFQepsscldpsakiGDQLIEAIPSWT-FKGKWWQRFKWRKKRAIEL--LHRVGI-KDHKDIMnsyPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIV 213
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
....
gi 1608348115 214 HDGP 217
Cdd:COG4170 239 ESGP 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-234 |
5.02e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-RAARARFLAGFGMLF 81
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVAF-RLRQRM---SDDRARGIALDKLARVGLgpetaDLMP----AELSGGMAKRAGLARAIADDPQ 153
Cdd:PRK11288 86 QELHLVPEMTVAENLYLgQLPHKGgivNRRLLNYEAREQLEHLGV-----DIDPdtplKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 154 IIFFDEPTTGLDpirARAIDALIRgIVTE---TGATALTITHDMASVARIGDRVALLQGGRIVHDGP-VAGMDAAPALAA 229
Cdd:PRK11288 161 VIAFDEPTSSLS---AREIEQLFR-VIRElraEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQA 236
|
....*
gi 1608348115 230 FLGRS 234
Cdd:PRK11288 237 MVGRE 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-193 |
5.21e-20 |
|
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: 88.19 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlS 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAFRlRQRMSDDRArgiaLDKLARVGLGPETADL----------MPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:TIGR02868 425 VRENLRLA-RPDATDEEL----WAALERVGLADWLRALpdgldtvlgeGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 1608348115 162 TGLDPIRARAIDALIRGivTETGATALTITHD 193
Cdd:TIGR02868 500 EHLDAETADELLEDLLA--ALSGRTVVLITHH 529
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-235 |
5.98e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGrpLDRAARARfLAGF----GMLFQGAAL-FD 88
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSK-LQGIrklvGIVFQNPETqFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 89 SLSVWQNVAF----------RLRQRMsdDRArgialdkLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PRK13644 92 GRTVEEDLAFgpenlclppiEIRKRV--DRA-------LAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVaRIGDRVALLQGGRIVHDGPVAGMDAAPALaAFLGRSP 235
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSL-QTLGLTP 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-216 |
6.57e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 8 QKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQG-------RPLDRAARARFLAGFGML 80
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSlSVWQNVAFRLRQRMSDDRARGIALDKLAR-VGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK13645 98 FPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-216 |
9.33e-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: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPldraaraRFLAGFGMLFQGaalfdSLSVWQ 94
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------SSLLGLGGGFNP-----ELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 95 NVAFRLR-QRMSDDRARgialDKLARV----GLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP-IR 168
Cdd:cd03220 104 NIYLNGRlLGLSRKEID----EKIDEIiefsELG-DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAaFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 169 ARAIDAlIRGIVtETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03220 179 EKCQRR-LRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-217 |
1.27e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRP---LDRAARARflAGFGMLFQG 83
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDislLPLHARAR--RGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 84 AALFDSLSVWQNV--AFRLRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:PRK10895 87 ASIFRRLSVYDNLmaVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 162 TGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALL-QGGRIVHDGP 217
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVsQGHLIAHGTP 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-233 |
1.38e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 87.19 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL--EAPEAGRILWQGRPLD-RAARARFLAGF 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKaSNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 GMLFQGAALFDSLSVWQNVAFRLR-----QRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLG 232
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
.
gi 1608348115 233 R 233
Cdd:TIGR02633 240 R 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
1.83e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAA-LFDSLSVWQN 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQRM-SDDRARGIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDA 174
Cdd:PRK13648 105 VAFGLENHAvPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1608348115 175 LIRGIVTETGATALTITHDMASVARiGDRVALLQGGRIVHDG 216
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-205 |
1.97e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKC-------ILGLEApeAGRILWQGRPL-----DRAA 69
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFRV--EGKVTFHGKNLyapdvDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 -RARFlagfGMLFQGAALFdSLSVWQNVAFRLR--------QRMSDDRARGIAL-----DKLARVGLGpetadlmpaeLS 135
Cdd:PRK14243 89 vRRRI----GMVFQKPNPF-PKSIYDNIAYGARingykgdmDELVERSLRQAALwdevkDKLKQSGLS----------LS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 136 GGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARIGDRVA 205
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTA 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-192 |
1.99e-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: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQKTFGATR------VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLE--APEAGRILWQGRPLDRaararfl 74
Cdd:COG2401 26 RVAIVLEAFGVELrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 agfgmlfqGAALFDSLSVWQNVAfrlrqrmsddrargIALDKLARVGLGpeTADLM---PAELSGGMAKRAGLARAIADD 151
Cdd:COG2401 99 --------EASLIDAIGRKGDFK--------------DAVELLNAVGLS--DAVLWlrrFKELSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITH 192
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-227 |
2.95e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEA--PEAGRILWQGRPL------DRAARARFL 74
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDIlelspdERARAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 AgfgmlFQ------GAALFDSLSVWQNVafRLRQRMSDDRARGIALDKLARVGLGPETADLMPAE-LSGGMAKRAGLARA 147
Cdd:COG0396 82 A-----FQypveipGVSVSNFLRTALNA--RRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 148 IADDPQIIFFDEPTTGLDpiraraIDALirGIVTET-------GATALTITHdmasVARIG-----DRVALLQGGRIVHD 215
Cdd:COG0396 155 LLLEPKLAILDETDSGLD------IDAL--RIVAEGvnklrspDRGILIITH----YQRILdyikpDFVHVLVDGRIVKS 222
|
250
....*....|..
gi 1608348115 216 GpvaGMDAAPAL 227
Cdd:COG0396 223 G---GKELALEL 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-212 |
5.67e-19 |
|
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: 82.52 E-value: 5.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 13 ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFdSLSV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLF-ARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 93 WQNVAFRLrQRMSDDRARGIAL-----DKLARVGLGPET-ADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP 166
Cdd:cd03248 105 QDNIAYGL-QSCSFECVKEAAQkahahSFISELASGYDTeVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1608348115 167 IRARAIDALIRGIVTETgaTALTITHDMASVARiGDRVALLQGGRI 212
Cdd:cd03248 184 ESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-216 |
7.00e-19 |
|
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: 85.18 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQRMSDD---RARGIA--LDKLARVGLGPETaDLMP--AELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR 168
Cdd:TIGR01193 568 LLLGAKENVSQDeiwAACEIAeiKDDIENMPLGYQT-ELSEegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 169 ARAIdalIRGIVTETGATALTITHDMaSVARIGDRVALLQGGRIVHDG 216
Cdd:TIGR01193 647 EKKI---VNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKIIEQG 690
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-211 |
7.71e-19 |
|
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: 79.80 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRpldraararflAGFGMLF 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QgaalfdslsvwqnvafrlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 162 TGLDPiraRAIDALIRGIVTETGaTALTITHDMASVARIGDRVALLQGGR 211
Cdd:cd03221 99 NHLDL---ESIEALEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.03e-18 |
|
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: 81.03 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA--GRILWQGRPL-DRAARARFLAGFG 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDItDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAAlfdslsvwqnvafrlrqrmsddRARGIALDKLAR-VGLGpetadlmpaeLSGGMAKRAGLARAIADDPQIIFF 157
Cdd:cd03217 81 LAFQYPP----------------------EIPGVKNADFLRyVNEG----------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIVTEtGATALTITHdmasVARI-----GDRVALLQGGRIVHDGPV 218
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH----YQRLldyikPDRVHVLYDGRIVKSGDK 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-216 |
1.78e-18 |
|
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: 84.29 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARArFLAGFGMLFQGAALFDSLSVWQNV 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 97 AF--RLRQRmSDDRARGIALDKLARVGLGPETADlMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAI-D 173
Cdd:TIGR01257 1025 LFyaQLKGR-SWEEAQLEMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIwD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1608348115 174 ALIRgivTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:TIGR01257 1103 LLLK---YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-222 |
1.80e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 3 EIRGLQ-KTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGfGMLF 81
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL-GVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 -----QGAALFDSLSVWQNVAFRLRQR--------MSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAI 148
Cdd:COG3845 338 ipedrLGRGLVPDMSVAENLILGRYRRppfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 149 ADDPQIIFFDEPTTGLDP-----IRARAIDAlirgivTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMD 222
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVgaiefIHQRLLEL------RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEAT 490
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-216 |
2.17e-18 |
|
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: 79.90 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEA--GRILWQGRPLDRAARARFLagfGMLFQGAALFDS 89
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKII---GYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 90 LSVWQNVAF--RLRQrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPI 167
Cdd:cd03213 97 LTVRETLMFaaKLRG-------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 168 RARAIDALIRGIVtETGATALTITHD-MASVARIGDRVALLQGGRIVHDG 216
Cdd:cd03213 146 SALQVMSLLRRLA-DTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-232 |
2.62e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSLSVWQN 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAF-------RLRQRMSDDRARgiALDKLARVGLGPETADLMPAeLSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR 168
Cdd:PRK10575 106 VAIgrypwhgALGRFGAADREK--VEEAISLVGLKPLAHRLVDS-LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 169 ARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLG 232
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
4.20e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARArFLAgfgML 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRG-LLA---LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDS-------LSVWQNVAFRLRQrmsddraRGIALDKLARvgLGPETADLMPAE---------LSGGMAKRAGL 144
Cdd:PRK13638 77 QQVATVFQDpeqqifyTDIDSDIAFSLRN-------LGVPEAEITR--RVDEALTLVDAQhfrhqpiqcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 145 ARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-233 |
5.26e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGE--SLCviGQSGTGKSVLLKCILGLeAPEA---GRILWQGRPLdraaRARFL- 74
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEivSLC--GENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEEL----QASNIr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 75 ----AGFGMLFQGAALFDSLSVWQNVaFRLRQ-----RMSDDRARGIALDKLARVGLgpetaDLMPA----ELSGGMAKR 141
Cdd:PRK13549 78 dterAGIAIIHQELALVKELSVLENI-FLGNEitpggIMDYDAMYLRAQKLLAQLKL-----DINPAtpvgNLGLGQQQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 142 AGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGM 221
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
250
....*....|..
gi 1608348115 222 DAAPALAAFLGR 233
Cdd:PRK13549 231 TEDDIITMMVGR 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-216 |
6.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGA-ALFDSLSVWQN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQRmsddrarGIALDKL-ARVGLGPETADLM------PAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR 168
Cdd:PRK13642 103 VAFGMENQ-------GIPREEMiKRVDEALLAVNMLdfktrePARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 169 ARAIDALIRGIVTETGATALTITHDMASVARiGDRVALLQGGRIVHDG 216
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-226 |
7.76e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 20 VDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR------------AARARFLAG--FGMLFQG-- 83
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqvielseqsAAQMRHVRGadMAMIFQEpm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 84 AALFDSLSVWQNVA--FRLRQRMSDDRARGIALDKLARVGLgPETADLM---PAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PRK10261 115 TSLNPVFTVGEQIAesIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILsryPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA 226
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-237 |
7.84e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.08 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-RAARARFLAGFGMLFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 83 GAALFDSLSVWQNV---------AFRLRQRMSDDRAR-----GIALDKLARVglgpetadlmpAELSGGMAKRAGLARAI 148
Cdd:PRK10982 81 ELNLVLQRSVMDNMwlgryptkgMFVDQDKMYRDTKAifdelDIDIDPRAKV-----------ATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 149 ADDPQIIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALA 228
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
|
....*....
gi 1608348115 229 AFLGRSPAQ 237
Cdd:PRK10982 229 MMVGRSLTQ 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
2.12e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDR---AARARFLAgf 77
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvAEACHYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 78 gmlfQGAALFDSLSVWQNVAFrlRQRMSDDRARGIAlDKLARVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:PRK13539 80 ----HRNAMKPALTVAENLEF--WAAFLGGEELDIA-AALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1608348115 158 DEPTTGLDpiraRAIDALIRGIVT---ETGATALTITH 192
Cdd:PRK13539 152 DEPTAALD----AAAVALFAELIRahlAQGGIVIAATH 185
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-225 |
4.83e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.69 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPE----AGRILWQGRPLDR-AARA 71
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRlSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 72 RF-LAG--FGMLFQ------------GAALFDSLSVWQNVAfRLRQRMSDDRARGIALdkLARVGLgPETADLM---PAE 133
Cdd:PRK15093 83 RRkLVGhnVSMIFQepqscldpservGRQLMQNIPGWTYKG-RWWQRFGWRKRRAIEL--LHRVGI-KDHKDAMrsfPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIV 213
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|..
gi 1608348115 214 HDGPVAGMDAAP 225
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-216 |
6.32e-17 |
|
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: 76.88 E-value: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFdSLSVWQNVafrlrqRMSDDRARG---IALDKLAR----VGLGPETADLMPAE----LSGGMAKRAGLARAIA 149
Cdd:cd03254 83 LQDTFLF-SGTIMENI------RLGRPNATDeevIEAAKEAGahdfIMKLPNGYDTVLGEnggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608348115 150 DDPQIIFFDEPTTGLDPIRARAIDALIRGIVteTGATALTITHDMASVaRIGDRVALLQGGRIVHDG 216
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-216 |
6.98e-17 |
|
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: 76.89 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRlRQRMSDDRARgialdKLARVGLGPETADLMP-----------AELSGGMAKRAGLARAIADDPQIIFFDEPTTGL 164
Cdd:cd03251 96 IAYG-RPGATREEVE-----EAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 165 DPIRARAIDALIRGIVteTGATALTITHDMASVARIgDRVALLQGGRIVHDG 216
Cdd:cd03251 170 DTESERLVQAALERLM--KNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-216 |
7.16e-17 |
|
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: 76.81 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQRMSDDRARGIaldKLAR-----VGLgPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP 166
Cdd:cd03249 97 IRYGKPDATDEEVEEAA---KKANihdfiMSL-PDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 167 ----IRARAIDALIRGIvtetgaTALTITHDMASVaRIGDRVALLQGGRIVHDG 216
Cdd:cd03249 173 esekLVQEALDRAMKGR------TTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-211 |
1.05e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.84 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTF----GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEaGRI----LWQGR--------P 64
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGReilnlpekE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 65 LDRAaRARFLAgfgMLFQGAalFDSLSVWQNVA------FRLRQRMSDDRARGIALDKLARVGLgPETADLM---PAELS 135
Cdd:PRK09473 91 LNKL-RAEQIS---MIFQDP--MTSLNPYMRVGeqlmevLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRMkmyPHEFS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 136 GGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGR 211
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-222 |
1.23e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-RAARARFLAGFGM 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVaFRLRQRMSddRARGIALDK--------LARVGLgPETADLMPAELSGGMAKRAGLARAIADD 151
Cdd:PRK10762 84 IHQELNLIPQLTIAENI-FLGREFVN--RFGRIDWKKmyaeadklLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIR-------GIVtetgatalTITHDMASVARIGDRVALLQGGRIVHDGPVAGMD 222
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRelksqgrGIV--------YISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
1.49e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRIlwqgrplDRAARARFlagfGML 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------KRNGKLRI----GYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLRQRMSddraRGIALDKLARVglgpETADLMPA---ELSGGMAKRAGLARAIADDPQIIFF 157
Cdd:PRK09544 73 PQKLYLDTTLPLTVNRFLRLRPGTK----KEDILPALKRV----QAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 158 DEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALL 207
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-216 |
2.56e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKT--FGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLF 81
Cdd:PRK10253 8 LRGEQLTlgYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNVA--------FRLRQRMSDDRARGIALDKLARVGLGPETADlmpaELSGGMAKRAGLARAIADDPQ 153
Cdd:PRK10253 88 QNATTPGDITVQELVArgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 154 IIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDG 216
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-217 |
3.39e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 22 LTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA----------GFGMLFQGAALfdsLS 91
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAyvpqseevdwSFPVLVEDVVM---MG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAFrLRQRMSDDRArgIALDKLARVGLgPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARA 171
Cdd:PRK15056 105 RYGHMGW-LRRAKKRDRQ--IVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1608348115 172 IDALIRGIVTEtGATALTITHDMASVARIGDRVALLQgGRIVHDGP 217
Cdd:PRK15056 181 IISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGP 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-244 |
9.40e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRgLQKTFGATRvLDgVDLTV-GQGESlCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLA---- 75
Cdd:PRK11144 1 MLELN-FKQQLGDLC-LT-VNLTLpAQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 76 GFGMLFQGAALFDSLSVWQNVAFRLRQRMSDDRARGIALdklarVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQII 155
Cdd:PRK11144 77 RIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVAL-----LGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 156 FFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLGRSp 235
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKE- 229
|
....*....
gi 1608348115 236 AQSAGFAAP 244
Cdd:PRK11144 230 EQSSILKVT 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-218 |
1.04e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 27 GESLCVIGQSGTGKSVLLKCILGLEAPE---AGRILWQGRPLDrAARARFLAGFGMlfQGAALFDSLSVWQNVAF----R 99
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-AKEMRAISAYVQ--QDDLFIPTLTVREHLMFqahlR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 100 LRQRMSDDRARGIALDKLARVGLGP------ETADLMPAeLSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAID 173
Cdd:TIGR00955 128 MPRRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1608348115 174 ALIRGIVTEtGATALTITHDMAS-VARIGDRVALLQGGRIVHDGPV 218
Cdd:TIGR00955 207 QVLKGLAQK-GKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-216 |
2.45e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.86 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFdSLSVWQN 95
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLF-SATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQrMSDDRARGIaldkLARVGL-----GPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP 166
Cdd:PRK11160 434 LLLAAPN-ASDEALIEV----LQQVGLeklleDDKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 167 IRARAIDALIRGIVteTGATALTITHDMASVARIgDRVALLQGGRIVHDG 216
Cdd:PRK11160 509 ETERQILELLAEHA--QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-219 |
5.35e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARFLAGFGML 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMaDARHRRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAA--LFDSLSVWQNVAF--RLRQRMSDDRARGIAlDKLARVGLGPeTADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:NF033858 82 PQGLGknLYPTLSVFENLDFfgRLFGQDAAERRRRID-ELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 157 FDEPTTGLDPIRARAIDALIRGIVTET-GATALTITHDMASVARIgDRVALLQGGRIVHDGPVA 219
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPA 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-215 |
6.76e-15 |
|
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: 73.32 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL-EAPEAGRILWQGRPLD-RAARARFLAGFGMLFQGA---ALFDSLS 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRkrhGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNV------AFRLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:TIGR02633 356 VGKNItlsvlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1608348115 166 PIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHD 215
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-209 |
7.36e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 6 GLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLfqgAA 85
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHL---PG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 86 LFDSLSVWQNVAFrlRQRMSDDRARGIALDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:PRK13543 93 LKADLSTLENLHF--LCGLHGRRAKQMPGSALAIVGLA-GYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 166 P----IRARAIDALIRgivteTGATALTITHDMASVARIGDRVALLQG 209
Cdd:PRK13543 170 LegitLVNRMISAHLR-----GGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-221 |
1.36e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 13 ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILG-LEAPEA-------GRILWQGRPLDRAARARFLAGFGMLFQGA 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 85 ALFDSLSVWQNVAF-----RLRQRMSDDRARGIALDKLARVGLGPETADLMpAELSGGMAKRAGLARAIAD--------- 150
Cdd:PRK13547 93 QPAFAFSAREIVLLgryphARRAGALTHRDGEIAWQALALAGATALVGRDV-TTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGM 221
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-232 |
2.30e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL---DRAARARFlagfG 78
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagDIATRRRV----G 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAALFDSLSVWQNVAF--RLRQRMSDDRARGIAlDKLARVGLGpETADLMPAELSGGMAKRAGLARAIADDPQIIF 156
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLELhaRLFHLPAAEIAARVA-EMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 157 FDEPTTGLDPIrARaiDALIRGIVT---ETGATALTITHDMASVARIgDRVALLQGGRI-VHDGPVAGMDA--APAL-AA 229
Cdd:NF033858 421 LDEPTSGVDPV-AR--DMFWRLLIElsrEDGVTIFISTHFMNEAERC-DRISLMHAGRVlASDTPAALVAArgAATLeEA 496
|
...
gi 1608348115 230 FLG 232
Cdd:NF033858 497 FIA 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-213 |
2.77e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKcILGLEAP-EAGRI----------LWQGRPldraa 69
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK-ILNGEVLlDDGRIiyeqdlivarLQQDPP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 70 raRFLAG--FGMLFQG-AALFDSLSVWQNVAFRLRQRMSD-------------DRARGIALDK-----LARVGLGPETad 128
Cdd:PRK11147 77 --RNVEGtvYDFVAEGiEEQAEYLKRYHDISHLVETDPSEknlnelaklqeqlDHHNLWQLENrinevLAQLGLDPDA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 129 lMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpiraraIDAL--IRGIVTETGATALTITHDMASVARIGDRVAL 206
Cdd:PRK11147 153 -ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD------IETIewLEGFLKTFQGSIIFISHDRSFIRNMATRIVD 225
|
....*..
gi 1608348115 207 LQGGRIV 213
Cdd:PRK11147 226 LDRGKLV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-232 |
2.90e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFL-AGFGM 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSLSVWQNVA----FRLRQRMSddrargialDKLARV-GLGP---ETADLMPAELSGGMAKRAGLARAIADD 151
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAmggfFAERDQFQ---------ERIKWVyELFPrlhERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPAL-AAF 230
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVrSAY 234
|
..
gi 1608348115 231 LG 232
Cdd:PRK11614 235 LG 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
2.25e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPE--AGRILWQGR------PLDRAARAR 72
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGEsildlePEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 73 FLAgfgmlFQ------GAALFDSLsvwqNVAFRLRQRMSDDRAR------GIALDKLARVGLGPETADLMPAE-LSGGMA 139
Cdd:CHL00131 87 FLA-----FQypieipGVSNADFL----RLAYNSKRKFQGLPELdpleflEIINEKLKLVGMDPSFLSRNVNEgFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 140 KRAGLARAIADDPQIIFFDEPTTGLDpiraraIDAL------IRGIVTETGATALtITHDMASVARIG-DRVALLQGGRI 212
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLD------IDALkiiaegINKLMTSENSIIL-ITHYQRLLDYIKpDYVHVMQNGKI 230
|
....
gi 1608348115 213 VHDG 216
Cdd:CHL00131 231 IKTG 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-229 |
3.91e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLeAPEAGRILWQG---RPLDRAARARFLAGFG---MLFQGaalf 87
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGielRELDPESWRKHLSWVGqnpQLPHG---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 88 dslSVWQNVAFRlRQRMSDDR-----ARGIALDKLARVGLGPETA--DLMpAELSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:PRK11174 438 ---TLRDNVLLG-NPDASDEQlqqalENAWVSEFLPLLPQGLDTPigDQA-AGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 161 TTGLDPIRARAI-DALIRGIvteTGATALTITHDMASVARIgDRVALLQGGRIVHDGPVAGMDAAPALAA 229
Cdd:PRK11174 513 TASLDAHSEQLVmQALNAAS---RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-217 |
4.54e-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: 65.90 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGA--TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGM 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 LFQGAALFDSlSVWQNVafRLRQRMSDDRARGiALdklaRVGLGPETadlmpaeLSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:cd03369 87 IPQDPTLFSG-TIRSNL--DPFDEYSDEEIYG-AL----RVSEGGLN-------LSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608348115 160 PTTGLDpiraRAIDALIRGIVTE--TGATALTITHDMASVARIgDRVALLQGGRIV-HDGP 217
Cdd:cd03369 152 ATASID----YATDALIQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVKeYDHP 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-213 |
1.15e-12 |
|
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: 66.77 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFND-TIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFrlrQRMSDDRARGIALDKLARV-----GLgPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP 166
Cdd:COG5265 452 IAY---GRPDASEEEVEAAARAAQIhdfieSL-PDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 167 IRARAI-DALIRgiVTEtGATALTITHDMASVARiGDRVALLQGGRIV 213
Cdd:COG5265 528 RTERAIqAALRE--VAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-216 |
1.30e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFdSLSVWQN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRqRMSDDRARGIALDKLAR--VGLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPira 169
Cdd:TIGR00958 575 IAYGLT-DTPDEEIMAAAKAANAHdfIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA--- 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1608348115 170 rAIDALIRGIVTETGATALTITHDMaSVARIGDRVALLQGGRIVHDG 216
Cdd:TIGR00958 651 -ECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-214 |
3.78e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRpldraararflAGFGMLF 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-----------ANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAA--------LFDSLSVWqnvafrlRQRMSDDRA-RGIaldkLARVGLGPETADLMPAELSGGMAKRAGLARAIADDP 152
Cdd:PRK15064 389 QDHAydfendltLFDWMSQW-------RQEGDDEQAvRGT----LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 153 QIIFFDEPTTGLDpirARAIDALIRGIVTETGaTALTITHDMASVARIGDRVALLQGGRIVH 214
Cdd:PRK15064 458 NVLVMDEPTNHMD---MESIESLNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-216 |
4.92e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.98 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 12 GATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALF---- 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFnrsi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 88 -DSLSVWQNVAFRLRQRMSDDRARgiALDKLARVGLGPETadlMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:PRK13657 426 eDNIRVGRPDATDEEMRAAAERAQ--AHDFIERKPDGYDT---VVGErgrqLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 163 GLDPIRAR----AIDALIRgivtetGATALTITHDMASVaRIGDRVALLQGGRIVHDG 216
Cdd:PRK13657 501 ALDVETEAkvkaALDELMK------GRTTFIIAHRLSTV-RNADRILVFDNGRVVESG 551
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-211 |
4.93e-12 |
|
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: 62.87 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRpldraararflagFGMLFQGAALFdSLSVWQN 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQ-NGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAF--RLRQRMSDDRARGIALDK-LARVGLGPETadlMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR 168
Cdd:cd03250 86 ILFgkPFDEERYEKVIKACALEPdLEILPDGDLT---EIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1608348115 169 ARAI-DALIRGIVTEtGATALTITHDMaSVARIGDRVALLQGGR 211
Cdd:cd03250 163 GRHIfENCILGLLLN-NKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-216 |
5.53e-12 |
|
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: 62.67 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL----EAPEaGRILWQGRPLDRAARArflagfgm 79
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFAEK-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 80 lFQGAALFDS--------LSVWQNVAFRLRQRmSDDRARGIaldklarvglgpetadlmpaelSGGMAKRAGLARAIADD 151
Cdd:cd03233 81 -YPGEIIYVSeedvhfptLTVRETLDFALRCK-GNEFVRGI----------------------SGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATAL--------TITHdmasvarIGDRVALLQGGRIVHDG 216
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFvslyqasdEIYD-------LFDKVLVLYEGRQIYYG 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-217 |
5.56e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 23 TVGQGESLCVIGQSGTGKSVLLKCILGLeAPEAGRILWQGRPLDRA-----ARAR-FLAGfgmlfQGAALFdSLSVWQNV 96
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWsaaelARHRaYLSQ-----QQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 97 AFRLRQRMSDDRARGiALDKLA-RVGLGpetaDLMP---AELSGGMAKRAGLA-------RAIADDPQIIFFDEPTTGLD 165
Cdd:PRK03695 91 TLHQPDKTRTEAVAS-ALNEVAeALGLD----DKLGrsvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 166 PIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:PRK03695 166 VAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-218 |
5.58e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEaPEA---GRILWQGRPLD----RAARARf 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRfkdiRDSEAL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 74 laGFGMLFQGAALFDSLSVWQNVaFrlrqrMSDDRAR-GI---------ALDKLARVGLGpETADLMPAELSGGMAKRAG 143
Cdd:NF040905 79 --GIVIIHQELALIPYLSIAENI-F-----LGNERAKrGVidwnetnrrARELLAKVGLD-ESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 144 LARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIV-----HDGPV 218
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIetldcRADEV 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-236 |
6.19e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILG-LEAPE-AGRILWQGRPLDRAARARFlagfGMLFQGAALFDSLSVW 93
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTKQILKRT----GFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 94 QNVAF----RLRQRMSDDRARGIALDKLARVGLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:PLN03211 159 ETLVFcsllRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 166 PIRA-RAIDALirGIVTETGATALTITHDMAS-VARIGDRVALLQGGRIVHDGpvAGMDAApALAAFLGRSPA 236
Cdd:PLN03211 239 ATAAyRLVLTL--GSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG--KGSDAM-AYFESVGFSPS 306
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-213 |
6.54e-12 |
|
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: 62.90 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVWQN 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRlrQRMSDDRARGIaldkLARVGLG------PETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:cd03244 98 LDPF--GEYSDEELWQA----LERVGLKefveslPGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1608348115 166 PIRARAIDALIRgivTE-TGATALTITHDMASVARIgDRVALLQGGRIV 213
Cdd:cd03244 172 PETDALIQKTIR---EAfKDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-232 |
7.00e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGL-EAPEAGRILWQGRPLD-RAARARFLAGFGML-----FQGaaLF 87
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVpedrkRDG--IV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 88 DSLSVWQNVA------FRLRQRMSDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:PRK13549 354 PVMGVGKNITlaaldrFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 162 TGLDpIRARA-IDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLG 232
Cdd:PRK13549 434 RGID-VGAKYeIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAALR 503
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-212 |
1.76e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.45 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDG-VDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAfrlrqrmSDDRARGIALDKLA-RVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDE 159
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKP-------ANPALVEKWLERLKmAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 160 PTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVARiGDRVALLQGGRI 212
Cdd:PRK10522 476 WAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-212 |
2.51e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 20 VDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR------PLDRAARarflagfGMLF-----QGAALFD 88
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKK-------GMAYitesrRDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 89 SLSVWQNVAF-------RLRQRM---SDDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PRK09700 355 NFSIAQNMAIsrslkdgGYKGAMglfHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 159 EPTTGLDpIRARA-IDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRI 212
Cdd:PRK09700 435 EPTRGID-VGAKAeIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-239 |
2.82e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 20 VDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL-DRAARARFLAGFGML---FQGAALFDSLSVWQN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLARGLVYLpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQRMS--DDRARGIA-LDKLAR-VGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpIRARA 171
Cdd:PRK15439 362 VCALTHNRRGfwIKPARENAvLERYRRaLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-VSARN 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 172 -IDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFLGRSPAQSA 239
Cdd:PRK15439 441 dIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFGEHQAQEA 508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-193 |
1.44e-10 |
|
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: 60.72 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILW----------QGRpldraara 71
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSR-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 72 rflagfgmlfqgAALFDSLSVWQNVA-----FRLRQRMSDDRA-------RGIalDKLARVGlgpetadlmpaELSGGMA 139
Cdd:TIGR03719 395 ------------DALDPNKTVWEEISggldiIKLGKREIPSRAyvgrfnfKGS--DQQKKVG-----------QLSGGER 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 140 KRAGLARAIADDPQIIFFDEPTTGLDPIRARAI-DALirgivTETGATALTITHD 193
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALeEAL-----LNFAGCAVVISHD 499
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-177 |
1.49e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGlEAPEA--------------GRILWQGRP--- 64
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfgrrrgsGETIWDIKKhig 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 65 -------LD----RAARARFLAGFgmlfqgaalFDSLSVWQNVAfrlrqrmsdDRARGIALDKLARVGLGPETADLMPAE 133
Cdd:PRK10938 340 yvssslhLDyrvsTSVRNVILSGF---------FDSIGIYQAVS---------DRQQKLAQQWLDILGIDKRTADAPFHS 401
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIR----ARAIDALIR 177
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNrqlvRRFVDVLIS 449
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-210 |
2.13e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILwqgRPldraararflAGFGMLF--------QGaa 85
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---RP----------AGARVLFlpqrpylpLG-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 86 lfdslsvwqnvafRLRQ---------RMSDDRARGIaldkLARVGLGP------ETADLmPAELSGGMAKRAGLARAIAD 150
Cdd:COG4178 441 -------------TLREallypataeAFSDAELREA----LEAVGLGHlaerldEEADW-DQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGivTETGATALTITHDmASVARIGDRVALLQGG 210
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-239 |
1.43e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQktfgATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLD-RAARARFLAGFgML 80
Cdd:PRK11288 258 LRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGI-ML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 ------FQGaaLFDSLSVWQNVAFRLRQRMS-------DDRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARA 147
Cdd:PRK11288 333 cpedrkAEG--IIPVHSVADNINISARRHHLragclinNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 148 IADDPQIIFFDEPTTGLDpIRARA-IDALIRGIvTETGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPA 226
Cdd:PRK11288 411 LSEDMKVILLDEPTRGID-VGAKHeIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQA 488
|
250
....*....|...
gi 1608348115 227 LAAFLGRSPAQSA 239
Cdd:PRK11288 489 LSLALPRTSAAVA 501
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
77-199 |
2.94e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 77 FGMLFQGAALFDsLSVWQNVAFRLRQRMSDDRARG---IALDKLARVGLGPETADLMP--AELSGGMAKRAGLARAIADD 151
Cdd:PTZ00265 1298 FSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRAckfAAIDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASVAR 199
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-210 |
1.05e-08 |
|
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: 55.40 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATR--VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLdRAARARFLAGFG 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 MLFQGAALFDSLSVWQNVAFRLRqrmsddrARGIALDKLARV------GLGPET-ADLMPAELSGGMAKRAGLARAIADD 151
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYAR-------LRGVPAEEIEKVanwsiqSLGLSLyADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTiTHDMASVARIGDRVALLQGG 210
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT-SHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-218 |
1.10e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAP---EAGRILWQGRPLDraarARFLAGFGMLFQGAALFDSLS 91
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSFQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNVAF--RLRQRMS-DDRARGIALDKLARVgLGPET-ADLM---PAE-LSGGMAKRAGLARAIADDPQ-IIFFDEPTT 162
Cdd:TIGR00956 853 VRESLRFsaYLRQPKSvSKSEKMEYVEEVIKL-LEMESyADAVvgvPGEgLNVEQRKRLTIGVELVAKPKlLLFLDEPTS 931
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 163 GLDPIRARAIDALIRGIVtETGATAL-TITHDMASVARIGDRVALLQ-GGRIVHDGPV 218
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLA-DHGQAILcTIHQPSAILFEEFDRLLLLQkGGQTVYFGDL 988
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-216 |
1.19e-08 |
|
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: 53.40 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 15 RVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCIlgleapeAGR---------ILWQGRPLDRAararFLAGFGMLFQGAA 85
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRktagvitgeILINGRPLDKN----FQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 86 LFDSLSVwqNVAFRLRQRMsddraRGIALDKLARVGLGPEtadlmpaelsggmakraglaraIADDPQIIFFDEPTTGLD 165
Cdd:cd03232 90 HSPNLTV--REALRFSALL-----RGLSVEQRKRLTIGVE----------------------LAAKPSILFLDEPTSGLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 166 PIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQ-GGRIVHDG 216
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKrGGKTVYFG 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-231 |
1.35e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGleapeagrilwqgrPLDRAARARFLAGFGMLFQGAALFDSLSVWQNV 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 97 AF--RLRQRMSDDRARGIALdkLARVGLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRAR 170
Cdd:TIGR00957 720 LFgkALNEKYYQQVLEACAL--LPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608348115 171 AI-DALIRGIVTETGATALTITHDMASVARIgDRVALLQGGRIVHDGPV-AGMDAAPALAAFL 231
Cdd:TIGR00957 798 HIfEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYqELLQRDGAFAEFL 859
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-209 |
1.57e-08 |
|
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: 53.57 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 23 TVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL---------DRAARARFLagfgmLFQGAALFDSLSVW 93
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikaDYEGTVRDL-----LSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 94 QNvafrlrqrmsdDRARGIALDKLArvglgpetaDLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAID 173
Cdd:cd03237 96 KT-----------EIAKPLQIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1608348115 174 ALIRGIVTETGATALTITHDMASVARIGDRVALLQG 209
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-244 |
2.37e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILwqgrpldrAARArflagFGMLFQGAALFDSlSVWQN 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------AERS-----IAYVPQQAWIMNA-TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRLRQRMSD--DRARGIALD-KLARVGLGPETA-DLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDP-IRAR 170
Cdd:PTZ00243 741 ILFFDEEDAARlaDAVRVSQLEaDLAQLGGGLETEiGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGER 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 171 AIDALIRGIVteTGATALTITHDMASVARiGDRVALLQGGRIVHDGP-------------------------------VA 219
Cdd:PTZ00243 821 VVEECFLGAL--AGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSsadfmrtslyatlaaelkenkdskegdadaeVA 897
|
250 260
....*....|....*....|....*
gi 1608348115 220 GMDAAPALAAFLGRSPAQSAGFAAP 244
Cdd:PTZ00243 898 EVDAAPGGAVDHEPPVAKQEGNAEG 922
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-210 |
4.06e-08 |
|
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: 53.38 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGrpldraaRARFLAGFGMLFQGaalfdslSVW 93
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQTSWIMPG-------TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 94 QNVAFRLrqrmSDDRARGIALDKLAR----VGLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:TIGR01271 505 DNIIFGL----SYDEYRYTSVIKACQleedIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1608348115 166 PIRARAI--DALIRGIVTEtgaTALTITHDMASVARiGDRVALLQGG 210
Cdd:TIGR01271 581 VVTEKEIfeSCLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-216 |
4.75e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGatrvldGVDLTV--GQ---GESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGR----P----LDR 67
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVegGEiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykPqyikPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 68 AARARFLagfgmLFQGAALFDSLSVWQNVAFRLRqrmsddrargiaLDKLArvglgpetaDLMPAELSGGMAKRAGLARA 147
Cdd:PRK13409 414 DGTVEDL-----LRSITDDLGSSYYKSEIIKPLQ------------LERLL---------DKNVKDLSGGELQRVAIAAC 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 148 IADDPQIIFFDEPTTGLDpIRARAIDA-LIRGIVTETGATALTITHDMASVARIGDRVallqggrIVHDG 216
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLD-VEQRLAVAkAIRRIAEEREATALVVDHDIYMIDYISDRL-------MVFEG 529
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-209 |
5.12e-08 |
|
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: 51.42 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 7 LQKTFGATRVLdgVDL-TVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGrpldraararflagfgmlfqgaa 85
Cdd:cd03222 6 CVKRYGVFFLL--VELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 86 lfdslsvwqnvafrlrqrmsddrargialdklARVGLGPETADLmpaelSGGMAKRAGLARAIADDPQIIFFDEPTTGLD 165
Cdd:cd03222 61 --------------------------------ITPVYKPQYIDL-----SGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1608348115 166 PIRARAIDALIRGIVTETGATALTITHDMASVARIGDRVALLQG 209
Cdd:cd03222 104 IEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-192 |
5.34e-08 |
|
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: 51.00 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRIlwqGRPLDRaararflagfGMLFqgaalfdslsvw 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE----------DLLF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 94 qnvafrLRQR--MSDDRARGIALDKLARVglgpetadlmpaeLSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPirarA 171
Cdd:cd03223 69 ------LPQRpyLPLGTLREQLIYPWDDV-------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----E 125
|
170 180
....*....|....*....|.
gi 1608348115 172 IDALIRGIVTETGATALTITH 192
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGH 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
5.41e-08 |
|
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: 53.02 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 4 IRGLQKTFGATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRilwqgrpldraarARFLAGF--GML 80
Cdd:TIGR03719 7 MNRVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPGIkvGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFDSLSVWQNVAFRLR-------------QRMSDDRARGIAL--------DKLARVG----------------LG 123
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGVAeikdaldrfneisAKYAEPDADFDKLaaeqaelqEIIDAADawdldsqleiamdalrCP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 124 PETADLmpAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpirARAIDALIRGIVTETGaTALTITHD 193
Cdd:TIGR03719 154 PWDADV--TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-216 |
5.46e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGML 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 81 FQGAALFdSLSVWQNVAfrLRQRMSDDRA----RGIALDKLARvGLgPETADLMPAE----LSGGMAKRAGLARAIADDP 152
Cdd:PRK10790 421 QQDPVVL-ADTFLANVT--LGRDISEEQVwqalETVQLAELAR-SL-PDGLYTPLGEqgnnLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 153 QIIFFDEPTTGLDPIRARAIDALIRGIVTETgaTALTITHDMASVARiGDRVALLQGGRIVHDG 216
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-239 |
5.50e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGfGMLF-----QGAALFDSLS 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVYisedrKRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 92 VWQNvafrlrqrMSDdrargIALDKLARVGLGPETADLMPA--------------------ELSGGMAKRAGLARAIADD 151
Cdd:PRK10762 347 VKEN--------MSL-----TALRYFSRAGGSLKHADEQQAvsdfirlfniktpsmeqaigLLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 152 PQIIFFDEPTTGLDPIRARAIDALIRGIVTEtGATALTITHDMASVARIGDRVALLQGGRIVHDGPVAGMDAAPALAAFL 231
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAAAV 492
|
....*...
gi 1608348115 232 GRSPAQSA 239
Cdd:PRK10762 493 GKLNRVNQ 500
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-216 |
7.04e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.71 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlSVW 93
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 94 QNVAFRLRQRMSDDRargiaLDKLARVGLGPETADLMP-----------AELSGGMAKRAGLARAIADDPQIIFFDEPTT 162
Cdd:PRK11176 435 NNIAYARTEQYSREQ-----IEEAARMAYAMDFINKMDngldtvigengVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 163 GLDPIRARAIDALIRGIvtETGATALTITHDMASVARiGDRVALLQGGRIVHDG 216
Cdd:PRK11176 510 ALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-217 |
7.25e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALF-------- 87
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFsgtvrfni 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 88 DSLS------VWQNVAfrlRQRMSDDRARG-IALDklARVGLGPETadlmpaeLSGGMAKRAGLARAIADDPQIIFFDEP 160
Cdd:PLN03232 1331 DPFSehndadLWEALE---RAHIKDVIDRNpFGLD--AEVSEGGEN-------FSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 161 TTGLDpIRaraIDALIRGIVTE--TGATALTITHDMASVARIgDRVALLQGGRIV-HDGP 217
Cdd:PLN03232 1399 TASVD-VR---TDSLIQRTIREefKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLeYDSP 1453
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-165 |
9.56e-08 |
|
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: 51.18 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRA------ARARFLAGFGMlfQGAALFDSl 90
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPsfeatrSRNRYSVAYAA--QKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 91 SVWQNVAF-----RLRQRMSDDRArgialdklarvGLGPETaDLMP-----------AELSGGMAKRAGLARAIADDPQI 154
Cdd:cd03290 94 TVEENITFgspfnKQRYKAVTDAC-----------SLQPDI-DLLPfgdqteigergINLSGGQRQRICVARALYQNTNI 161
|
170
....*....|.
gi 1608348115 155 IFFDEPTTGLD 165
Cdd:cd03290 162 VFLDDPFSALD 172
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-167 |
9.89e-08 |
|
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: 52.22 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 10 TFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEaGRILWQGRPLDRAARARFLAGFGMLFQGAALFDS 89
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 90 lsvwqnvAFRLR----QRMSDDRARGIAldklARVGLG------PETADLMPAE----LSGGMAKRAGLARAIADDPQII 155
Cdd:TIGR01271 1307 -------TFRKNldpyEQWSDEEIWKVA----EEVGLKsvieqfPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKIL 1375
|
170
....*....|..
gi 1608348115 156 FFDEPTTGLDPI 167
Cdd:TIGR01271 1376 LLDEPSAHLDPV 1387
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
9.90e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 1 MIEIRGLQKTFGATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPL--DRAARARFLAGFG 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 79 mlfQGAALFDSLSVWQNVAFRLRQrmsddRARGIALDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PRK13540 81 ---HRSGINPYLTLRENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1608348115 159 EPTTGLDPIRARAIDALIRGIVTETGATALTITHDMA 195
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLP 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-217 |
1.90e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 8 QKTFgatRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCIL----GLEAPEAGRILWQGRPLDRAARaRFLAGFGMLFQG 83
Cdd:TIGR00956 71 TKTF---DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKK-HYRGDVVYNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 84 AALFDSLSVWQNVAFRLRQRMSDDRARGIALDKLAR---------VGL----GPETADLMPAELSGGMAKRAGLARAIAD 150
Cdd:TIGR00956 147 DVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKhiadvymatYGLshtrNTKVGNDFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 151 DPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATAL-TITHDMASVARIGDRVALLQGGRIVHDGP 217
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
133-209 |
3.31e-07 |
|
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: 49.67 E-value: 3.31e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608348115 133 ELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpIRARAIDA-LIRGIVTETGATaLTITHDMASVARIGDRVALLQG 209
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD-IKQRLNAArLIRELAEDDNYV-LVVEHDLAVLDYLSDYIHCLYG 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-165 |
3.36e-07 |
|
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: 49.86 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 13 ATRVLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGrpldraaRARFLAGFGMLFQGaalfdslSV 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------RISFSSQFSWIMPG-------TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 93 WQNVAFRLrqrmSDDRARGIALDKLAR----VGLGPETADLMPAE----LSGGMAKRAGLARAIADDPQIIFFDEPTTGL 164
Cdd:cd03291 115 KENIIFGV----SYDEYRYKSVVKACQleedITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
.
gi 1608348115 165 D 165
Cdd:cd03291 191 D 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-193 |
2.76e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 2 IEIRGLQKTFGAtRVL-DGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILW----------QGRpldraar 70
Cdd:PRK11819 325 IEAENLSKSFGD-RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdQSR------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 71 arflagfgmlfqgAALFDSLSVWQNVA-----FRLRQRMSDDRA-------RGIalDKLARVGlgpetadlmpaELSGGM 138
Cdd:PRK11819 397 -------------DALDPNKTVWEEISggldiIKVGNREIPSRAyvgrfnfKGG--DQQKKVG-----------VLSGGE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 139 AKRAGLARAIADDPQIIFFDEPTTGLDPIRARAI-DALIrgivtETGATALTITHD 193
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALeEALL-----EFPGCAVVISHD 501
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-204 |
2.87e-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: 47.86 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 14 TRVLDGVDLTVG-----QGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQgrpLDRAARARFL-AGFGML---FQGA 84
Cdd:COG1245 348 TKSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKISYKPQYIsPDYDGTveeFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 85 ALFDSL--SVWQN-VAFRLRqrmsddrargiaLDKLArvglgpetaDLMPAELSGGMAKRAGLARAIADDPQIIFFDEPT 161
Cdd:COG1245 425 ANTDDFgsSYYKTeIIKPLG------------LEKLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1608348115 162 TGLDpIRARAIDA-LIRGIVTETGATALTITHDMASVARIGDRV 204
Cdd:COG1245 484 AHLD-VEQRLAVAkAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-216 |
5.73e-06 |
|
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: 45.39 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCILgleAPEAGRILWQGRPLDRAARARFLagfgmlfqgaalfDSLsvwqnv 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPKFSRNKLIFI-------------DQL------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 97 afrlrQRMSDdrargialdklarVGLGPETADLMPAELSGGMAKRAGLARAIADDPQ--IIFFDEPTTGLDPIRARAIDA 174
Cdd:cd03238 69 -----QFLID-------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1608348115 175 LIRGIVTEtGATALTITHDMAsVARIGDRV------ALLQGGRIVHDG 216
Cdd:cd03238 131 VIKGLIDL-GNTVILIEHNLD-VLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-217 |
6.52e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 16 VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILWQGRPLDRAARARFLAGFGMLFQGAALFDSlsvwqN 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-----T 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 96 VAFRL----------------RQRMSDD-RARGIALDklARVGLGPETadlmpaeLSGGMAKRAGLARAIADDPQIIFFD 158
Cdd:PLN03130 1329 VRFNLdpfnehndadlwesleRAHLKDViRRNSLGLD--AEVSEAGEN-------FSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 159 EPTTGLDpIRAraiDALIRGIVTE--TGATALTITHDMASVARIgDRVALLQGGRIV-HDGP 217
Cdd:PLN03130 1400 EATAAVD-VRT---DALIQKTIREefKSCTMLIIAHRLNTIIDC-DRILVLDAGRVVeFDTP 1456
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-193 |
1.10e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.27 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 17 LDGVDLTVGQGESLCVIGQSGTGKSVLLKCI---LGLEAPEAGRILWQGRPLDRAARARFLAGFgmLFQgaalfdslsvw 93
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIglaLGGAQSATRRRSGVKAGCIVAAVSAELIFT--RLQ----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 94 qnvafrlrqrmsddrargialdklarvglgpetadlmpaeLSGGMAKRAGLARAIA----DDPQIIFFDEPTTGLDPIRA 169
Cdd:cd03227 78 ----------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDG 117
|
170 180
....*....|....*....|....
gi 1608348115 170 RAIDALIRGIVTEtGATALTITHD 193
Cdd:cd03227 118 QALAEAILEHLVK-GAQVIVITHL 140
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
134-218 |
1.26e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpirARAIDALIRGI--VTETGATAL-TITHDMASVARIGDRVALLQ-G 209
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD---ARAAAIVMRTVrnTVDTGRTVVcTIHQPSIDIFEAFDELLLMKrG 1096
|
....*....
gi 1608348115 210 GRIVHDGPV 218
Cdd:PLN03140 1097 GQVIYSGPL 1105
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-193 |
1.90e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 19 GVDLTvgqgESLCVIGQSGTGKSVLLKCILGLEAPEAGRILwqgrpldRAARARfLAGF------GMLFQGAALFDSLSV 92
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVR-MAVFsqhhvdGLDLSSNPLLYMMRC 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 93 WQNVafrLRQRMsddRARgialdkLARVGLGPETAdLMPA-ELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpirARA 171
Cdd:PLN03073 599 FPGV---PEQKL---RAH------LGSFGVTGNLA-LQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDA 662
|
170 180
....*....|....*....|..
gi 1608348115 172 IDALIRGIVTETGATaLTITHD 193
Cdd:PLN03073 663 VEALIQGLVLFQGGV-LMVSHD 683
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
133-195 |
2.85e-05 |
|
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: 44.78 E-value: 2.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 133 ELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpIRAR-AIDALIRGIvTETGATALTITHDMA 195
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-IYQRlNVARLIREL-AEEGKYVLVVEHDLA 273
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
133-195 |
3.09e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 3.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608348115 133 ELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpIRARAIDA-LIRGIVteTGATALTITHDMA 195
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-IRQRLNVArLIRELA--EGKYVLVVEHDLA 272
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
114-217 |
5.35e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 114 LDKLARVGLG------PETadlmpaELSGGMAKRAGLARAI---ADDPQIIFFDEPTTGL--DPIRaRAIDALIRgiVTE 182
Cdd:cd03271 150 LQTLCDVGLGyiklgqPAT------TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfHDVK-KLLEVLQR--LVD 220
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1608348115 183 TGATALTITHDMaSVARIGDRVALL------QGGRIVHDGP 217
Cdd:cd03271 221 KGNTVVVIEHNL-DVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-193 |
5.67e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 5 RGLQKTFGATR-VLDGVDLTVGQGESLCVIGQSGTGKSVLLKCILGLEAPEAGrilwqgrpldraaRARFLAGF--GMLF 81
Cdd:PRK11819 10 NRVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAPGIkvGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 82 QGAALFDSLSVWQNV------AFRLRQR-------MSDDRArgiALDKLARvglgpETADL------------------- 129
Cdd:PRK11819 77 QEPQLDPEKTVRENVeegvaeVKAALDRfneiyaaYAEPDA---DFDALAA-----EQGELqeiidaadawdldsqleia 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608348115 130 MPA-----------ELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDpirARAIDALIRGIVTETGaTALTITHD 193
Cdd:PRK11819 149 MDAlrcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
128-217 |
2.21e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 128 DLMPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATAL-TITHDMASVARIGDRVAL 206
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLmSLLQPAPETFDLFDDIIL 410
|
90
....*....|.
gi 1608348115 207 LQGGRIVHDGP 217
Cdd:PLN03140 411 LSEGQIVYQGP 421
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-209 |
2.50e-04 |
|
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: 40.05 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 26 QGESLCVIGQSGTGKSVLLKCILGLEAPEAGRILwqgrpldraararflagfgmlfqgaalfdslsvwqnvafrlrqRMS 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------------------YID 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 106 DDRARGIALDKLARVGLGPEtadlmPAELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVT---- 181
Cdd:smart00382 38 GEDILEEVLDQLLLIIVGGK-----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllk 112
|
170 180 190
....*....|....*....|....*....|....*
gi 1608348115 182 -ETGATALTITH------DMASVARIGDRVALLQG 209
Cdd:smart00382 113 sEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-197 |
4.57e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 4.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608348115 132 AELSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAIDALIRGIVTETGATALTITHDMASV 197
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
114-216 |
7.66e-04 |
|
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: 39.55 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 114 LDKLARVGLGPETADLMPAELSGGMAKRAGLARAI-ADDPQIIF-FDEPTTGLDPiraRAIDALIRGI--VTETGATALT 189
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGLHP---RDNDRLIETLkrLRDLGNTVLV 194
|
90 100 110
....*....|....*....|....*....|...
gi 1608348115 190 ITHDMASVaRIGDRV------ALLQGGRIVHDG 216
Cdd:cd03270 195 VEHDEDTI-RAADHVidigpgAGVHGGEIVAQG 226
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
129-193 |
1.09e-03 |
|
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: 39.13 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608348115 129 LMPAELSGG------MAKRAGLARAIADDPQIIFFDEPTTGLDPIRAR-AIDALIRGIVTETGATALTITHD 193
Cdd:cd03240 111 DMRGRCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHD 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-194 |
2.23e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 114 LDKLARVGLG------PETAdlmpaeLSGGMAKRAGLARAI---ADDPQIIFFDEPTTGL--DPIRaRAIDALIRGIvtE 182
Cdd:TIGR00630 810 LQTLCDVGLGyirlgqPATT------LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfDDIK-KLLEVLQRLV--D 880
|
90
....*....|..
gi 1608348115 183 TGATALTITHDM 194
Cdd:TIGR00630 881 KGNTVVVIEHNL 892
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
114-194 |
2.60e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 114 LDKLARVGLG------PETadlmpaELSGGMAKRAGLARAIA--DDPQIIF-FDEPTTGL--DPIRA--RAIDALIrgiv 180
Cdd:COG0178 807 LQTLQDVGLGyiklgqPAT------TLSGGEAQRVKLASELSkrSTGKTLYiLDEPTTGLhfHDIRKllEVLHRLV---- 876
|
90
....*....|....
gi 1608348115 181 tETGATALTITHDM 194
Cdd:COG0178 877 -DKGNTVVVIEHNL 889
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
134-216 |
3.17e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 38.42 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLARAIADDPQIIFFDEPTTGLDPIRARAI-DALIRGIVteTGATALTITHDMASVARIgDRVALLQGGRI 212
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDEL--KGKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
....
gi 1608348115 213 VHDG 216
Cdd:PLN03232 818 KEEG 821
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-221 |
3.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 114 LDKLARVGLGPETADLMPAELSGGMAKRAGLARAIADDPQIIFF--DEPTTGLDPiraRAIDALIRGI--VTETGATALT 189
Cdd:PRK00635 457 LSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHP---QDTHKLINVIkkLRDQGNTVLL 533
|
90 100 110
....*....|....*....|....*....|....
gi 1608348115 190 ITHD--MASVArigdrvallqgGRIVHDGPVAGM 221
Cdd:PRK00635 534 VEHDeqMISLA-----------DRIIDIGPGAGI 556
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-210 |
3.75e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608348115 134 LSGGMAKRAGLAR---AIADDPQIIFFDEPTTGLdpiRARAIDALIRGI--VTETGATALTITHDMaSVARIGDRVALL- 207
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGL---HTHDIKALIYVLqsLTHQGHTVVIIEHNM-HVVKVADYVLELg 885
|
....
gi 1608348115 208 -QGG 210
Cdd:PRK00635 886 pEGG 889
|
|
| |
