|
Name |
Accession |
Description |
Interval |
E-value |
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-229 |
4.35e-89 |
|
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: 264.19 E-value: 4.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDE 159
Cdd:COG1122 81 FQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHlaDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLER 229
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-210 |
3.46e-75 |
|
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: 228.12 E-value: 3.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDE 159
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGlrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGE 210
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
1.34e-56 |
|
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: 189.73 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAP----ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDL---RTSE 73
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 74 LARRVGFLFQNPDSQICCN-TVREELLFGFKALG-LDGPDADSRVDAIVEEFAFDPDD---DPFLLNRGARQLLALASIV 148
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLadrYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 149 VLAPPVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN-RET 226
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQrELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANpQHP 499
|
....*.
gi 496664120 227 LERASL 232
Cdd:COG1123 500 YTRALL 505
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
5.00e-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: 182.80 E-value: 5.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA---GQVLIDGVPTSDLRTSELAR 76
Cdd:COG1123 4 LLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 RVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPV 154
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERrlDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 155 VVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERA 230
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-253 |
2.40e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 167.15 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSD--LRTSELARRVGFLFQNPDSQICCNTVR 95
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 96 EELLFGFKALGLDGPDADSRVDAIVEEFAFDPDD----DPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVK 171
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 172 VMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVPPQIVELSLELGREMPH 250
Cdd:PRK13637 183 ILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGLAVPQVTYLVRKLRKKGFN 262
|
...
gi 496664120 251 LAD 253
Cdd:PRK13637 263 IPD 265
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-239 |
5.66e-50 |
|
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: 165.22 E-value: 5.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQ--IccnTVREELLFG----FKALGLDGPDADSRVDAI-----VEEFAfdpdDDPFL-LNRGARQLLALAS-- 146
Cdd:COG1120 80 VPQEPPAPfgL---TVRELVALGryphLGLFGRPSAEDREAVEEAlertgLEHLA----DRPVDeLSGGERQRVLIARal 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 147 -------IvvlappvvvLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTF 218
Cdd:COG1120 153 aqeppllL---------LDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
250 260
....*....|....*....|.
gi 496664120 219 DVLrNRETLERASLVPPQIVE 239
Cdd:COG1120 224 EVL-TPELLEEVYGVEARVIE 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
5.88e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 166.02 E-value: 5.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR--V 78
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRV-DAI----VEEFAFDPdddPFLLNRGARQLLALASIVVLAPP 153
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVkEALkavgMEGFENKP---PHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 154 VVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLV 233
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLR 237
|
250
....*....|....
gi 496664120 234 PPQIVELSLELGRE 247
Cdd:PRK13639 238 LPRVAHLIEILNKE 251
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
1.79e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtSELARRVGFL 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNP--DSQIccnTVREELLFgFKAL-GLDGPDADSRVDAIVEEFAFDPD-DDPF-LLNRGARQLLALAS---------I 147
Cdd:COG1131 79 PQEPalYPDL---TVRENLRF-FARLyGLPRKEARERIDELLELFGLTDAaDRKVgTLSGGMKQRLGLALallhdpellI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 148 vvlappvvvLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDApTFDVLRNReTL 227
Cdd:COG1131 155 ---------LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG-TPDELKAR-LL 223
|
.
gi 496664120 228 E 228
Cdd:COG1131 224 E 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
1.41e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 157.91 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RR 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVE-------EFAFdpdddPFLLNRGARQLLA--- 143
Cdd:COG2884 81 IGVVFQDfrllPDR-----TVYENVALPLRVTGKSRKEIRRRVREVLDlvglsdkAKAL-----PHELSGGEQQRVAiar 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 144 ---------LAsivvlappvvvlDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:COG2884 151 alvnrpellLA------------DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
..
gi 496664120 215 AP 216
Cdd:COG2884 219 EA 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-212 |
1.11e-45 |
|
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: 152.80 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 6 DVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSdlrTSELARRVGFLFQNP 85
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 86 DSQICCNTVREELLFGFKALgldgPDADSRVDAIVEEFA-FDPDDD-PFLLNRGARQLLALASIVVLAPPVVVLDEPTTG 163
Cdd:cd03226 81 DYQLFTDSVREELLLGLKEL----DAGNEQAETVLKDLDlYALKERhPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496664120 164 LDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-244 |
1.25e-45 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 154.79 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIV-----EEFAfdpDDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:PRK13635 86 VFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALrqvgmEDFL---NREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADyAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVP 234
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGLDV 241
|
250
....*....|
gi 496664120 235 PQIVELSLEL 244
Cdd:PRK13635 242 PFSVKLKELL 251
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
1.93e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 153.99 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGS-APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:PRK13632 7 MIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPDSQICCNTVREELLFGFKALGLDgpdaDSRVDAIVEEFAFDP------DDDPFLLNRGARQLLALASIVVLAPP 153
Cdd:PRK13632 87 IIFQNPDNQFIGATVEDDIAFGLENKKVP----PKKMKDIIDDLAKKVgmedylDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 154 VVVLDEPTTGLDYRECVKVMDIIRRIHERGT-TVVMVCHDME--VVADYaarCIVMSGGEVVDDAPTFDVLRNRETLERA 230
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDeaILADK---VIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
250
....*....|....*
gi 496664120 231 SLVPPQIVELSLELG 245
Cdd:PRK13632 240 KIDSPFIYKLSKKLK 254
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-230 |
2.92e-45 |
|
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: 152.70 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlRTSELARRVGF 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQN---PDSqiccNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVV 155
Cdd:COG4555 79 LPDErglYDR----LTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVgeLSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV--DDAPTFDVLRNRETLERA 230
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVaqGSLDELREEIGEENLEDA 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-247 |
6.03e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 150.62 E-value: 6.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY-----DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLR-TSEL 74
Cdd:PRK13633 4 MIKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ARRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRGARQLLALASIVV 149
Cdd:PRK13633 84 RNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKkvgmyEYR---RHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 150 LAPPVVVLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADyAARCIVMSGGEVVDDAPTFDVLRNRETLE 228
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMK 239
|
250
....*....|....*....
gi 496664120 229 RASLVPPQIVELSLELGRE 247
Cdd:PRK13633 240 KIGLDVPQVTELAYELKKE 258
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-244 |
6.71e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 150.52 E-value: 6.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDL-RTSELARRVG 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKyrHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADyAARCIVMSGGEVVDDAPTFDVLRNrETLERASLVPPQI 237
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSD-VSLQTLGLTPPSL 238
|
....*..
gi 496664120 238 VELSLEL 244
Cdd:PRK13644 239 IELAENL 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-212 |
2.26e-42 |
|
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: 143.34 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLf 82
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 83 qnpdSQICcntvreellfgfKALGLDGPdADSRVDAiveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEPTT 162
Cdd:cd03214 79 ----PQAL------------ELLGLAHL-ADRPFNE---------------LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496664120 163 GLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03214 127 HLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-269 |
4.75e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 142.96 E-value: 4.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVP-TSDLRTSELA- 75
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 --RRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADS------RVDAIVEEFAfdpDDDPFLLNRGARQLLALASI 147
Cdd:PRK13649 83 irKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEAlareklALVGISESLF---EKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 148 VVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETL 227
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 496664120 228 ERASLVPPQIVELSLELGREMPHLADGPVgranTLDEMAAAV 269
Cdd:PRK13649 240 EEKQLGVPKITKFAQRLADRGISFSSLPI----TIEEFREVL 277
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
8.75e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.56 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA-- 75
Cdd:COG1136 4 LLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 --RRVGFLFQNPdsqiccN-----TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQ------ 140
Cdd:COG1136 84 rrRHIGFVFQFF------NllpelTALENVALPLLLAGVSRKERRERARELLERVGLGDrlDHRPSQLSGGQQQrvaiar 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 141 --------LLAlasivvlappvvvlDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEvVADYAARCIVMSGGEV 211
Cdd:COG1136 158 alvnrpklILA--------------DEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE-LAARADRVIRLRDGRI 222
|
...
gi 496664120 212 VDD 214
Cdd:COG1136 223 VSD 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-274 |
2.15e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 141.51 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG----VPTSDLRTSE 73
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 74 LARRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPD---DDPFLLNRGARQLLALASIVVL 150
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlisKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERA 230
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKH 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 496664120 231 SLVPPQIVELSLELGREMPHLADGPVgranTLDEMAAAVMEEVR 274
Cdd:PRK13641 243 YLDEPATSRFASKLEKGGFKFSEMPL----TIDELVDGIKNNLK 282
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-278 |
5.47e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.99 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV--------------LIDG 63
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 64 VPTSDL----------RTSELARRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPD---DD 130
Cdd:PRK13651 83 VLEKLViqktrfkkikKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESylqRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 131 PFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGE 210
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 211 VVDDAPTFDVLRNRETLERASLVPPQIVELSLELgremphLADG-PVGRANTLDEMAAAVMEEVRTSER 278
Cdd:PRK13651 243 IIKDGDTYDILSDNKFLIENNMEPPKLLNFVNKL------EKKGiDVPKVTSIEELASEINMYLEKKNK 305
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
9.16e-40 |
|
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: 138.02 E-value: 9.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA-- 75
Cdd:cd03257 1 LLEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 -RRVGFLFQNPDSQIccN---TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDpfLLNRGARQL---------- 141
Cdd:cd03257 81 rKEIQMVFQDPMSSL--NprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEE--VLNRYPHELsggqrqrvai 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 142 -LALAS-----IvvlappvvvLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:cd03257 157 aRALALnpkllI---------ADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
.
gi 496664120 215 A 215
Cdd:cd03257 228 G 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-252 |
9.20e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 139.91 E-value: 9.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGV----PTSDLRTSE 73
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 74 LARRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPD---DDPFLLNRGARQLLALASIVVL 150
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLER 229
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLAD 242
|
250 260
....*....|....*....|....*..
gi 496664120 230 ASLVPPQIVELSLEL----GREMPHLA 252
Cdd:PRK13646 243 WHIGLPEIVQLQYDFeqkyQTKLKDIA 269
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-269 |
3.21e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 138.61 E-value: 3.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI------DGVPTSDLRT 71
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 72 seLARRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPD---DDPFLLNRGARQLLALASIV 148
Cdd:PRK13634 83 --LRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEEllaRSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 149 VLAPPVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETL 227
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 496664120 228 ERASLVPPQIVELSLELGREM------PHLadgpvgranTLDEMAAAV 269
Cdd:PRK13634 241 EAIGLDLPETVKFKRALEEKFgisfpkPCL---------TLEELAHEV 279
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
4.28e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 138.01 E-value: 4.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLD 158
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEElrDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 159 EPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVPPQI 237
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSL 242
|
...
gi 496664120 238 VEL 240
Cdd:PRK13652 243 PKL 245
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-194 |
6.68e-39 |
|
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: 134.86 E-value: 6.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 11 YDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTS--ELARRVGFLFQNPDSQ 88
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGllERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFD--PDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDY 166
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASglRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*...
gi 496664120 167 RECVKVMDIIRRIHERGTTVVMVCHDME 194
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
8.05e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 8.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtselaRRVGF 80
Cdd:COG1121 6 AIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQ----NPDSQIccnTVREELLFGF----KALGLDGPDADSRVDAI-----VEEFAfdpdDDPF-----------LLnr 136
Cdd:COG1121 80 VPQraevDWDFPI---TVRDVVLMGRygrrGLFRRPSRADREAVDEAlervgLEDLA----DRPIgelsggqqqrvLL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 137 gAR------QLLALasivvlappvvvlDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGe 210
Cdd:COG1121 151 -ARalaqdpDLLLL-------------DEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG- 215
|
250 260
....*....|....*....|
gi 496664120 211 VVDDAPTFDVLrNRETLERA 230
Cdd:COG1121 216 LVAHGPPEEVL-TPENLSRA 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
1.45e-38 |
|
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: 132.75 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLF 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 83 QnpdsqiccntvreellfgfkalgldgpdadsrvdaiveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEPTT 162
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496664120 163 GLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGE 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-211 |
2.87e-38 |
|
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: 132.52 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTsELARRVGFL 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDsqiccntvreelLFGfkalgldgpdadsrvDAIVEEFafdpdddpFLLNRGARQLLALASIVVLAPPVVVLDEPT 161
Cdd:cd03230 79 PEEPS------------LYE---------------NLTVREN--------LKLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496664120 162 TGLD--YREcvKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:cd03230 124 SGLDpeSRR--EFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
3.15e-38 |
|
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: 133.80 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFL 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsqicCN----TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDD--PFLLNRGARQLLALASIVVLAPPVV 155
Cdd:cd03259 78 FQDY-----ALfphlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNryPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQrELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-211 |
3.35e-38 |
|
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: 133.77 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA---PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA--- 75
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 -RRVGFLFQNPdsqiccN-----TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPdddpfLLNR-------GARQLL 142
Cdd:cd03255 81 rRHIGFVFQSF------NllpdlTALENVELPLLLAGVPKKERRERAEELLERVGLGD-----RLNHypselsgGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 143 ALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEvVADYAARCIVMSGGEV 211
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
7.26e-38 |
|
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: 133.57 E-value: 7.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RR 77
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQNP---DSQiccnTVREELLFGFKAL-GLDGPDADSRVDAIVEEF----AFD--PDDdpflLNRG-------AR- 139
Cdd:COG1127 84 IGMLFQGGalfDSL----TVFENVAFPLREHtDLSEAEIRELVLEKLELVglpgAADkmPSE----LSGGmrkrvalARa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 140 -----QLLALasivvlappvvvlDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:COG1127 156 laldpEILLY-------------DEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|
gi 496664120 214 DApTFDVLRN 223
Cdd:COG1127 223 EG-TPEELLA 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-211 |
2.29e-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: 131.38 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RRV 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQnpDSQICCN-TVREELLFGFKALGLDGPDADSRVDAIVEE--FAFDPDDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:cd03292 81 GVVFQ--DFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELvgLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
2.91e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.43 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTS--ELARRV 78
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVV 156
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHlkDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 157 LDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVPP 235
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLP 244
|
....*
gi 496664120 236 QIVEL 240
Cdd:PRK13636 245 RIGHL 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
4.15e-37 |
|
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: 131.54 E-value: 4.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RRV 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPdsqiccN-----TVREELLFG-------FKALGLDGPDAD--------SRVDaiVEEFAFDPDDdpfLLNRGA 138
Cdd:cd03256 81 GMIFQQF------NlierlSVLENVLSGrlgrrstWRSLFGLFPKEEkqralaalERVG--LLDKAYQRAD---QLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 139 RQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAP- 216
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPp 229
|
250
....*....|
gi 496664120 217 ---TFDVLRN 223
Cdd:cd03256 230 aelTDEVLDE 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-245 |
8.59e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.78 E-value: 8.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDA---IVEEFAFDpDDDPFLLNRGARQLLALASIVVLAPPVVVLD 158
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEalkAVRMWDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 159 EPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTfDVLRNRETLERASLVPPQIV 238
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRLPLVA 242
|
....*..
gi 496664120 239 ELSLELG 245
Cdd:PRK13647 243 QIFEDLP 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-210 |
1.61e-36 |
|
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: 127.88 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGS-APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdsQICCNTVREELLFGfkalgldgpdadsrvdaiveefafdpdddpfllnrGARQLLALA-------SIvvlapp 153
Cdd:cd03228 81 VPQDP--FLFSGTIRENILSG-----------------------------------GQRQRIAIArallrdpPI------ 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 154 vVVLDEPTTGLDYRECVKVMDIIRRIHeRGTTVVMVCHDMEVVADyAARCIVMSGGE 210
Cdd:cd03228 118 -LILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-223 |
2.32e-36 |
|
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: 129.54 E-value: 2.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSEL---ARRV 78
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNP---DSQiccnTVREELLFGFKALG-LDGPDADSRVDAIVEEFAFDPDDD--PFLLNRGARQLLALASIVVLAP 152
Cdd:cd03261 80 GMLFQSGalfDSL----TVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDlyPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDApTFDVLRN 223
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG-TPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
3.44e-36 |
|
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: 128.85 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYD---GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSEL--- 74
Cdd:cd03258 1 MIELKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ARRVGFLFQN---PDSQiccnTVREELLFGFKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRGARQLLALAS 146
Cdd:cd03258 81 RRRIGMIFQHfnlLSSR----TVFENVALPLEIAGVPKAEIEERVLELLElvgleDKA---DAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 147 IVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
8.75e-36 |
|
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: 135.35 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG-SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpDSQICCNTVREELLFGfkalgldGPDA-DSRVDAIVEEFAFDPD--DDP-----FLLNRGA------RQLLALA- 145
Cdd:COG2274 554 VLQ--DVFLFSGTIRENITLG-------DPDAtDEEIIEAARLAGLHDFieALPmgydtVVGEGGSnlsggqRQRLAIAr 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 146 ------SIvvlappvVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHDMEVVADyAARCIVMSGGEVVDDApTFD 219
Cdd:COG2274 625 allrnpRI-------LILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDG-THE 694
|
....*.
gi 496664120 220 VLRNRE 225
Cdd:COG2274 695 ELLARK 700
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-211 |
1.38e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.70 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSA--PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRV 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVD---AIVEEFAFDpDDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNealELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVAdYAARCIVMSGGEV 211
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-244 |
1.50e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 128.76 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA---GQVLIDGVPTSDLRTSELARR 77
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:PRK13640 86 VGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDyiDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEvVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVP 234
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDI 244
|
250
....*....|
gi 496664120 235 PQIVELSLEL 244
Cdd:PRK13640 245 PFVYKLKNKL 254
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-254 |
1.94e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.81 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSEL--A 75
Cdd:COG1135 1 MIELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 RR-VGFLFQNPdsqiccN-----TVREELLFGFKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRGARQ---- 140
Cdd:COG1135 81 RRkIGMIFQHF------NllssrTVAENVALPLEIAGVPKAEIRKRVAELLElvglsDKA---DAYPSQLSGGQKQrvgi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 141 ----------LLAlasivvlappvvvlDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:COG1135 152 aralannpkvLLC--------------DEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 496664120 210 EVVDDAPTFDVLRNRETLERASLVPPQI-VELSLELGREMPHLADG 254
Cdd:COG1135 218 RIVEQGPVLDVFANPQSELTRRFLPTVLnDELPEELLARLREAAGG 263
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-223 |
2.48e-35 |
|
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: 126.78 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG-SApiLKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VG 79
Cdd:cd03219 1 LEVRGLTKRFGGlVA--LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsQICCN-TVREELL----------FGFKALGLDGPDADSRVDAIVEEFAFDPDDD--PFLLNRGARQLLALAS 146
Cdd:cd03219 79 RTFQIP--RLFPElTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADrpAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 147 IVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
2.90e-35 |
|
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: 124.99 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLR--TSELARRVG 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsqiccN-----TVREELlfgfkALGLDGPDAdSRVdAIVEEFAFDPDddpfllnrgarqLLALasivvlappv 154
Cdd:cd03229 80 MVFQDF------AlfphlTVLENI-----ALGLSGGQQ-QRV-ALARALAMDPD------------VLLL---------- 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 155 vvlDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGE 210
Cdd:cd03229 125 ---DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
3.75e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDsqiccntvreeLLFGFK-----ALGL-DGPDADSRVDAIVEEfAFDPDDDPFLLNRGARQL---------LA-- 143
Cdd:PRK13548 81 LPQHSS-----------LSFPFTveevvAMGRaPHGLSRAEDDALVAA-ALAQVDLAHLAGRDYPQLsggeqqrvqLArv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 144 LASIVVLAPPVVVL--DEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDV 220
Cdd:PRK13548 149 LAQLWEPDGPPRWLllDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
250
....*....|
gi 496664120 221 LRNrETLERA 230
Cdd:PRK13548 229 LTP-ETLRRV 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
3.79e-35 |
|
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: 132.57 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsQICCNTVREELLFGfkalgldGPDAD----------SRVDAIVEEFAFDPD----DDPFLLNRGARQLLALA-- 145
Cdd:COG4988 417 PQNP--YLFAGTIRENLRLG-------RPDASdeeleaaleaAGLDEFVAALPDGLDtplgEGGRGLSGGQAQRLALAra 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 146 -----SIvvlappvVVLDEPTTGLDYRECVKVMDIIRRIHeRGTTVVMVCHDMEVVADyAARCIVMSGGEVVdDAPTFDV 220
Cdd:COG4988 488 llrdaPL-------LLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIV-EQGTHEE 557
|
....*
gi 496664120 221 LRNRE 225
Cdd:COG4988 558 LLAKN 562
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
4.52e-35 |
|
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: 126.25 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VG 79
Cdd:COG0410 3 MLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 F------LFQNPdsqiccnTVREELLFGFKALGlDGPDADSRVDAIVEEFafdpdddPFLLNR----------GARQLLA 143
Cdd:COG0410 82 YvpegrrIFPSL-------TVEENLLLGAYARR-DRAEVRADLERVYELF-------PRLKERrrqragtlsgGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 144 LASIVVLAPPVVVLDEPTTGL--DYREcvKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVL 221
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLapLIVE--EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....*...
gi 496664120 222 RNRETLER 229
Cdd:COG0410 225 ADPEVREA 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-223 |
4.69e-35 |
|
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: 126.26 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP----DDDPFLLNRGARQLLALASIVVLAPP 153
Cdd:cd03295 81 IQQiglfPHM-----TVEENIALVPKLLKWPKEKIRERADELLALVGLDPaefaDRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 154 VVVLDEPTTGLD--YREcvKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:cd03295 156 LLLMDEPFGALDpiTRD--QLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-271 |
6.09e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.43 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 6 DVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLID--GVPTSDLRTSE---LAR 76
Cdd:PRK13645 11 NVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKIKEvkrLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 RVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFdPDD----DPFLLNRGARQLLALASIVVLAP 152
Cdd:PRK13645 91 EIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PEDyvkrSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERAS 231
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIE 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 496664120 232 LVPPQIVELSLELGREMPHLADGPVgraNTLDEMAAAVME 271
Cdd:PRK13645 250 IDPPKLYQLMYKLKNKGIDLLNKNI---RTIEEFAKELAK 286
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
6.41e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.38 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:COG4559 1 MLEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNpdSQIccN---TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPdddpfLLNRGARQL---------LA--LAS 146
Cdd:COG4559 80 LPQH--SSL--AfpfTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAH-----LAGRSYQTLsggeqqrvqLArvLAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 147 IVVLAPPVVVL---DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLrN 223
Cdd:COG4559 151 LWEPVDGGPRWlflDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL-T 229
|
....*..
gi 496664120 224 RETLERA 230
Cdd:COG4559 230 DELLERV 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-212 |
6.44e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.65 E-value: 6.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGF 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDsqiccN----TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPdddpfLLNR-------GARQLLALAsivv 149
Cdd:COG3839 80 VFQSYA-----LyphmTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED-----LLDRkpkqlsgGQRQRVALGralv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 150 lappvvvlDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHD------MevvADyaaRCIVMSGGEVV 212
Cdd:COG3839 150 repkvfllDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveamtL---AD---RIAVMNDGRIQ 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
1.46e-34 |
|
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: 125.54 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VG 79
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsQICCN-TVRE---------------ELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQL 141
Cdd:COG0411 83 RTFQNP--RLFPElTVLEnvlvaaharlgrgllAALLRLPRARREEREARERAEELLERVGLADraDEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 142 L----ALASivvlappvvvlDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAP 216
Cdd:COG0411 161 LeiarALATepkl----lllDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
250
....*....|..
gi 496664120 217 TFDVLRNRETLE 228
Cdd:COG0411 237 PAEVRADPRVIE 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-209 |
2.23e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 123.80 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtselaRRVGFLF 82
Cdd:cd03235 1 EVEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 83 Q----NPDSQIccnTVREellfgFKALGLDGP---------DADSRVDAIVE-----EFAfdpdDDPF-LLNRGARQLLA 143
Cdd:cd03235 75 QrrsiDRDFPI---SVRD-----VVLMGLYGHkglfrrlskADKAKVDEALErvglsELA----DRQIgELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 144 LASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-267 |
2.26e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.00 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPI----LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI-DGVPTSDLRTSELA 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 ---RRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPD---DDPFLLNRGARQLLALASIVV 149
Cdd:PRK13643 81 pvrKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfweKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 150 LAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLER 229
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 496664120 230 ASLVPPQIVELSLELGREMPHLADG-PVGRANTLDEMAA 267
Cdd:PRK13643 241 HELGVPKATHFADQLQKTGAVTFEKlPITRAELVTLLTS 279
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-212 |
8.77e-34 |
|
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: 122.72 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQnpDSQICCNTVREELLFGfkalgldGPDADsrvDAIVEEFAFDPDDDPF-----------------LLNRGARQLLAL 144
Cdd:cd03254 83 LQ--DTFLFSGTIMENIRLG-------RPNAT---DEEVIEAAKEAGAHDFimklpngydtvlgenggNLSQGERQLLAI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 145 ASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHErGTTVVMVCHDMEVVADyAARCIVMSGGEVV 212
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
1.14e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 122.88 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPD--SQIccnTVREELLFG-FkalgldgP-------DADSR-VDAIVEEFAFDPDDDPFL--LNRGARQ------- 140
Cdd:COG4604 80 LRQENHinSRL---TVRELVAFGrF-------PyskgrltAEDREiIDEAIAYLDLEDLADRYLdeLSGGQRQrafiamv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 141 --------LLalasivvlappvvvlDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:COG4604 150 laqdtdyvLL---------------DEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
250
....*....|....*...
gi 496664120 212 VDDAPTFDVLRnRETLER 229
Cdd:COG4604 215 VAQGTPEEIIT-PEVLSD 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-212 |
3.86e-33 |
|
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: 120.62 E-value: 3.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VGF 80
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPD--SQIccnTVREELLFGFKALGLDGPDAdsRVDAIVEEFafdpdddPFLLNR----------GARQLLALASIV 148
Cdd:cd03224 80 VPEGRRifPEL---TVEENLLLGAYARRRAKRKA--RLERVYELF-------PRLKERrkqlagtlsgGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 149 VLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-214 |
6.09e-33 |
|
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: 120.00 E-value: 6.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA-PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpDSQICCNTVREELLFGfkalgldGPDADSR--VDAI----VEEFAfdpDDDP-----------FLLNRGARQLLA 143
Cdd:cd03245 83 VPQ--DVTLFYGTLRDNITLG-------APLADDEriLRAAelagVTDFV---NKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 144 LASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHDMEVVaDYAARCIVMSGGEVVDD 214
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
8.73e-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: 117.91 E-value: 8.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSE-LARRVGF 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpdsqiccntvreellfgfkalgldgpdadsrvdaiveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:cd03216 80 VYQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496664120 161 TTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.19e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.51 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGF 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRGARQLLALAsivvla 151
Cdd:COG3842 82 VFQDyalfPHL-----TVAENVAFGLRMRGVPKAEIRARVAELLElvgleGLA---DRYPHQLSGGQQQRVALAralape 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 152 ppvvvlDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDME---VVADyaaRCIVMSGGEVVDDAPTFDVLRN 223
Cdd:COG3842 154 prvlllDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEealALAD---RIAVMNDGRIEQVGTPEEIYER 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-245 |
5.56e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 118.96 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 15 APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR--VGFLFQNPDSQICCN 92
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRqqVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFGFKALGLDGPDADSRVDAIV-----EEFAFDPDDdpfLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYR 167
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALtlvdaQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 168 ECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVPPQIVELSLELG 245
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLVKLHTQLG 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
6.23e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.44 E-value: 6.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPtsdlRTSELARRVGF 80
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP----LDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 ------LFQNpdsqiccNTVREELLFgFKAL-GLDGPDADSRVDAIVEEF-----AFDPDDDpflLNRGARQLLALAS-- 146
Cdd:COG4152 76 lpeergLYPK-------MKVGEQLVY-LARLkGLSKAEAKRRADEWLERLglgdrANKKVEE---LSKGNQQKVQLIAal 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 147 -------IvvlappvvvLDEPTTGLD--YREcvKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:COG4152 145 lhdpellI---------LDEPFSGLDpvNVE--LLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-214 |
1.84e-31 |
|
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: 116.42 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA---PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPtsdlrTSELARRV 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPdsqiccN-----TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLA 151
Cdd:cd03293 76 GYVFQQD------AllpwlTVLDNVALGLELQGVPKAEARERAEELLELVGLSGfeNAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 152 PPVVVLDEPTTGLDY--REcvKVMDIIRRI-HERGTTVVMVCHDME---VVADyaaRCIVMSG--GEVVDD 214
Cdd:cd03293 150 PDVLLLDEPFSALDAltRE--QLQEELLDIwRETGKTVLLVTHDIDeavFLAD---RVVVLSArpGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-240 |
2.92e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.73 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPtsdlrTSELARR 77
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQNPdsqiccN-----TVREELLFGFKALGLDGPDADSRVDAIVEE---------------------------FAF 125
Cdd:COG1116 82 RGVVFQEP------AllpwlTVLDNVALGLELRGVPKAERRERARELLELvglagfedayphqlsggmrqrvaiaraLAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 126 DPDddpfLLnrgarqLLalasivvlappvvvlDEPTTGLDY--REcvKVMDIIRRIH-ERGTTVVMVCHDME---VVADy 199
Cdd:COG1116 156 DPE----VL------LM---------------DEPFGALDAltRE--RLQDELLRLWqETGKTVLFVTHDVDeavFLAD- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496664120 200 aaRCIVMSG--GEVVDDaPTFDVLRNRETLERASlvpPQIVEL 240
Cdd:COG1116 208 --RVVVLSArpGRIVEE-IDVDLPRPRDRELRTS---PEFAAL 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-212 |
3.72e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.43 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQnpDSQICCNTVREELLFGfkalgldGPDAD----------SRVDAIVEEFafdPDD-DPFLLNRGA------RQLLAL 144
Cdd:COG1132 420 PQ--DTFLFSGTIRENIRYG-------RPDATdeeveeaakaAQAHEFIEAL---PDGyDTVVGERGVnlsggqRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 145 A-------SIvvlappvVVLDEPTTGLDYRECVKVMDIIRRIHeRGTTVVMVCHDMEVVADyAARCIVMSGGEVV 212
Cdd:COG1132 488 ArallkdpPI-------LILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIV 553
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-214 |
5.94e-31 |
|
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: 114.77 E-value: 5.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYD---GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlRTSELARR 77
Cdd:cd03266 1 MITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQNpDSQICCNTVREELLFgFKAL-GLDGPDADSRVDAIVEEFAFDPdddpfLLNR-------GARQLLALASIVV 149
Cdd:cd03266 80 LGFVSDS-TGLYDRLTARENLEY-FAGLyGLKGDELTARLEELADRLGMEE-----LLDRrvggfstGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 150 LAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-217 |
1.00e-30 |
|
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: 114.59 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLK-----PDAGQVLIDG--VPTSDLRTSEL 74
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ARRVGFLFQNPdsqiccN----TVREELLFGFKALGLDGpdaDSRVDAIVEEF--------AFDPDDDPFLLNRGARQLL 142
Cdd:cd03260 80 RRRVGMVFQKP------NpfpgSIYDNVAYGLRLHGIKL---KEELDERVEEAlrkaalwdEVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 143 ALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERgTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT 217
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-277 |
1.43e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.49 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSD----------------LRTSELARRVGF 80
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpyskkiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP---DDDPFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsylERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVPPQI 237
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSIQVPRV 280
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 496664120 238 VELSLELGREMPHLADGPVGRANTLDEMAAAVMEEVRTSE 277
Cdd:PRK13631 281 IQVINDLIKKDPKYKKLYQKQPRTIEQLADAINEFIKGGK 320
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-222 |
1.67e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.41 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsdlRTS---ELArrVGFlfqNPDSqiccnT 93
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSallELG--AGF---HPEL-----T 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 94 VREELLFGFKALGLDGPDADSRVDAIVE-----EF----------------------AFDPD----DDpfllnrgarqll 142
Cdd:COG1134 105 GRENIYLNGRLLGLSRKEIDEKFDEIVEfaelgDFidqpvktyssgmrarlafavatAVDPDillvDE------------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 143 ALAsivvlappvvvldeptTG-LDYREcvKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVL 221
Cdd:COG1134 173 VLA----------------VGdAAFQK--KCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
.
gi 496664120 222 R 222
Cdd:COG1134 235 A 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
4.84e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.08 E-value: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPI-LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAF--DPDDDPFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK13648 87 IVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMleRADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDME--VVADYAarcIVMSGGEVVDDAPTFDVLRNRETLERASLVP 234
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSeaMEADHV---IVMNKGTVYKEGTPTEIFDHAEELTRIGLDL 243
|
250
....*....|.
gi 496664120 235 PQIVELSLELG 245
Cdd:PRK13648 244 PFPIKINQMLG 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
6.99e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.09 E-value: 6.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK09536 3 MIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpDSQICCN-TVREELLFG----FKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRGARQLLALASIVVL 150
Cdd:PRK09536 82 VPQ--DTSLSFEfDVRQVVEMGrtphRSRFDTWTETDRAAVERAMErtgvaQFA---DRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLrNRETLERA 230
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL-TADTLRAA 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-211 |
1.08e-29 |
|
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: 110.38 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG-SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpdsqiccntvrEELLFgfkalgldgpdADSRVDAIveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:cd03246 81 LPQ------------DDELF-----------SGSIAENI--------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496664120 161 TTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADyAARCIVMSGGEV 211
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
1.32e-29 |
|
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: 113.99 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKP---DAGQVLIDGVPTSDLRTSEL 74
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ----ARRVGFLFQNPDSqiCCN---TVREELLFGFKA-LGLDGPDADSRVDAIVEEFAFDPDDDpfLLNR-------GAR 139
Cdd:COG0444 81 rkirGREIQMIFQDPMT--SLNpvmTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPER--RLDRyphelsgGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 140 Q----LLALAS-----IvvlappvvvLDEPTTGLDyrecV----KVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIV 205
Cdd:COG0444 157 QrvmiARALALepkllI---------ADEPTTALD----VtiqaQILNLLKDLQrELGLAILFITHDLGVVAEIADRVAV 223
|
250
....*....|....*...
gi 496664120 206 MSGGEVVDDAPTFDVLRN 223
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-192 |
4.45e-29 |
|
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: 109.49 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtSELARRVGF 80
Cdd:COG4133 2 MLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNP---DSQiccnTVREELLFGFKALGLDGPDADsrVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:COG4133 80 LGHADglkPEL----TVRENLRFWAALYGLRADREA--IDEALEAVGLAGlaDLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHD 192
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-211 |
1.18e-28 |
|
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: 108.77 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG--VPTSDLRTSELARRVG 79
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQN----PDSqiccnTVREELLFG-FKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAP 152
Cdd:cd03262 80 MVFQQfnlfPHL-----TVLENITLApIKVKGMSKAEAEERALELLEKVGLADkaDAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 153 PVVVLDEPTTGLDyRECVK-VMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:cd03262 155 KVMLFDEPTSALD-PELVGeVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-212 |
1.45e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 108.52 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlrtsELARRVGFL 81
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVV 155
Cdd:cd03269 76 PEErglyPKM-----KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVeeLSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-235 |
1.56e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQNPDSQICCNTVREE 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 98 LLFGFKALGLDGPDADSRVD-AIVEEFAFD-PDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDI 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDeALLAVNMLDfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 176 IRRIHER-GTTVVMVCHDMEVVADyAARCIVMSGGEVVDDAPTFDVLRNRETLERASLVPP 235
Cdd:PRK13642 183 IHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVP 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-212 |
2.50e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.95 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQ--IccnTVREELLFG----FKALGLDGPDADSRVD-AI----VEEFAFDPDDDpflLNRGARQLLALASIVV 149
Cdd:PRK11231 81 LPQHHLTPegI---TVRELVAYGrspwLSLWGRLSAEDNARVNqAMeqtrINHLADRRLTD---LSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 150 LAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
2.77e-28 |
|
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: 108.29 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSA---PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELAR- 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 ---RVGFLFQNpdsqiccntvrEELLFGFKALG-------LDG-PDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLA 143
Cdd:COG4181 88 rarHVGFVFQS-----------FQLLPTLTALEnvmlpleLAGrRDARARARALLERVGLGHrlDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 144 LASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVvadyAARC---IVMSGGEVVDDAPT 217
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPAL----AARCdrvLRLRAGRLVEDTAA 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
2.79e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYD-GSA---PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELAR 76
Cdd:COG1101 1 MLELKNLSKTFNpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 RVGFLFQNPDSQICCN-TVREELL--------FGFKaLGLDGPDADS--------------RVDAIVEefafdpdddpfL 133
Cdd:COG1101 81 YIGRVFQDPMMGTAPSmTIEENLAlayrrgkrRGLR-RGLTKKRRELfrellatlglglenRLDTKVG-----------L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 134 LNRGARQLLAL--ASIvvLAPPVVVLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGE 210
Cdd:COG1101 149 LSGGQRQALSLlmATL--TKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
....
gi 496664120 211 VVDD 214
Cdd:COG1101 227 IILD 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
6.31e-28 |
|
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: 106.53 E-value: 6.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVptSDLRTSELARRVGFL 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FqnpDSQICCN--TVREELLFGFKALGLDgpdaDSRVDAIVEEFAFDPDDD----PFLLnrGARQLLALASIVVLAPPVV 155
Cdd:cd03268 78 I---EAPGFYPnlTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKkkvkGFSL--GMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCH---DMEVVADyaaRCIVMSGGEVVDDA 215
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHllsEIQKVAD---RIGIINKGKLIEEG 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-212 |
7.01e-28 |
|
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: 107.32 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFL 81
Cdd:cd03300 1 IELENVSKFYGGF-VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIV-----EEFAfdpDDDPFLLNRGARQLLALASIVVLAP 152
Cdd:cd03300 78 FQNyalfPHL-----TVFENIAFGLRLKKLPKAEIKERVAEALdlvqlEGYA---NRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 153 PVVVLDEPTTGLDYReCVKVMDI-IRRIHER-GTTVVMVCHDME---VVADyaaRCIVMSGGEVV 212
Cdd:cd03300 150 KVLLLDEPLGALDLK-LRKDMQLeLKRLQKElGITFVFVTHDQEealTMSD---RIAVMNKGKIQ 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-274 |
7.13e-28 |
|
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: 109.02 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVP-TSDLRtsELARRVGFLFQ--NPDSQI 89
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvVREPR--KVRRSIGIVPQyaSVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 90 ccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAF-DPDDDPF-LLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYR 167
Cdd:TIGR01188 82 ---TGRENLEMMGRLYGLPKDEAEERAEELLELFELgEAADRPVgTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 168 ECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV-DDAP---------TFDVLRNRETLERASLVPPQI 237
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIaEGTPeelkrrlgkDTLESRPRDIQSLKVEVSMLI 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 496664120 238 VEL-SLELGREMPHLADGPVG-RANTLDEMAAAVMEEVR 274
Cdd:TIGR01188 239 AELgETGLGLLAVTVDSDRIKiLVPDGDETVPEIVEAAI 277
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-233 |
7.98e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.47 E-value: 7.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG-VPTSDLRTSElaRRVGF 80
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLPPRE--RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPdddpfLLNR-------GARQLLALASIVV 149
Cdd:COG1118 80 VFQHyalfPHM-----TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG-----LADRypsqlsgGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 150 LAPPVVVLDEPTTGLDyrecVKV----MDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNR 224
Cdd:COG1118 150 VEPEVLLLDEPFGALD----AKVrkelRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
....*....
gi 496664120 225 ETLERASLV 233
Cdd:COG1118 226 ATPFVARFL 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
8.15e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.02 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHAsydgsapiLKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG-VPTsdLRTSELARRVGFL 81
Cdd:COG4586 31 EYREVEA--------VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPF--KRRKEFARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 F-QnpdsqiccntvREELLF------GFKAL----GLDGPDADSRVDAIVEEFAFDPdddpfLLNRGARQL--------- 141
Cdd:COG4586 101 FgQ-----------RSQLWWdlpaidSFRLLkaiyRIPDAEYKKRLDELVELLDLGE-----LLDTPVRQLslgqrmrce 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 142 LALA-----SIvvlappvVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDA 215
Cdd:COG4586 165 LAAAllhrpKI-------LFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
....*....
gi 496664120 216 PtFDVLRNR 224
Cdd:COG4586 238 S-LEELKER 245
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-212 |
1.05e-27 |
|
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: 111.78 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA-PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:COG4987 334 LELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDsqICCNTVREELLFGfkalgldGPDADSrvDAIVE--------EFAFDPDD--DPFLLNRGA------RQLLAL 144
Cdd:COG4987 414 VPQRPH--LFDTTLRENLRLA-------RPDATD--EELWAalervglgDWLAALPDglDTWLGEGGRrlsggeRRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 145 ASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRiHERGTTVVMVCHDMEVVaDYAARCIVMSGGEVV 212
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGL-ERMDRILVLEDGRIV 548
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-230 |
2.48e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.85 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTS--ELARRV 78
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPdsqiccN-----TVREELLFG-FKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRG-------ARq 140
Cdd:COG1126 80 GMVFQQF------NlfphlTVLENVTLApIKVKKMSKAEAEERAMELLErvglaDKA---DAYPAQLSGGqqqrvaiAR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 141 llALAsivvlappvvvlDEPTTGLDyRECVK-VMDIIRRIHERGTTVVMVCHDMEV---VADyaaRCIVMSGGEVVDDAP 216
Cdd:COG1126 150 --ALAmepk----vmlfDEPTSALD-PELVGeVLDVMRDLAKEGMTMVVVTHEMGFareVAD---RVVFMDGGRIVEEGP 219
|
250
....*....|....
gi 496664120 217 TFDVLRNRETlERA 230
Cdd:COG1126 220 PEEFFENPQH-ERT 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-145 |
3.28e-27 |
|
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: 103.11 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQNP--DSQIccnTVR 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPqlFPRL---TVR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 96 EELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFLLNR------GARQLLALA 145
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtlsgGQRQRVAIA 133
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-212 |
6.17e-27 |
|
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: 104.26 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFL 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:cd03301 78 FQNyalyPHM-----TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHllDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
2.62e-26 |
|
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: 107.37 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsQICCNTVREELLFGFKalglDGPDADSR-----------VDAIVEEFAFDPDDDPFLLNRGARQLLALASIVVL 150
Cdd:TIGR02857 402 PQHP--FLFAGTIAENIRLARP----DASDAEIRealeragldefVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHDMEVVADyAARCIVM 206
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-212 |
2.72e-26 |
|
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: 102.27 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFvAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtSELARRVGFL 81
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQ--NPDSQIccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:cd03264 78 PQefGVYPNF---TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDraKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHErGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-214 |
3.99e-26 |
|
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: 102.80 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 14 SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG-VPTSdlRTSELARRVGFLFQNPDSQICCN 92
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWK--RRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPdddpfLLNRGARQL-------LALASIVVLAPPVVVLDEPTTGLD 165
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEE-----LLDTPVRQLslgqrmrAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496664120 166 YRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:cd03267 186 VVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-212 |
4.15e-26 |
|
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: 102.69 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQnpDSQICCNTVREELLFGfkalGLDGPDAD-------SRVDAIVEEFAFDPD----DDPFLLNRGARQLLALASIVVL 150
Cdd:cd03253 81 PQ--DTVLFNDTIGYNIRYG----RPDATDEEvieaakaAQIHDKIMRFPDGYDtivgERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHDMEVVADyAARCIVMSGGEVV 212
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-213 |
1.18e-25 |
|
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: 101.26 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFLFQN----PDSqiccnT 93
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNyalfPHM-----T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 94 VREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVK 171
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496664120 172 VMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:cd03299 168 LREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-248 |
1.38e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSdLRTSELARR--V 78
Cdd:COG1129 4 LLEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQNPDsqICCN-TVREELLFGF---KALGLDGPDADSRVDAIVEEF--AFDPDDDPFLLNRGARQLL----ALAS-- 146
Cdd:COG1129 82 AIIHQELN--LVPNlSVAENIFLGReprRGGLIDWRAMRRRARELLARLglDIDPDTPVGDLSVAQQQLVeiarALSRda 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 147 ---IvvlappvvvLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDdaptfdvlrn 223
Cdd:COG1129 160 rvlI---------LDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG---------- 220
|
250 260
....*....|....*....|....*
gi 496664120 224 reTLERASLVPPQIVELSleLGREM 248
Cdd:COG1129 221 --TGPVAELTEDELVRLM--VGREL 241
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-230 |
1.45e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG--SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsQICCNTVREELLFGFKalglDGPDAD-------SRVDAIVEEFAFDPDDDPF----LLNRGARQLLALASIV 148
Cdd:TIGR00958 559 LVGQEP--VLFSGSVRENIAYGLT----DTPDEEimaaakaANAHDFIMEFPNGYDTEVGekgsQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 149 VLAPPVVVLDEPTTGLDyRECVKVMDIIRRIHERgtTVVMVCHDMEVVADyAARCIVMSGGEVVDDApTFDVLRNRETLE 228
Cdd:TIGR00958 633 VRKPRVLILDEATSALD-AECEQLLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMG-THKQLMEDQGCY 707
|
..
gi 496664120 229 RA 230
Cdd:TIGR00958 708 KH 709
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-220 |
1.79e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.96 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPI---LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSEL--A 75
Cdd:PRK11153 1 MIELKNISKVFPQGGRTihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 RR-VGFLFQ--NPDSQiccNTVREELLFGFKALGLDGPDADSRVDAIVE-----EFAfdpDDDPFLLNRGARQLLALASI 147
Cdd:PRK11153 81 RRqIGMIFQhfNLLSS---RTVFDNVALPLELAGTPKAEIKARVTELLElvglsDKA---DRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 148 VVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDV 220
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-192 |
2.06e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 105.14 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsQICCNTVREELLFGFKalglDGPDADSR-----------VDAIVEEFAFDPDDDPFLLNRGARQLLALASIVVL 150
Cdd:TIGR02868 415 AQDA--HLFDTTVRENLRLARP----DATDEELWaalervgladwLRALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHD 192
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
6.68e-25 |
|
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: 99.34 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFL 81
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdSQICCNTVREELLFGFKAL-GLDGPDAD---SRVDAIVEEFAFD--PDDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:cd03296 80 FQHY-ALFRHMTVFDNVAFGLRVKpRSERPPEAeirAKVHELLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-217 |
9.74e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 9.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTsDLRTSELARR--VGFLFQNP---DSQiccn 92
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAIAlgIGMVHQHFmlvPNL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFGF---KALGLDGPDADSRVDAIVEEFAF--DPD----DDPF----------LLNRGARqLLALasivvlapp 153
Cdd:COG3845 96 TVAENIVLGLeptKGGRLDRKAARARIRELSERYGLdvDPDakveDLSVgeqqrveilkALYRGAR-ILIL--------- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 154 vvvlDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT 217
Cdd:COG3845 166 ----DEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-214 |
3.30e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLrtsELArrVGFlfqNPDSqiccnTVRE 96
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---GLG--GGF---NPEL-----TGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 97 ELLFGFKALGLDGPDADSRVDAIVeEFAFDPD--DDPFL-LNRGARQLLALASIVVLAPPVVVLDEPTTGLD--YREcvK 171
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEII-EFSELGDfiDLPVKtYSSGMKARLAFAIATALEPDILLIDEVLAVGDaaFQE--K 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496664120 172 VMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-212 |
4.03e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlrTSELARRVGF 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIV-----EEFAfdpDDDPFLLNRGARQLLALASIVVLA 151
Cdd:PRK11607 96 MFQSyalfPHM-----TVEQNIAFGLKQDKLPKAEIASRVNEMLglvhmQEFA---KRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 152 PPVVVLDEPTTGLDY----RECVKVMDIIRRIherGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:PRK11607 168 PKLLLLDEPMGALDKklrdRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-213 |
4.12e-24 |
|
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: 97.23 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG--SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsQICCNTVREELLFgfkalGLDGPDADSRVDAIVEEFAFD-----PD-------DDPFLLNRGARQLLALASI 147
Cdd:cd03249 81 LVSQEP--VLFDGTIAENIRY-----GKPDATDEEVEEAAKKANIHDfimslPDgydtlvgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 148 VVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHeRGTTVVMVCHDMEVVADyAARCIVMSGGEVVD 213
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-223 |
5.37e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGV----PTSDLRtsELAR 76
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvndPKVDER--LIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 RVGFLFQ--NPDSQIccnTVREELLFG-FKALGLDGPDADSRVDAIVEE--FAFDPDDDPFLLNRGARQLLALASIVVLA 151
Cdd:PRK09493 78 EAGMVFQqfYLFPHL---TALENVMFGpLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 152 PPVVVLDEPTTGLD---YRECVKVMdiiRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:PRK09493 155 PKLMLFDEPTSALDpelRHEVLKVM---QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-222 |
1.92e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 96.29 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 8 HASYDGSAP---ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RRVGFL 81
Cdd:PRK10419 15 HGGLSGKHQhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQ------NPDSQIcCNTVREELLfgfKALGLDGPDADSRVDAIVEEFAFDP---DDDPFLLNRGARQLLALASIVVLAP 152
Cdd:PRK10419 95 FQdsisavNPRKTV-REIIREPLR---HLLSLDKAERLARASEMLRAVDLDDsvlDKRPPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLR 222
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-212 |
1.95e-23 |
|
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: 95.05 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 21 VSFTIrDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLR----TSELARRVGFLFQN----PDSqiccn 92
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinLPPQQRKIGLVFQQyalfPHL----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFGFKALGlDGPDADsRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECV 170
Cdd:cd03297 91 NVRENLAFGLKRKR-NREDRI-SVDELLDLLGLDHllNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496664120 171 KVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
2.43e-23 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 94.87 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTtmrLMNGLLK---PDAGQVLIDGVPTSDLRTSELARR 77
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSS---LLLALFRlveLSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQNPdsQICCNTVREEL-LFG-------FKALgldgpdADSRVDAIVEEFA----FDPDDDPFLLNRGARQLLALA 145
Cdd:cd03244 80 ISIIPQDP--VLFSGTIRSNLdPFGeysdeelWQAL------ERVGLKEFVESLPggldTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 146 SIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRiHERGTTVVMVCHDMEVVADYaARCIVMSGGEVVD-DAP 216
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEfDSP 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-212 |
6.55e-23 |
|
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: 93.59 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPIlKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlRTSELARRVGFL 81
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNP--DSQIccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFLLNR--GARQLLALASIVVLAPPVVVL 157
Cdd:cd03265 79 FQDLsvDDEL---TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYsgGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-212 |
8.81e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 92.61 E-value: 8.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDV-----HASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKP--DAGQVLIDGVPTSDlrtSEL 74
Cdd:cd03213 4 LSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ARRVGFLFQNpDSQICCNTVREELLFGFKALGLDGPDAdSRVdAIVEEFAFDPdddpfllnrgarQLLALasivvlappv 154
Cdd:cd03213 81 RKIIGYVPQD-DILHPTLTVRETLMFAAKLRGLSGGER-KRV-SIALELVSNP------------SLLFL---------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 155 vvlDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCH----DMEVVADyaaRCIVMSGGEVV 212
Cdd:cd03213 136 ---DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpssEIFELFD---KLLLLSQGRVI 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-239 |
1.06e-22 |
|
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: 93.61 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI------DGVPTSDLRtsel 74
Cdd:COG1119 3 LLELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWELR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 aRRVGF----LFQNPDSQIccnTVREELLFGFKA-LGL-DGPDAD--SRVDAIVEEFAFDPD-DDPFL-LNRG------- 137
Cdd:COG1119 78 -KRIGLvspaLQLRFPRDE---TVLDVVLSGFFDsIGLyREPTDEqrERARELLELLGLAHLaDRPFGtLSQGeqrrvli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 138 AR------QLLALasivvlappvvvlDEPTTGLDYRECVKVMDIIRRIHERG-TTVVMVCHDMEVVADYAARCIVMSGGE 210
Cdd:COG1119 154 ARalvkdpELLIL-------------DEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
250 260
....*....|....*....|....*....
gi 496664120 211 VVDDAPTFDVLRNrETLERASLVPPQIVE 239
Cdd:COG1119 221 VVAAGPKEEVLTS-ENLSEAFGLPVEVER 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-212 |
1.06e-22 |
|
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: 92.95 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvpTSDLRTSELARR-VG 79
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQsLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNpDSQICCNTVREELLF--GFKalGLDGPDADSRVDAIVEEFAFDPDddpflLNRGARQL-------LALASIVVL 150
Cdd:cd03263 79 YCPQF-DALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDK-----ANKRARTLsggmkrkLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
1.27e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.02 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSE---LARR 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQnpDSQICCN-TVREELLFGFKALGLDGPDADSRVDAIVEEFAF--DPDDDPFLLNRGARQLLALASIVVLAPPV 154
Cdd:PRK10908 81 IGMIFQ--DHHLLMDrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLldKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 155 VVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
1.95e-22 |
|
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: 92.93 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAP-ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpDSQICCNTVREELlfgfkALGLDGPDADSrvdaiVEEFAFDPDDDPFL-----------------LNRGARQLLA 143
Cdd:cd03252 81 VLQ--ENVLFNRSIRDNI-----ALADPGMSMER-----VIEAAKLAGAHDFIselpegydtivgeqgagLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 144 LASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHErGTTVVMVCHDMEVVADyAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
.
gi 496664120 224 R 224
Cdd:cd03252 227 N 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-256 |
1.97e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQN-PDSQicCNTVR 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAE--GMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 96 EELLFG----FKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVVVLDEPTTGLDYREC 169
Cdd:PRK10575 104 ELVAIGrypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 170 VKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNrETLERASLVPPQIvelslelgreM 248
Cdd:PRK10575 184 VDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG-ETLEQIYGIPMGI----------L 252
|
....*....
gi 496664120 249 PHLADG-PV 256
Cdd:PRK10575 253 PHPAGAaPV 261
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-218 |
2.29e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG------VPTSDLRTSELA 75
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 RRVGFLFQN----PDSqiccnTVREELLFG-FKALGLDGPDADSRVDAIV-----EEFAfdpDDDPFLLNRGARQLLALA 145
Cdd:PRK11124 82 RNVGMVFQQynlwPHL-----TVQQNLIEApCRVLGLSKDQALARAEKLLerlrlKPYA---DRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 146 SIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVD--DAPTF 218
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEqgDASCF 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
2.74e-22 |
|
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: 90.84 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA-PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtSELARRVGF 80
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdsqiccntvreeLLFgfkalgldgpdADSRVDAIVEEFAfdpdddpfllnRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:cd03247 80 LNQRP------------YLF-----------DTTLRNNLGRRFS-----------GGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496664120 161 TTGLDYRECVKVMDIIRRiHERGTTVVMVCHDMEVVAdYAARCIVMSGGEVV 212
Cdd:cd03247 126 TVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIE-HMDKILFLENGKII 175
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-211 |
4.64e-22 |
|
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: 91.76 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG--SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsQICCNTVREELLFGFKALGLD-------GPDADSRVDAIVEEFAFDPDDDPFLLNRGARQLLALASIVVLAP 152
Cdd:cd03248 92 LVGQEP--VLFARSLQDNIAYGLQSCSFEcvkeaaqKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRIHERgTTVVMVCHDMEVVaDYAARCIVMSGGEV 211
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-217 |
4.72e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA-- 75
Cdd:PRK10535 4 LLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 76 RR--VGFLFQnpdsqiccntvREELLFGFKAL----------GLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQL 141
Cdd:PRK10535 84 RRehFGFIFQ-----------RYHLLSHLTAAqnvevpavyaGLERKQRLLRAQELLQRLGLEDrvEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 142 LALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADyAARCIVMSGGEVVDDAPT 217
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
6.38e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLrTSELARRVG- 79
Cdd:PRK15439 11 LLCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 -------FLFQNpdsqiccNTVREELLFGFKAlgldGPDADSRVDAIVEEFA--FDPDDDPFLLNRGARQLLALASIVVL 150
Cdd:PRK15439 89 ylvpqepLLFPN-------LSVKENILFGLPK----RQASMQKMKQLLAALGcqLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT 217
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
7.88e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.64 E-value: 7.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQnpDSQICCNTVREELLFGfKAlglDGPDADSRvDAIVEEFAFDpdddpFLLNR-----------------GARQLLAL 144
Cdd:PRK13657 415 FQ--DAGLFNRSIEDNIRVG-RP---DATDEEMR-AAAERAQAHD-----FIERKpdgydtvvgergrqlsgGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 145 ASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVmVCHDMEVVADyAARCIVMSGGEVVdDAPTFDVLRNR 224
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVV-ESGSFDELVAR 559
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-223 |
9.97e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPD----AGQVLIDGVPT--SDLRtselARRVGFLFQNPDSQI 89
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVapCALR----GRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 90 C-CNTVREELLFGFKALGLDGPDAdsRVDAIVEEFAFDPDDD-----PFLLNRGARQLLALASIVVLAPPVVVLDEPTTG 163
Cdd:PRK10418 93 NpLHTMHTHARETCLALGKPADDA--TLTAALEAVGLENAARvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 164 LDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:PRK10418 171 LDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-211 |
8.30e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 8.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 4 FRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFLFQ 83
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 84 N----PDSqiccnTVREELLFGFKALGLDGPDADSRVDAIVE--EFAFDPDDDPFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK11000 83 SyalyPHL-----SVAENMSFGLKLAGAKKEEINQRVNQVAEvlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
1.11e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlrTSELAR-RVGF 80
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARaRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 L--FQNPDSQIccnTVREELLFGFKALGLDGPDADSRVDAIVeEFA---FDPDDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:PRK13536 119 VpqFDNLDLEF---TVRENLLVFGRYFGMSTREIEAVIPSLL-EFArleSKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAAR-CIVMSGGEVVDDAP 216
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRlCVLEAGRKIAEGRP 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-222 |
1.12e-20 |
|
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: 91.40 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY----DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI----DGVPTSDLRTS 72
Cdd:TIGR03269 279 IIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 73 ELARR---VGFLFQN----PDSQICCNTVreellfgfKALGLDGPDADSRVDAIV--EEFAFDPDDDPFLLNR------- 136
Cdd:TIGR03269 359 GRGRAkryIGILHQEydlyPHRTVLDNLT--------EAIGLELPDELARMKAVItlKMVGFDEEKAEEILDKypdelse 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 137 GARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMD-IIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDA 215
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*..
gi 496664120 216 PTFDVLR 222
Cdd:TIGR03269 511 DPEEIVE 517
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
2.28e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlRTSELARRVGFL 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 --FQNPDSQIccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK13537 86 pqFDNLDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAAR-CIVMSGGEVVDDAP 216
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRlCVIEEGRKIAEGAP 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-211 |
5.18e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 88.36 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGF 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQN----PDSqiccnTVREELLFGFKALGLDGPDADSRVDA---IVEEfafdpddDPFL------LNRGARQLLALASI 147
Cdd:PRK11650 81 VFQNyalyPHM-----SVRENMAYGLKIRGMPKAEIEERVAEaarILEL-------EPLLdrkpreLSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 148 VVLAPPVVVLDEPTTGLDYRECVKvMDI-IRRIHER-GTTVVMVCHD-ME--VVADyaaRCIVMSGGEV 211
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRlKTTSLYVTHDqVEamTLAD---RVVVMNGGVA 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-216 |
5.56e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.47 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLrtSELARRVGFL 81
Cdd:PRK09452 15 VELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQN----PDSqiccnTVREELLFGFKALGLDGPDADSRV-DAI----VEEFAfdpDDDPFLLNRGARQLLALASIVVLAP 152
Cdd:PRK09452 92 FQSyalfPHM-----TVFENVAFGLRMQKTPAAEITPRVmEALrmvqLEEFA---QRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 153 PVVVLDEPTTGLDYReCVKVMDI-IRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAP 216
Cdd:PRK09452 164 KVLLLDESLSALDYK-LRKQMQNeLKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-212 |
1.18e-19 |
|
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: 85.36 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA-PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03251 1 VEFKNVTFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQnpDSQICCNTVREELLFGfkalgldGPDADsrvDAIVEEFAFDPDDDPFL-----------------LNRGARQLLA 143
Cdd:cd03251 81 VSQ--DVFLFNDTVAENIAYG-------RPGAT---REEVEEAARAANAHEFImelpegydtvigergvkLSGGQRQRIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 144 LASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVmVCHDMEVVADyAARCIVMSGGEVV 212
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
3.45e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV-----LIDG-VPTSDLRT--S 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 73 ELARRVGFLFQN----PDsqiccNTVREELLFG-FKALGLDGPDADSRVDAIVEEFAFDPDDD--PFLLNRGARQLLALA 145
Cdd:PRK11264 82 QLRQHVGFVFQNfnlfPH-----RTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETsyPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 146 SIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVL---- 221
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFadpq 236
|
250
....*....|
gi 496664120 222 --RNRETLER 229
Cdd:PRK11264 237 qpRTRQFLEK 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-216 |
3.78e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQNPDS--QIc 90
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgDI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 91 cnTVREELLFG----------FKALGLDGPDADSRVDAIVEEFAFDPDDdpflLNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:PRK10253 97 --TVQELVARGryphqplftrWRKEDEEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 161 TTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVV-DDAP 216
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVaQGAP 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-212 |
5.03e-19 |
|
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: 86.41 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQnpDSQICCNTVREELLFGfkalgldGPDADsrvDAIVEEFAFDPDDDPFLLN-----------RG------------- 137
Cdd:COG5265 438 PQ--DTVLFNDTIAYNIAYG-------RPDAS---EEEVEAAARAAQIHDFIESlpdgydtrvgeRGlklsggekqrvai 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 138 ARQLLALASIvvlappvVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCHDMEVVADyAARCIVMSGGEVV 212
Cdd:COG5265 506 ARTLLKNPPI-------LIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-212 |
5.31e-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: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMR-LM-NGLLKPDAGQVLIDGVPTSDLRTSELARR-VG 79
Cdd:COG0396 2 EIKNLHVSVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMgHPKYEVTSGSILLDGEDILELSPDERARAgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPDS----------QICCNTVREELLfgfkalglDGPDADSRVDAIVEEFAFDPDddpfLLNRGA----------R 139
Cdd:COG0396 81 LAFQYPVEipgvsvsnflRTALNARRGEEL--------SAREFLKLLKEKMKELGLDED----FLDRYVnegfsggekkR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 140 ----QLLALA---SIVvlappvvvlDEPTTGLDyrecV----KVMDIIRRIHERGTTVVMVCH-----DmEVVADYAarc 203
Cdd:COG0396 149 neilQMLLLEpklAIL---------DETDSGLD----IdalrIVAEGVNKLRSPDRGILIITHyqrilD-YIKPDFV--- 211
|
....*....
gi 496664120 204 IVMSGGEVV 212
Cdd:COG0396 212 HVLVDGRIV 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-240 |
5.48e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLkPDAGQVLIDGVPTSDLRTSELARRVGFLFQN--PDSQIccntvr 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqsPPFAM------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 96 eeLLFGFKALGLDGPDADSRVDAIVEEFA--FDPDDdpfLLNRGARQL-------LALASI-------VVLAPPVVVLDE 159
Cdd:COG4138 85 --PVFQYLALHQPAGASSEAVEQLLAQLAeaLGLED---KLSRPLTQLsggewqrVRLAAVllqvwptINPEGQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNrETLERASLVPPQIVE 239
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP-ENLSEVFGVKFRRLE 238
|
.
gi 496664120 240 L 240
Cdd:COG4138 239 V 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-223 |
6.17e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.78 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 20 GVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RRVGFLFQNPDSQIccN---T 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPYASL--NprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 94 VREELLFGFKALGL-DGPDADSRVDAIVEEFAFDPDDdpflLNR-------GARQLLALASIVVLAPPVVVLDEPTTGLD 165
Cdd:COG4608 114 VGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEH----ADRyphefsgGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 166 YRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:COG4608 190 VSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-223 |
9.84e-19 |
|
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: 82.59 E-value: 9.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VGF 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLD 158
Cdd:cd03218 80 LPQEA-SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHlrKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 159 EPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
1.04e-18 |
|
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: 85.51 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTT----MRLMNGLLKPDAGQVLIDGVPTSDLRTSE 73
Cdd:COG4172 6 LLSVEDLSVAFgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 74 LAR----RVGFLFQNPDS----------QICcntvrEELLFgfkALGLDGPDADSRVDAIVEEFAF-DP----DDDPFLL 134
Cdd:COG4172 86 LRRirgnRIAMIFQEPMTslnplhtigkQIA-----EVLRL---HRGLSGAAARARALELLERVGIpDPerrlDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 135 NRGARQ----LLALAS-----IVvlappvvvlDEPTTGLDyrecV----KVMDIIRRI-HERGTTVVMVCHDMEVVADYA 200
Cdd:COG4172 158 SGGQRQrvmiAMALANepdllIA---------DEPTTALD----VtvqaQILDLLKDLqRELGMALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|...
gi 496664120 201 ARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-224 |
1.37e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.11 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSApilKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGF 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNpdsqiccN------TVREELlfgfkALGLD-----GPDADSRVDAIVEEFAFDPdddpfLLNR-------GARQLL 142
Cdd:COG3840 76 LFQE-------NnlfphlTVAQNI-----GLGLRpglklTAEQRAQVEQALERVGLAG-----LLDRlpgqlsgGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 143 ALASIVVLAPPVVVLDEPTTGLD---YRECvkvMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTF 218
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDpalRQEM---LDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
....*.
gi 496664120 219 DVLRNR 224
Cdd:COG3840 216 ALLDGE 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-191 |
1.60e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDsqICCNTVREELLFGfkalgldGPDA-DSRVDAIVEEFAFDP--DDDPFL---LNRGARQL-------LALASI 147
Cdd:PRK11160 419 VSQRVH--LFSATLRDNLLLA-------APNAsDEALIEVLQQVGLEKllEDDKGLnawLGEGGRQLsggeqrrLGIARA 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496664120 148 VVLAPPVVVLDEPTTGLDYRECVKVMDIIRRiHERGTTVVMVCH 191
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITH 532
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-223 |
1.89e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 6 DVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSE------------ 73
Cdd:PRK10619 10 DLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 74 -LARRVGFLFQ--NPDSQIccnTVREELLFG-FKALGLDGPDADSRVDAIVEEFAFDP---DDDPFLLNRGARQLLALAS 146
Cdd:PRK10619 89 lLRTRLTMVFQhfNLWSHM---TVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDEraqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 147 IVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-213 |
2.73e-18 |
|
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: 80.92 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdsqiccntvreELLFGFKALGLDGPDADSRVDaIVEefAFDPDDDPFLLNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:cd03369 87 IPQDP-----------TLFSGTIRSNLDPFDEYSDEE-IYG--ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496664120 161 TTGLDYRECVKVMDIIRRIHErGTTVVMVCHDMEVVADYaARCIVMSGGEVVD 213
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-192 |
2.79e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 4 FRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsDLrtselarRVGFLFQ 83
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GL-------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 84 NP--DSQiccNTVREELLFGFKALG--------------------------------LDGPDADSRVDAIVEEFAFDPDD 129
Cdd:COG0488 69 EPplDDD---LTVLDTVLDGDAELRaleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARAEEILSGLGFPEED 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 130 dpflLNRGARQL-------LALASIVVLAPPVVVLDEPTTGLDyrecvkvMDIIR----RIHERGTTVVMVCHD 192
Cdd:COG0488 146 ----LDRPVSELsggwrrrVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHD 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-217 |
3.50e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.17 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 22 SFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptSDLRTSELARR-VGFLFQ--NPDSQIccnTVREEL 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRpVSMLFQenNLFSHL---TVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 99 lfgfkALGLDgP----DADSR--VDAIVEEFAFDPdddpfLLNR-------GARQLLALASIVVLAPPVVVLDEPTTGLD 165
Cdd:PRK10771 93 -----GLGLN-PglklNAAQRekLHAIARQMGIED-----LLARlpgqlsgGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 166 ---YRECVKVMDIIrrIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT 217
Cdd:PRK10771 162 palRQEMLTLVSQV--CQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPT 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
3.78e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.50 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL--LKPDA---GQVLIDGVPTSDLRTSELAR 76
Cdd:PRK14247 4 IEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEArvsGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 RVGFLFQNPDSqICCNTVREELLFGFK--ALGLDGPDADSRVDAIVEEFAF-----DPDDDPF-LLNRGARQLLALASIV 148
Cdd:PRK14247 83 RVQMVFQIPNP-IPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLwdevkDRLDAPAgKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 149 VLAPPVVVLDEPTTGLDYRECVKVMDIIRRIhERGTTVVMVCH---DMEVVADYAArciVMSGGEVVDDAPTFDVLRN 223
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHfpqQAARISDYVA---FLYKGQIVEWGPTREVFTN 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-240 |
5.59e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 21 VSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLkPDAGQVLIDGVPTSDLRTSELARRVGFLFQNPDSQIccntvreeLLF 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF--------AMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 101 GFKALGLDGPD------ADSRVDAIVEEFAFDPdddpfLLNRGARQL---------LAlASIVVLAPPVVVL------DE 159
Cdd:PRK03695 86 VFQYLTLHQPDktrteaVASALNEVAEALGLDD-----KLGRSVNQLsggewqrvrLA-AVVLQVWPDINPAgqllllDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNrETLERASLVPPQIVE 239
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP-ENLAQVFGVNFRRLD 238
|
.
gi 496664120 240 L 240
Cdd:PRK03695 239 V 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-212 |
1.28e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 10 SYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTtmrLMNGLLK--PDAGQVLIDGVPTSDLRTSELARRVGFLFQNPds 87
Cdd:PRK11174 359 SPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTS---LLNALLGflPYQGSLKINGIELRELDPESWRKHLSWVGQNP-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 88 QICCNTVREELLFGfkalgldGPDA-DSRVDAIVE-----EF--------AFDPDDDPFLLNRGARQLLALASIVVLAPP 153
Cdd:PRK11174 433 QLPHGTLRDNVLLG-------NPDAsDEQLQQALEnawvsEFlpllpqglDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 154 VVVLDEPTTGLDYRECVKVMDIIRRIHeRGTTVVMVCHDMEVVADYaARCIVMSGGEVV 212
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-223 |
1.43e-17 |
|
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: 82.04 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLkPDAGQVLIDGVPTSDLRTSELA---RRVGFLFQNPDS------- 87
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDPFGslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 88 --QIccntVREELLfgFKALGLDGPDADSRVDAIVEEFAFDPDDdpflLNR-------GARQLLALASIVVLAPPVVVLD 158
Cdd:COG4172 381 vgQI----IAEGLR--VHGPGLSAAERRARVAEALEEVGLDPAA----RHRyphefsgGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 159 EPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-233 |
6.15e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSE-LARRVGFLFQN----PDSqiccn 92
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFG---FKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVVVLDEPTTGLDYR 167
Cdd:PRK11288 95 TVAENLYLGqlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 168 ECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDdapTFDVLRNretLERASLV 233
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA---TFDDMAQ---VDRDQLV 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-221 |
8.81e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 20 GVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI---DGVPTSDLRTSELARRV------GFLFQNPdsqic 90
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRllrtewGFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 91 cntvREELLFGFKAlgldGPDADSRVDAI---------------VEEFAFDP---DDDPFLLNRGARQLLALASIVVLAP 152
Cdd:PRK11701 99 ----RDGLRMQVSA----GGNIGERLMAVgarhygdiratagdwLERVEIDAariDDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRR-IHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVL 221
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
9.94e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVhASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGf 80
Cdd:PRK13539 2 MLEGEDL-ACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 lFQNPdsqicCN---TVREELLFGFKALGldgpDADSRVDAIVEEFAFDP-DDDPF-LLNRGARQLLALASIVVLAPPVV 155
Cdd:PRK13539 80 -HRNA-----MKpalTVAENLEFWAAFLG----GEELDIAAALEAVGLAPlAHLPFgYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCH 191
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-214 |
1.76e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA----RRVGFLFQN----PDSQ 88
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFhhllPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCNtVREELLFGFKALGldgpDADSRVDAIVEEFAFD--PDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDY 166
Cdd:PRK11629 104 ALEN-VAMPLLIGKKKPA----EINSRALEMLAAVGLEhrANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496664120 167 RECVKVMDIIRRIHER-GTTVVMVCHDMEvVADYAARCIVMSGGEVVDD 214
Cdd:PRK11629 179 RNADSIFQLLGELNRLqGTAFLVVTHDLQ-LAKRMSRQLEMRDGRLTAE 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
2.08e-16 |
|
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: 75.99 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPIlkGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVptsDLRTSELARR-VGF 80
Cdd:cd03298 1 VRLDKIRFSY-GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRpVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNpdsqiccNTVREEL-LFGFKALGLD-----GPDADSRVDAIVEEFAFDPDDD--PFLLNRGARQLLALASIVVLAP 152
Cdd:cd03298 75 LFQE-------NNLFAHLtVEQNVGLGLSpglklTAEDRQAIEVALARVGLAGLEKrlPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-212 |
3.18e-16 |
|
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: 75.77 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 12 DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA---GQVLIDGVPtsdLRTSELARRVGFLFQNpDSQ 88
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQKCVAYVRQD-DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCNTVREELLFGFKaLGLDGPDADSRVDAIVEEF-----AFDPDDDPFL--LNRGARQLLALASIVVLAPPVVVLDEPT 161
Cdd:cd03234 93 LPGLTVRETLTYTAI-LRLPRKSSDAIRKKRVEDVllrdlALTRIGGNLVkgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 162 TGLDYRECVKVMDIIRRIHERGTTVVMVCH----DMEVVADyaaRCIVMSGGEVV 212
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHqprsDLFRLFD---RILLLSSGEIV 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-221 |
3.89e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQNPDSQICCNTVREE 97
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 98 LL-FGFKA-LGLDGPDADSRVDAIVEEFAFDPDDD---PFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKV 172
Cdd:PRK15112 109 ILdFPLRLnTDLEPEQREKQIIETLRQVGLLPDHAsyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496664120 173 MDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVL 221
Cdd:PRK15112 189 INLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-192 |
6.36e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK10247 7 LLQLQNVGYLAGD-AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdsQICCNTVREELLFGFKALGlDGPDADSRVDAIvEEFAFdPDDdpfLLNR-------GARQLLALASIVVLAPP 153
Cdd:PRK10247 86 CAQTP--TLFGDTVYDNLIFPWQIRN-QQPDPAIFLDDL-ERFAL-PDT---ILTKniaelsgGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496664120 154 VVVLDEPTTGLDYRECVKVMDIIRR-IHERGTTVVMVCHD 192
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLWVTHD 197
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-212 |
1.02e-15 |
|
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: 74.99 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSEL----ARRVGFLFQN---- 84
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSfall 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 85 PDsqiccNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDD--PFLLNRGARQLLALASIVVLAPPVVVLDEPTT 162
Cdd:cd03294 115 PH-----RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHkyPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496664120 163 GLD---YREcvkVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:cd03294 190 ALDpliRRE---MQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-202 |
1.47e-15 |
|
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: 73.30 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSeLARRVGFL 81
Cdd:cd03231 1 LEADELTCERDGRA-LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQICCnTVREELLFgFKALGLDGP--DADSRVD-AIVEEFAFDPdddpflLNRGARQLLALASIVVLAPPVVVLD 158
Cdd:cd03231 79 GHAPGIKTTL-SVLENLRF-WHADHSDEQveEALARVGlNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496664120 159 EPTTGLDYRECVKVMDIIRRIHERGTTVVMVCH-DMEVVADYAAR 202
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGARE 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-224 |
1.50e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 5 RDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtsELARrvgFLFQN 84
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR--EDTR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 85 ----PDSQICCNTvreellfgfkALGLDG---PDADSRVDAI-VEEFAfdpDDDPFLLNRGARQLLALASIVVLAPPVVV 156
Cdd:PRK11247 90 arllPWKKVIDNV----------GLGLKGqwrDAALQALAAVgLADRA---NEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 157 LDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDM-EVVAdYAARCIVMSGGEVVDDApTFDVLRNR 224
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVsEAVA-MADRVLLIEEGKIGLDL-TVDLPRPR 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-191 |
1.52e-15 |
|
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: 73.05 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLM-----NGLLKpdaGQVLIDGVPtsdlRTSELARRVGFLFQNpDS 87
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRP----LDKNFQRSTGYVEQQ-DV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 88 QICCNTVREELLFGFKALGLdGPDADSRVdAIVEEFAFDPdddpfllnrgarQLLALasivvlappvvvlDEPTTGLDYR 167
Cdd:cd03232 90 HSPNLTVREALRFSALLRGL-SVEQRKRL-TIGVELAAKP------------SILFL-------------DEPTSGLDSQ 142
|
170 180
....*....|....*....|....
gi 496664120 168 ECVKVMDIIRRIHERGTTVVMVCH 191
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCTIH 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-213 |
1.54e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI-DGVptsdlrtselarRVG 79
Cdd:COG0488 315 VLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQ-----NPDsqiccNTVREELlfgfKALGLDGPDADSRvdAIVEEFAFDPDDdpflLNRGARQL-------LALASI 147
Cdd:COG0488 382 YFDQhqeelDPD-----KTVLDEL----RDGAPGGTEQEVR--GYLGRFLFSGDD----AFKPVGVLsggekarLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 148 VVLAPPVVVLDEPTTGLDyrecvkvMDIIRRIHE-----RGtTVVMVCHD---MEVVADyaaRCIVMSGGEVVD 213
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLD-------IETLEALEEalddfPG-TVLLVSHDryfLDRVAT---RILEFEDGGVRE 509
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-211 |
1.97e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.12 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSElaRRVGFL 81
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdSQICCNTVREELLFGFKALGL-DGPDA---DSRVDAIVE--EFAFDPDDDPFLLNRGARQLLALASIVVLAPPVV 155
Cdd:PRK10851 80 FQHY-ALFRHMTVFDNIAFGLTVLPRrERPNAaaiKAKVTQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
3.03e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL--LKPDA---GQVLIDG--VPTSDLRTSEL 74
Cdd:PRK14267 5 IETVNLRVYY-GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGrnIYSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ARRVGFLFQ--NPDSQIccnTVREELLFGFKALGLDGP--DADSRVD------AIVEEFAFDPDDDPFLLNRGARQLLAL 144
Cdd:PRK14267 84 RREVGMVFQypNPFPHL---TIYDNVAIGVKLNGLVKSkkELDERVEwalkkaALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 145 ASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERgTTVVMVCHD---MEVVADYAArciVMSGGEVVDDAPTFDVL 221
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSpaqAARVSDYVA---FLYLGKLIEVGPTRKVF 236
|
....
gi 496664120 222 RNRE 225
Cdd:PRK14267 237 ENPE 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-191 |
3.41e-15 |
|
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: 72.39 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRtSELARRVGFLFQNPDSQICCn 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFgfkaLGLDGPDADSRVDAIVEEFAF-DPDDDPF-LLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECV 170
Cdd:TIGR01189 89 SALENLHF----WAAIHGGAQRTIEDALAAVGLtGFEDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 496664120 171 KVMDIIRRIHERGTTVVMVCH 191
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-223 |
4.44e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.68 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSEL----ARRVGFLFQN----PDSQI 89
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfalmPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 90 CCNTVreellFGFKALGLDGPDADSR-VDAI----VEEFAFDPDDDpflLNRGARQLLALASIVVLAPPVVVLDEPTTGL 164
Cdd:PRK10070 124 LDNTA-----FGMELAGINAEERREKaLDALrqvgLENYAHSYPDE---LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 165 DYRECVKVMDIIRRI---HERgtTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:PRK10070 196 DPLIRTEMQDELVKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-123 |
5.19e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.37 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VG 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 496664120 80 FLFQNPdS---QIccnTVREELLFGFKALGLDGPDADSRVDAIVEEF 123
Cdd:COG1137 82 YLPQEA-SifrKL---TVEDNILAVLELRKLSKKEREERLEELLEEF 124
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-191 |
5.61e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTM-----RLMNGLLKpdAGQVLIDGVPtsdLRTSELARRVGFLFQNpDSQICC 91
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMP---IDAKEMRAISAYVQQD-DLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 92 NTVREELLFG--FKaLGLDGPDAD--SRVDAIVEEFAFDP--------DDDPFLLNRGARQLLALASIVVLAPPVVVLDE 159
Cdd:TIGR00955 114 LTVREHLMFQahLR-MPRRVTKKEkrERVDEVLQALGLRKcantrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|..
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERGTTVVMVCH 191
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-212 |
7.07e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 4 FRDVHAsydgsapiLKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLrTSELARR--VGFL 81
Cdd:PRK09700 15 FGPVHA--------LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAAQlgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdSQICCNTVREELLFGF----KALGLDGPD---ADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAP 152
Cdd:PRK09700 86 YQEL-SVIDELTVLENLYIGRhltkKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVanLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-209 |
1.92e-14 |
|
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: 70.96 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELArrvgfLFQNPdSQICCNTVREE 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNY-SLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 98 LLFGFKALGLDGPDADSRvdAIVEE------FAFDPDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVK 171
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERR--AIVEEhialvgLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 496664120 172 VMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:TIGR01184 153 LQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-233 |
2.20e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKP-----DAGQVLIDGVPTSDLR-TSELARRVGFLFQNPDSqiC 90
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNP--F 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 91 CNTVREELLFGFKALGLDGPD-----ADSRV------DAIVEEFAfdpdDDPFLLNRGARQLLALASIVVLAPPVVVLDE 159
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKefrgvAQARLtevglwDAVKDRLS----DSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERgTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRETLERASLV 233
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-213 |
2.89e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTT----MRLMNGllkpdAGQVLIDGVPTSDLRTSEL---ARRVGFLFQNPDS-- 87
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINS-----QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 88 -------QIccntVREELLFGFKAlgLDGPDADSRVDAIVEEFAFDPDDD---PFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK15134 376 nprlnvlQI----IEEGLRVHQPT--LSAAQREQQVIAVMEEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-232 |
3.21e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VGFLFQNP---------D 86
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEAsifrrlsvyD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 87 SQICCNTVREEllfgfkalgLDGPDADSRVDAIVEEFAFDPDDDPF--LLNRGARQLLALASIVVLAPPVVVLDEPTTGL 164
Cdd:PRK10895 98 NLMAVLQIRDD---------LSAEQREDRANELMEEFHIEHLRDSMgqSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 165 DYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNrETLERASL 232
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD-EHVKRVYL 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-203 |
4.03e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDL----RTSELARRVGFLFQN----PDSQ 88
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCNTVREELLFGFKalgldgpDADSRVDAI--VEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGL 164
Cdd:PRK10584 105 ALENVELPALLRGES-------SRQSRNGAKalLEQLGLGKrlDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496664120 165 DYRECVKVMDIIRRI-HERGTTVVMVCHDMEVvadyAARC 203
Cdd:PRK10584 178 DRQTGDKIADLLFSLnREHGTTLILVTHDLQL----AARC 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-211 |
4.12e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptSDLRTSELARRVGfLFQNPDSQICCN--T 93
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQS-LGMCPQHNILFHhlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 94 VREELLFGFKALGLDGPDADSRVDAIVEEFAF--DPDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVK 171
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496664120 172 VMDIIRRiHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:TIGR01257 1100 IWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-165 |
4.30e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 21 VSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPT--SDLRTSelaRRVGFLfqnpdSQ-------Icc 91
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATR---RRVGYM-----SQafslygeL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 92 nTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALAS---------IvvlappvvvLDEP 160
Cdd:NF033858 355 -TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADvaDALPDSLPLGIRQRLSLAVavihkpellI---------LDEP 424
|
....*
gi 496664120 161 TTGLD 165
Cdd:NF033858 425 TSGVD 429
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-213 |
5.71e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFL 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsqiccnTVREELLFGFKALGLD-GPDADSRVDAIVE--EFAFD-PD-------DDPFLLNRGARQLLALASIVVL 150
Cdd:PRK10790 421 QQDP-------VVLADTFLANVTLGRDiSEEQVWQALETVQlaELARSlPDglytplgEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIHERgTTVVMVCHDMEVVADyAARCIVMSGGEVVD 213
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
1.25e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQICCNTVREEL-LFGFKAlglDGPDADSRVDAIVEEFafdpdddPFLLNR----------GARQLLALASIVV 149
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLaMGGFFA---ERDQFQERIKWVYELF-------PRLHERriqragtmsgGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 150 LAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-226 |
1.37e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:PLN03232 1234 SIKFEDVHLRYrPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 FLFQNPdsQICCNTVReellFGFKALGlDGPDAD-------SRVDAIVEEFAFDPDDDPFL----LNRGARQLLALASIV 148
Cdd:PLN03232 1314 IIPQSP--VLFSGTVR----FNIDPFS-EHNDADlwealerAHIKDVIDRNPFGLDAEVSEggenFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 149 VLAPPVVVLDEPTTGLDYRECVKVMDIIRRiHERGTTVVMVCHDMEVVADyAARCIVMSGGEVVD-DAPtfDVLRNRET 226
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEyDSP--QELLSRDT 1461
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-211 |
1.53e-13 |
|
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: 67.46 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSE-LARRVGFLfqnPDSQiccntvRE 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYV---PEDR------KR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 97 ELLFgfkaLGLDgpdadsrvdaIVEEFAFdpdddPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDyrecVK----V 172
Cdd:cd03215 87 EGLV----LDLS----------VAENIAL-----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGakaeI 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 496664120 173 MDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:cd03215 144 YRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-85 |
8.09e-13 |
|
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: 65.63 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL--LKPDAGQVLIDGVPTSDLRTSELARRVG 79
Cdd:cd03217 1 LEIKDLHVSVGGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGI 79
|
....*..
gi 496664120 80 FL-FQNP 85
Cdd:cd03217 80 FLaFQYP 86
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-68 |
9.78e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 9.78e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSD 68
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA 389
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-201 |
1.63e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 11 YDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL--LKPDA---GQVLIDG--VPTSDLRTSELARRVGFLFQ 83
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGknLYAPDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 84 NPDSqiCCNTVREELLFGFKALGLDGpDADSRVD------AIVEEFAFDPDDDPFLLNRGARQLLALASIVVLAPPVVVL 157
Cdd:PRK14243 99 KPNP--FPKSIYDNIAYGARINGYKG-DMDELVErslrqaALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERgTTVVMVCHDMEV---VADYAA 201
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQaarVSDMTA 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-223 |
1.63e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 5 RDVHAsydgsapiLKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELA---RRVGFL 81
Cdd:PRK10261 335 REVHA--------VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQI-CCNTVREELLFGFKALGL-DGPDADSRVDAIVEEFAFDPDDD---PFLLNRGARQLLALASIVVLAPPVVV 156
Cdd:PRK10261 407 FQDPYASLdPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwryPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 157 LDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRN 223
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-231 |
2.18e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlrTSELARRVGFL 81
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQN----PDSQIccntvREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVV 155
Cdd:PRK11432 84 FQSyalfPHMSL-----GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVdqISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDME---VVADyaaRCIVMSGGEVVDDAPTFDVLRNRETLERAS 231
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSeafAVSD---TVIVMNKGKIMQIGSPQELYRQPASRFMAS 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-209 |
2.54e-12 |
|
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: 64.76 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDgvptSDLRTSELA----------RR--VGFLfq 83
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDGGWVDLAqaspreilalRRrtIGYV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 84 npdSQI--------CCNTVREELLfgfkALGLDGPDADSRVDAiveefafdpdddpfLLNR-----------------GA 138
Cdd:COG4778 99 ---SQFlrviprvsALDVVAEPLL----ERGVDREEARARARE--------------LLARlnlperlwdlppatfsgGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 139 RQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-216 |
2.80e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGS-APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PLN03130 1238 IKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdsQICCNTVREEL----------------------LFGFKALGLdgpdaDSRVDAIVEEFAFdpdddpfllnrGA 138
Cdd:PLN03130 1318 IPQAP--VLFSGTVRFNLdpfnehndadlweslerahlkdVIRRNSLGL-----DAEVSEAGENFSV-----------GQ 1379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 139 RQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRiHERGTTVVMVCHDMEVVADyAARCIVMSGGEVVD-DAP 216
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEfDTP 1456
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-217 |
4.57e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG--VPTSDLRTSELARR-VGFLFQNPDSQIccN-- 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdLLKADPEAQKLLRQkIQIVFQNPYGSL--Npr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 -----TVREELLFGFKalgLDGPDADSRVDAIVEEFAFDP---DDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGL 164
Cdd:PRK11308 109 kkvgqILEEPLLINTS---LSAAERREKALAMMAKVGLRPehyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 165 DyrecVKV--------MDIIRrihERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT 217
Cdd:PRK11308 186 D----VSVqaqvlnlmMDLQQ---ELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-84 |
4.91e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.81 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGS-APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
....
gi 496664120 81 LFQN 84
Cdd:PRK11176 422 VSQN 425
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-216 |
5.13e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 14 SAPILKG-VSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTsDLRTSELARRVGFLFQNPDSQ---- 88
Cdd:PRK11288 264 KGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIRAGIMLCPEDRKaegi 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCNTVREEL------LFGFKALGLDGPDADSRVDAIVEEFAF---DPDDDPFLLNRGARQLLALASIVVLAPPVVVLDE 159
Cdd:PRK11288 343 IPVHSVADNInisarrHHLRAGCLINNRWEAENADRFIRSLNIktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 160 PTTGLDYRECVKVMDIIRRIHERGTTVVMVCHD-MEV--VADyaaRCIVMSGGEVVDDAP 216
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVlgVAD---RIVVMREGRIAGELA 479
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-59 |
6.86e-12 |
|
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: 61.70 E-value: 6.86e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 2 IEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV 59
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-208 |
8.32e-12 |
|
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: 63.58 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 24 TIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTS---DLRTSELARRV-GFLFQNPDSQICCNTVREELL 99
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKADYEGTVrDLLSSITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 100 fgfKALGLDgPDADSRVdaiveefafdPDddpflLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRI 179
Cdd:cd03237 101 ---KPLQIE-QILDREV----------PE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180 190
....*....|....*....|....*....|.
gi 496664120 180 HERGTTVVMVC-HDMeVVADYAA-RCIVMSG 208
Cdd:cd03237 162 AENNEKTAFVVeHDI-IMIDYLAdRLIVFEG 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-194 |
1.21e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTsDLRTSELARRVGF-LFQNPDSQICCNTVRE 96
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGIsMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 97 ELLFG---FKALGLDGPDADSRVDAIVEEFAF--DPDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVK 171
Cdd:PRK10982 93 NMWLGrypTKGMFVDQDKMYRDTKAIFDELDIdiDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180
....*....|....*....|...
gi 496664120 172 VMDIIRRIHERGTTVVMVCHDME 194
Cdd:PRK10982 173 LFTIIRKLKERGCGIVYISHKME 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-209 |
1.35e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlrtsELARRvGF 80
Cdd:PRK11248 1 MLQISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG----PGAER-GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNpDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPFL--LNRGARQLLALASIVVLAPPVVVLD 158
Cdd:PRK11248 75 VFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwqLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496664120 159 EPTTGLD--YRECVKVMdIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:PRK11248 154 EPFGALDafTREQMQTL-LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-232 |
2.83e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 20 GVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VGFLFQNPD--SQIccnTVRE 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRlfREM---TVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 97 ELLF--------GFKAlGLDGPDADSRVDAIVEEFAFDPDDDPFLL---NRGARQL-------LALASIVVLAPPVVVLD 158
Cdd:PRK11300 100 NLLVaqhqqlktGLFS-GLLKTPAFRRAESEALDRAATWLERVGLLehaNRQAGNLaygqqrrLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 159 EPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGE-VVDDAPtfDVLRNRETLERASL 232
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTpLANGTP--EEIRNNPDVIKAYL 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-251 |
6.72e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA--GQVLIDGVP--TSDLRTSElarRVGFLFQNPDSQ 88
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkASNIRDTE---RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCN-TVREELLFG----FKALGLDGPDADSRVDAIVEEFAFDPDDDPFL---LNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:TIGR02633 89 LVPElSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvgdYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 161 TTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVddaptfdvlrnrETLERASLVPPQIVel 240
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV------------ATKDMSTMSEDDII-- 234
|
250
....*....|.
gi 496664120 241 SLELGREMPHL 251
Cdd:TIGR02633 235 TMMVGREITSL 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-222 |
7.21e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA--------GQVLIDGVPTSDLRTSELARRVGFLFQNPDSQ 88
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCnTVREELLFG-------------------FKALGLDGPDADSRVDAIV---EEFA----------FDPDDDPfllNR 136
Cdd:PRK13547 96 FAF-SAREIVLLGrypharragalthrdgeiaWQALALAGATALVGRDVTTlsgGELArvqfarvlaqLWPPHDA---AQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 137 GARQLLalasivvlappvvvLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDA 215
Cdd:PRK13547 172 PPRYLL--------------LDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
....*..
gi 496664120 216 PTFDVLR 222
Cdd:PRK13547 238 APADVLT 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-222 |
7.25e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 21 VSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLL----KPDAGQVLIDGvptSDL-RTSELARR------VGFLFQNPDSQI 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNG---QDLqRISEKERRnlvgaeVAMIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 90 C-CNTVREELLFGFKA----------------LGLDG-PDADSRVDAIveefafdpdddPFLLNRGARQLLALASIVVLA 151
Cdd:PRK11022 103 NpCYTVGFQIMEAIKVhqggnkktrrqraidlLNQVGiPDPASRLDVY-----------PHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 152 PPVVVLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLR 222
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-223 |
7.78e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.94 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMN--GLLKPD---AGQVLIDG----VPTSDlrT 71
Cdd:PRK14239 5 ILQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGhniySPRTD--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 72 SELARRVGFLFQNPDSqiCCNTVREELLFGfkaLGLDGPDADSRVDAIVE----------EFAFDPDDDPFLLNRGARQL 141
Cdd:PRK14239 82 VDLRKEIGMVFQQPNP--FPMSIYENVVYG---LRLKGIKDKQVLDEAVEkslkgasiwdEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 142 LALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERgTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVL 221
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
..
gi 496664120 222 RN 223
Cdd:PRK14239 236 MN 237
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-224 |
7.94e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPdsQICCNTVREEL-LFGFKA-----LGLDGPDADSRVDAIVEEFAFDPDDDPFLLNRGARQLLALASIVVLAPPV 154
Cdd:TIGR00957 1365 IPQDP--VLFSGSLRMNLdPFSQYSdeevwWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 155 VVLDEPTTGLDYRECVKVMDIIRRIHErGTTVVMVCHDMEVVADYaARCIVMSGGEVVD-DAPTfDVLRNR 224
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEfGAPS-NLLQQR 1510
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-209 |
1.20e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASY---DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPD---AGQVLIDGVPTSDLRTSEL 74
Cdd:PRK09473 12 LLDVKDLRVTFstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ----ARRVGFLFQNPDSQIccN---TVREEL---LFGFKALG-----------LDG---PDADSRVDAIVEEFAfdpddd 130
Cdd:PRK09473 92 nklrAEQISMIFQDPMTSL--NpymRVGEQLmevLMLHKGMSkaeafeesvrmLDAvkmPEARKRMKMYPHEFS------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 131 pfllnRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:PRK09473 164 -----GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-213 |
1.71e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG----------VPTSDLRTSELARRVG----FL 81
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQIC-CNTVREELLFGFKA-LGLDGPDADSRVDAIVEEFAFdPDDD------PFLLNRGARQLLALASIVVLAPP 153
Cdd:PRK10261 110 FQEPMTSLNpVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRI-PEAQtilsryPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 154 VVVLDEPTTGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-219 |
2.59e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.64 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPD-AGQVLIDGVPTSDLRTSELARRV-------GFLFQ--NPDS 87
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDkSAGSHIELLGRTVQREGRLARDIrksrantGYIFQqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 88 QIccnTVREELLFGfkALG-----------------LDGPDADSRVDaiVEEFAFDPDDDpflLNRGARQLLALASIVVL 150
Cdd:PRK09984 100 RL---SVLENVLIG--ALGstpfwrtcfswftreqkQRALQALTRVG--MVHFAHQRVST---LSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 151 APPVVVLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT--FD 219
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSqqFD 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-212 |
2.89e-10 |
|
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: 60.59 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL--LKPDAGQVL------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 61 --------------IDGVPTSDLRTSELARRVGFLFQNPDSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEE---- 122
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 123 -----FAFDpdddpflLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRR-IHERGTTVVMVCHDMEVV 196
Cdd:TIGR03269 160 hrithIARD-------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVI 232
|
250
....*....|....*.
gi 496664120 197 ADYAARCIVMSGGEVV 212
Cdd:TIGR03269 233 EDLSDKAIWLENGEIK 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-201 |
3.20e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDgSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDaGQVLIDG--------VPTSDLRTSE 73
Cdd:PRK14258 8 IKVNNLSFYYD-TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 74 LARRVGFLFQNPDsqICCNTVREELLFGFKALGLDgPDADsrVDAIVEEFAFDPD----------DDPFLLNRGARQLLA 143
Cdd:PRK14258 86 LRRQVSMVHPKPN--LFPMSVYDNVAYGVKIVGWR-PKLE--IDDIVESALKDADlwdeikhkihKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 144 LASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGT-TVVMVCHDMEVV---ADYAA 201
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVsrlSDFTA 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-208 |
4.37e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 24 TIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG---------VPTSDLRTSELARRVGflfqnpdSQICCNTV 94
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELkisykpqyiKPDYDGTVEDLLRSIT-------DDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 95 REELLfgfKALGLDgPDADSRVDAiveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMD 174
Cdd:PRK13409 434 KSEII---KPLQLE-RLLDKNVKD---------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 496664120 175 IIRRIHE-RGTTVVMVCHDMeVVADYAA-RCIVMSG 208
Cdd:PRK13409 495 AIRRIAEeREATALVVDHDI-YMIDYISdRLMVFEG 529
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-204 |
4.76e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptSDLRTSELARRVGFLFQNPDSQICCN-TV 94
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER---QSIKKDLCTYQKQLCFVGHRSGINPYlTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 95 REELLFgfkalGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKV 172
Cdd:PRK13540 92 RENCLY-----DIHFSPGAVGITELCRLFSLEHliDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180 190
....*....|....*....|....*....|....
gi 496664120 173 MDIIRRIHERGTTVVMVCH-DMEV-VADYAARCI 204
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHqDLPLnKADYEEYHL 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-200 |
4.94e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASyDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG--VPT-SDLRTSELARR 77
Cdd:PRK11831 7 LVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAmSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQN------------------PDSQICCNTVREELLFGFKALGLDG-----PDADS----RVDAIVEEFAFDPD-- 128
Cdd:PRK11831 86 MSMLFQSgalftdmnvfdnvayplrEHTQLPAPLLHSTVMMKLEAVGLRGaaklmPSELSggmaRRAALARAIALEPDli 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 129 --DDPFLlnrgarqllalasivvlappvvVLDEPTTGLdyreCVKVMDIIRriHERGTTVVMVCHDM-EV--VADYA 200
Cdd:PRK11831 166 mfDEPFV----------------------GQDPITMGV----LVKLISELN--SALGVTCVVVSHDVpEVlsIADHA 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-212 |
7.05e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTsDLRTSE--LARRVGF---------L 81
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRdaIRAGIAYvpedrkgegL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNpdsqiccNTVREEL----LFGFKALG-LDGPDADSRVDAIVEEF---AFDPDDDPFLLNRG-------ARQLLA--- 143
Cdd:COG1129 342 VLD-------LSIRENItlasLDRLSRGGlLDRRRERALAEEYIKRLrikTPSPEQPVGNLSGGnqqkvvlAKWLATdpk 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 144 ---LasivvlappvvvlDEPTTGLD-------YRecvkvmdIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVV 212
Cdd:COG1129 415 vliL-------------DEPTRGIDvgakaeiYR-------LIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-165 |
1.48e-09 |
|
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: 58.41 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI-DGVptsdlrtselarRVGF 80
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNPDSQICCNTVREELLFGFKALGLDGPDADSRvdAIVEEFAFDPDDDPFL---LNRGARQLLALASIVVLAPPVVVL 157
Cdd:TIGR03719 390 VDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSR--AYVGRFNFKGSDQQKKvgqLSGGERNRVHLAKTLKSGGNVLLL 467
|
....*...
gi 496664120 158 DEPTTGLD 165
Cdd:TIGR03719 468 DEPTNDLD 475
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-85 |
2.40e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 2.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 15 APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTsdlRTSELARRVGFLFQNP 85
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYLGHLP 91
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-196 |
2.49e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAG------QVLIDGVPTSDLRTSEL 74
Cdd:PRK09544 4 LVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGvikrngKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 75 ARRVG-FLFQNPdsqiccNTVREELLFGFKALgldgpDADSRVDAIVEEfafdpdddpflLNRGARQLLALASIVVLAPP 153
Cdd:PRK09544 83 PLTVNrFLRLRP------GTKKEDILPALKRV-----QAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496664120 154 VVVLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVV 196
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLV 184
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-72 |
2.75e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 2.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 496664120 20 GVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTS 72
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE 71
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-208 |
3.70e-09 |
|
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: 57.10 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSApiLKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVlidgvpTSDLRTSELARRVgfl 81
Cdd:COG1245 342 VEYPDLTKSYGGFS--LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKISYKPQYI--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 fqNPDSQIccnTVrEELLFGFKALGLDGPDADSRvdaIVEEFAFDPdddpfLLNR-------GARQLLALASIVVLAPPV 154
Cdd:COG1245 411 --SPDYDG---TV-EEFLRSANTDDFGSSYYKTE---IIKPLGLEK-----LLDKnvkdlsgGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 155 VVLDEPTTGLDYRECVKVMDIIRRIHE-RGTTVVMVCHDMEVVaDYAA-RCIVMSG 208
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMVVDHDIYLI-DYISdRLMVFEG 531
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-210 |
5.04e-09 |
|
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: 55.84 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 26 RDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQvlIDGVPTSD-----LRTSELarrvgflfQNPDSQICCNTVR----- 95
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDeildeFRGSEL--------QNYFTKLLEGDVKvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 96 ---EELLFGFKA---LGLDGPDADSRVDAIVEEFAFDP--DDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYR 167
Cdd:cd03236 94 qyvDLIPKAVKGkvgELLKKKDERGKLDELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496664120 168 ECVKVMDIIRRIHERGTTVVMVCHDMEVVaDYAARCIVMSGGE 210
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHDLAVL-DYLSDYIHCLYGE 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-85 |
1.11e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYD--GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI-DGVPTSDLRTSELARRV 78
Cdd:PTZ00265 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
....*..
gi 496664120 79 GFLFQNP 85
Cdd:PTZ00265 463 GVVSQDP 469
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-211 |
1.33e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 21 VSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSE-LA---------RRVGFLFQnpDSQIC 90
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLArglvylpedRQSSGLYL--DAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 91 CNTVreELLFGFKALGLDgPDADSrvdAIVEEFAF-------DPDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTG 163
Cdd:PRK15439 360 WNVC--ALTHNRRGFWIK-PAREN---AVLERYRRalnikfnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496664120 164 LDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-216 |
2.05e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTM-----RLMNGLLKpdaGQVLIDGVPTsdlRTSELARRVGFLFQNP--DSQI 89
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYIE---GDIRISGFPK---KQETFARISGYCEQNDihSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 90 ccnTVREELLF-GFKALgldgPDADSR------VDAIVEEFAFDPDDDPFL-------LNRGARQLLALASIVVLAPPVV 155
Cdd:PLN03140 969 ---TVRESLIYsAFLRL----PKEVSKeekmmfVDEVMELVELDNLKDAIVglpgvtgLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 156 VLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCH--DMEVVADYAARCIVMSGGEVVDDAP 216
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGP 1104
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-211 |
2.16e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.09 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDaGQVLIDGVPTSDLRTSELARRVG- 79
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 80 -----FLF-----QNPDSQICCNTvrEELLFGFKALGLdgpdadsrvDAIVEEFA----FDPDDDPFLLNRGARQLLALA 145
Cdd:cd03289 82 ipqkvFIFsgtfrKNLDPYGKWSD--EEIWKVAEEVGL---------KSVIEQFPgqldFVLVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 146 SIVVLAPPVVVLDEPTTGLDyrecVKVMDIIRRIHER---GTTVVMVCHDMEVVADyAARCIVMSGGEV 211
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLD----PITYQVIRKTLKQafaDCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-230 |
4.76e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELarrVGFL 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQICCNTVREELL----FGFKALgLDGPDADSRvdAIVEEFAFDPDDDPFL------LNRGARQLLALASIVVLA 151
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVmmgrYGHMGW-LRRAKKRDR--QIVTAALARVDMVEFRhrqigeLSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 152 PPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARcIVMSGGEVVDDAPTfDVLRNRETLERA 230
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGPT-ETTFTAENLELA 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-257 |
4.92e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMrLMNGLLKPDAGQVLIDgVPTSDLRTSELARRVGFLFQNPDSQICCN 92
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWR-F*TWCANRRALRRTIG*HRPVR*GRRESF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFGFKALGLDGPDADSRVDAIVEEFAFD--PDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECV 170
Cdd:NF000106 102 SGRENLYMIGR*LDLSRKDARARADELLERFSLTeaAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 171 KVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTfDVLRNRETLERASLVPPQIVELSLELGREMPH 250
Cdd:NF000106 182 EVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV-DELKTKVGGRTLQIRPAHAAELDRMVGAIAQA 260
|
....*..
gi 496664120 251 LADGPVG 257
Cdd:NF000106 261 GLDGIAG 267
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-210 |
5.13e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 24 TIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVliDGVPTSD-----LRTSELarrvgflfQNPDSQICCNTVR--- 95
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPSWDevlkrFRGTEL--------QNYFKKLYNGEIKvvh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 96 -----EELLFGFKalG-----LDGPDADSRVDAIVEEFAFDPdddpfLLNRGARQL-------LALASIVVLAPPVVVLD 158
Cdd:PRK13409 165 kpqyvDLIPKVFK--GkvrelLKKVDERGKLDEVVERLGLEN-----ILDRDISELsggelqrVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496664120 159 EPTTGLDYRECVKVMDIIRRIHErGTTVVMVCHDMEVVaDYAARCIVMSGGE 210
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVL-DYLADNVHIAYGE 287
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-59 |
7.71e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 7.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 3 EFRDVHASYDGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV 59
Cdd:PRK11147 321 EMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-227 |
8.32e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARR-VGFL 81
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPDSQICC--NTVREELLFGF-------KALGLDGPDADSRVDAIVEEF---AFDPDDDPFLLNRG-------ARQLL 142
Cdd:COG3845 339 PEDRLGRGLVpdMSVAENLILGRyrrppfsRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPARSLSGGnqqkvilARELS 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 143 A-----LASivvlappvvvldEPTTGLdyrecvkvmDI--IRRIHER-------GTTVVMVCHDMEVVADYAARCIVMSG 208
Cdd:COG3845 419 RdpkllIAA------------QPTRGL---------DVgaIEFIHQRllelrdaGAAVLLISEDLDEILALSDRIAVMYE 477
|
250
....*....|....*....
gi 496664120 209 GEVVDDAPTFDVlrNRETL 227
Cdd:COG3845 478 GRIVGEVPAAEA--TREEI 494
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-59 |
9.06e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 9.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 496664120 2 IEFRDVHASYDGsAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV 59
Cdd:PRK15064 320 LEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-74 |
9.85e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 9.85e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsDLRTSEL 74
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ----DLIVARL 71
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-101 |
1.05e-07 |
|
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: 51.32 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG----SAPILKGVSFTIRDGEFVAFVGTNGAGKSTtmrLMNGLLkpdaGQV-LIDGvptsdlrTSELAR 76
Cdd:cd03250 1 ISVEDASFTWDSgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALL----GELeKLSG-------SVSVPG 66
|
90 100
....*....|....*....|....*
gi 496664120 77 RVGFLFQNPdsQICCNTVREELLFG 101
Cdd:cd03250 67 SIAYVSQEP--WIQNGTIRENILFG 89
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-199 |
1.17e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 24 TIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQvlIDGVPTSD-----LRTSELAR----------RVGFLFQNPD-- 86
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEPSWDevlkrFRGTELQDyfkklangeiKVAHKPQYVDli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 87 SQICCNTVREeLLfgfkalgldgPDADSR--VDAIVEEFAFDPdddpfLLNRGARQL-------LALASIVVLAPPVVVL 157
Cdd:COG1245 173 PKVFKGTVRE-LL----------EKVDERgkLDELAEKLGLEN-----ILDRDISELsggelqrVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEV---VADY 199
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAIldyLADY 281
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-211 |
1.42e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 14 SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDlRTSELARRVGFLFQNPDSQ----I 89
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT-RSPQDGLANGIVYISEDRKrdglV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 90 CCNTVREEL------LFGFKALGLDGPDADSRVDAIVEEFAFD-PDDDPF--LLNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:PRK10762 343 LGMSVKENMsltalrYFSRAGGSLKHADEQQAVSDFIRLFNIKtPSMEQAigLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496664120 161 TTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-191 |
1.46e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTM-----RLMNGLLkpDAGQVLIDGVPtsdlRTSELARRVGFLFQNpDSQICC 91
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRP----LDSSFQRSIGYVQQQ-DLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 92 NTVREELLFgfkALGLDGP------DADSRVDAIVEEFAFDPDDDPFL------LNRGARQLLALA-SIVVLAPPVVVLD 158
Cdd:TIGR00956 851 STVRESLRF---SAYLRQPksvsksEKMEYVEEVIKLLEMESYADAVVgvpgegLNVEQRKRLTIGvELVAKPKLLLFLD 927
|
170 180 190
....*....|....*....|....*....|...
gi 496664120 159 EPTTGLDYRECVKVMDIIRRIHERGTTVVMVCH 191
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-61 |
1.58e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPIlKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLI 61
Cdd:PRK11819 325 IEAENLSKSFGDRLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-213 |
2.68e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 11 YDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL-------LKPDaGQVLIDGVPTSDLRTSELARRVGFLFQ 83
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydskIKVD-GKVLYFGKDIFQIDAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 84 NPDSqICCNTVREELLFGFKALGLDgpdaDSR-VDAIVEEF---------AFDPDDDPF-LLNRGARQLLALASIVVLAP 152
Cdd:PRK14246 98 QPNP-FPHLSIYDNIAYPLKSHGIK----EKReIKKIVEEClrkvglwkeVYDRLNSPAsQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664120 153 PVVVLDEPTTGLDyreCVKVMDIIRRIHE--RGTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:PRK14246 173 KVLLMDEPTSMID---IVNSQAIEKLITElkNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-130 |
2.70e-07 |
|
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: 51.47 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 10 SYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIdgvptsdlrtsELARRVGFLFQNP--DS 87
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQEPqlDP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496664120 88 QiccNTVREELLFGFKalglDGPDADSRVDAIVEEFAfDPDDD 130
Cdd:TIGR03719 82 T---KTVRENVEEGVA----EIKDALDRFNEISAKYA-EPDAD 116
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-191 |
3.37e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 17 ILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPD--AGQVLIDGVPTsdlrTSELARRVGFLFQNpDSQICCNTV 94
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQD-DILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 95 REELLFGfkAL-----GLDGPDADSRVDAIVEEFAFDPDDDPFLLNR-------GARQLLALASIVVLAPPVVVLDEPTT 162
Cdd:PLN03211 158 RETLVFC--SLlrlpkSLTKQEKILVAESVISELGLTKCENTIIGNSfirgisgGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|....*....
gi 496664120 163 GLDYRECVKVMDIIRRIHERGTTVVMVCH 191
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-251 |
3.52e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 3 EFRDVHAsydgsapiLKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLkPDA---GQVLIDGVP--TSDLRTSElARR 77
Cdd:PRK13549 14 TFGGVKA--------LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEElqASNIRDTE-RAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 VGFLFQN----PDSqiccnTVREELLFG---FKALGLDGPDADSRVDAIVEE--FAFDPDDDPFLLNRGARQLLALASIV 148
Cdd:PRK13549 84 IAIIHQElalvKEL-----SVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQlkLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 149 VLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVAdyaarcivmsggEVVDdapTFDVLRNRE--- 225
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVK------------AISD---TICVIRDGRhig 223
|
250 260
....*....|....*....|....*.
gi 496664120 226 TLERASLVPPQIVelSLELGREMPHL 251
Cdd:PRK13549 224 TRPAAGMTEDDII--TMMVGRELTAL 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-130 |
6.41e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 11 YDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQ-VLIDGVptsdlrtselarRVGFLFQNP--DS 87
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI------------KVGYLPQEPqlDP 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496664120 88 QiccNTVREELLFGFKALgldgPDADSRVDAIVEEFAfDPDDD 130
Cdd:PRK11819 84 E---KTVRENVEEGVAEV----KAALDRFNEIYAAYA-EPDAD 118
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-209 |
7.92e-07 |
|
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: 50.40 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 11 YDG-SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG--VPTSdlrTSELARRVGFL--FQNP 85
Cdd:TIGR01257 1947 YSGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksILTN---ISDVHQNMGYCpqFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 86 DSQIccnTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDPDDDPF--LLNRGARQLLALASIVVLAPPVVVLDEPTTG 163
Cdd:TIGR01257 2024 DDLL---TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496664120 164 LDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGG 209
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-165 |
8.14e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGllKPD----AGQVLIDGVPTSDLRTSELAR 76
Cdd:CHL00131 7 ILEIKNLHASVNEN-EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 77 RVGFL-FQNPDS----------QICCNTVReellfgfKALGLDGPDADSRVDAIVEEFAFDPDDDPFL---LNRGAR--- 139
Cdd:CHL00131 84 LGIFLaFQYPIEipgvsnadflRLAYNSKR-------KFQGLPELDPLEFLEIINEKLKLVGMDPSFLsrnVNEGFSgge 156
|
170 180 190
....*....|....*....|....*....|...
gi 496664120 140 -------QLLALASIVVLAppvvvlDEPTTGLD 165
Cdd:CHL00131 157 kkrneilQMALLDSELAIL------DETDSGLD 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-101 |
1.26e-06 |
|
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: 48.70 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 15 APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsdlrtselarRVGFLFQNpdSQICCNTV 94
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQF--SWIMPGTI 114
|
....*..
gi 496664120 95 REELLFG 101
Cdd:cd03291 115 KENIIFG 121
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-213 |
1.45e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.93 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 19 KGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptSDLR-TSELARR-----VGFLFQNP----DSQ 88
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG---KDLLgMKDDEWRavrsdIQMIFQDPlaslNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 89 ICCNTVREELLFGFKAlGLDGPDADSRVDAIVEEFAFDPDddpfLLNR-------GARQLLALASIVVLAPPVVVLDEPT 161
Cdd:PRK15079 115 MTIGEIIAEPLRTYHP-KLSRQEVKDRVKAMMLKVGLLPN----LINRyphefsgGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496664120 162 TGLDYRECVKVMDIIRRIH-ERGTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
158-212 |
1.58e-06 |
|
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: 49.24 E-value: 1.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVV--ADYaarcIV-------MSGGEVV 212
Cdd:TIGR00630 857 DEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIktADY----IIdlgpeggDGGGTVV 916
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-262 |
2.62e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRdvhaSYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKpDAGQVLIDGVPTSD---LRTSELARR- 77
Cdd:PRK15093 11 IEFK----TSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDidlLRLSPRERRk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 78 -----VGFLFQNPDSqiCCN---TVREELLFGFKALGLDGPD------ADSRVDAIVEEFAFDPDDD-----PFLLNRGA 138
Cdd:PRK15093 86 lvghnVSMIFQEPQS--CLDpseRVGRQLMQNIPGWTYKGRWwqrfgwRKRRAIELLHRVGIKDHKDamrsfPYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 139 RQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHER-GTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPT 217
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 496664120 218 FDVLRN-----RETLERAslVPpqivelslELGREMPHLAdgpvgRANTL 262
Cdd:PRK15093 244 KELVTTphhpyTQALIRA--IP--------DFGSAMPHKS-----RLNTL 278
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-165 |
3.37e-06 |
|
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: 48.37 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsdlrtselarRVGFLFQNPdsQICCNTVR 95
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTS--WIMPGTIK 504
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 96 EELLFGfkaLGLDGPDADSRVDA--IVEEFAFDPDDDPFLLNRGA-------RQLLALASIVVLAPPVVVLDEPTTGLD 165
Cdd:TIGR01271 505 DNIIFG---LSYDEYRYTSVIKAcqLEEDIALFPEKDKTVLGEGGitlsggqRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-65 |
4.79e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 4.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLK--PDAGQVLIDGVP 65
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ 95
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-214 |
6.29e-06 |
|
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: 47.13 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 21 VSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPD-AGQVLIDGVPTsDLRTSELARRVGFLFQNPDSqiccntvREELL 99
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-DIRNPAQAIRAGIAMVPEDR-------KRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 100 FGFKALG-------LDGPDADSRVDAIVEEFAFDPD--------DDPFL----LNRGARQLLALASIVVLAPPVVVLDEP 160
Cdd:TIGR02633 351 VPILGVGknitlsvLKSFCFKMRIDAAAELQIIGSAiqrlkvktASPFLpigrLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496664120 161 TTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDD 214
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-85 |
7.22e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 7.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 14 SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQNP 85
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
158-199 |
7.42e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.07 E-value: 7.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVV--ADY 199
Cdd:cd03271 197 DEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIkcADW 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-194 |
7.66e-06 |
|
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: 47.21 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 5 RDVHASY--DGSApILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDaGQVLIDGVPTSDLRTSELARRVGFLF 82
Cdd:TIGR01271 1221 QGLTAKYteAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 83 QNpdSQICCNTVR-----------EELLFGFKALGLdgpdadsrvDAIVEEFA----FDPDDDPFLLNRGARQLLALASI 147
Cdd:TIGR01271 1299 QK--VFIFSGTFRknldpyeqwsdEEIWKVAEEVGL---------KSVIEQFPdkldFVLVDGGYVLSNGHKQLMCLARS 1367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496664120 148 VVLAPPVVVLDEPTTGLDyrecVKVMDIIRRIHERG---TTVVMVCHDME 194
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD----PVTLQIIRKTLKQSfsnCTVILSEHRVE 1413
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-63 |
9.60e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 9.60e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDG 63
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-67 |
1.49e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTS 67
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT 69
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
158-227 |
1.93e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVAdYAARCIVMS------GGEVVDDAPTFDVLRNRETL 227
Cdd:PRK00635 503 DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LADRIIDIGpgagifGGEVLFNGSPREFLAKSDSL 577
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-208 |
2.31e-05 |
|
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: 44.10 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 25 IRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVptsdlrtselarRVGFLFQNPDsqiccntvreellfgfka 104
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYID------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 105 lgldgpdadsrvdaiveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGT 184
Cdd:cd03222 72 -----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*.
gi 496664120 185 -TVVMVCHDMeVVADYAA-RCIVMSG 208
Cdd:cd03222 123 kTALVVEHDL-AVLDYLSdRIHVFEG 147
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
158-212 |
2.69e-05 |
|
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: 43.85 E-value: 2.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVaDYAARCIVM------SGGEVV 212
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVV 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-216 |
2.98e-05 |
|
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: 45.32 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsdlrtselarRVGFLFQNPDSQICcn 92
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQND-- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 93 TVREELLFGfKALgldgpdADSRVDAIVEEFAFDPD-------------DDPFLLNRGARQLLALASIVVLAPPVVVLDE 159
Cdd:TIGR00957 714 SLRENILFG-KAL------NEKYYQQVLEACALLPDleilpsgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 160 PTTGLD-------YRECVKVMDIIrriheRGTTVVMVCHDMEVVADYAArCIVMSGGEVVDDAP 216
Cdd:TIGR00957 787 PLSAVDahvgkhiFEHVIGPEGVL-----KNKTRILVTHGISYLPQVDV-IIVMSGGKISEMGS 844
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-73 |
3.04e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 3.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLkPDA---GQVLIDGVPT--SDLRTSE 73
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCrfKDIRDSE 76
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-59 |
4.14e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 4.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 1 MIEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV 59
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-211 |
6.03e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 19 KGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGV---PTSDLRT--------SELARRVGFlFQNPDS 87
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAvkkgmayiTESRRDNGF-FPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 88 QICCNTVREELLFGFK-ALGLDGPDADSRV-DAIVEEFAF---DPDDDPFLLNRGARQLLALASIVVLAPPVVVLDEPTT 162
Cdd:PRK09700 359 AQNMAISRSLKDGGYKgAMGLFHEVDEQRTaENQRELLALkchSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496664120 163 GLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEV 211
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-85 |
6.35e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 1 MIEFRDVHASYDGSaPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGL--LKPDAGQVLIDGVPTSDLRTSELARRV 78
Cdd:PRK09580 1 MLSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEG 79
|
....*...
gi 496664120 79 GFL-FQNP 85
Cdd:PRK09580 80 IFMaFQYP 87
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-187 |
7.22e-05 |
|
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: 42.63 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 15 APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA---GQVLIDGVPtSDLRTSELARRVGFLFQNpDSQICC 91
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIP-YKEFAEKYPGEIIYVSEE-DVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 92 NTVREELLFGFKALGldgpDADSRVdaiveefafdpdddpflLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYR---E 168
Cdd:cd03233 98 LTVRETLDFALRCKG----NEFVRG-----------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSStalE 156
|
170
....*....|....*....
gi 496664120 169 CVKVMDIIRRIhERGTTVV 187
Cdd:cd03233 157 ILKCIRTMADV-LKTTTFV 174
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-50 |
8.05e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 8.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 496664120 2 IEFRDVHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNG 50
Cdd:PRK10938 261 IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-213 |
8.19e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.97 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGS-APILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 81 LFQNP-----------DSQICCNTVREELLFGFKALGLDGPDADSRVDAIVEEFAFDpdddpflLNRGARQLLALASIVV 149
Cdd:cd03288 100 ILQDPilfsgsirfnlDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN-------FSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664120 150 LAPPVVVLDEPTTGLDY-RECVKVMDIIRRIHERgtTVVMVCHDMEVVADyAARCIVMSGGEVVD 213
Cdd:cd03288 173 RKSSILIMDEATASIDMaTENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-85 |
9.92e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASY-DGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGF 80
Cdd:PTZ00243 1309 LVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
....*
gi 496664120 81 LFQNP 85
Cdd:PTZ00243 1389 IPQDP 1393
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-191 |
1.07e-04 |
|
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: 41.76 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVlidGVPTSdlrtselaRRVGFL 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEG--------EDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsQICCNTVREELLFgfkalgldgpdadsrvdaiveefafdPDDDpfLLNRGARQLLALASIVVLAPPVVVLDEPT 161
Cdd:cd03223 70 PQRP--YLPLGTLREQLIY--------------------------PWDD--VLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 496664120 162 TGLDYRECVKVMDIIRrihERGTTVVMVCH 191
Cdd:cd03223 120 SALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-62 |
1.12e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLID 62
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
158-199 |
1.61e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.61e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 496664120 158 DEPTTGL---DYRecvKVMDIIRRIHERGTTVVMVCHDMEVV--ADY 199
Cdd:COG0178 854 DEPTTGLhfhDIR---KLLEVLHRLVDKGNTVVVIEHNLDVIktADW 897
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-213 |
1.62e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 16 PILKGVSFTIRDGEFVAFVGTNGAGKSTT----MRLmngLLKPDA----GQVLIDGvpTSDLRTSELARR------VGFL 81
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRL---LPSPPVvypsGDIRFHG--ESLLHASEQTLRgvrgnkIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 82 FQNPdsQICCNTVR--EELLFGFKAL--GLDGPDADSRVDAIVEEF-----AFDPDDDPFLLNRGARQLLALASIVVLAP 152
Cdd:PRK15134 98 FQEP--MVSLNPLHtlEKQLYEVLSLhrGMRREAARGEILNCLDRVgirqaAKRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 153 PVVVLDEPTTGLDYRECVKVMDIIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVD 213
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
158-227 |
2.15e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVV--ADYaarcIV-------MSGGEVVDDAPTFDVLRNRETL 227
Cdd:TIGR00630 515 DEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIraADY----VIdigpgagEHGGEVVASGTPEEILANPDSL 589
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-225 |
2.26e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 18 LKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGvptsdlRTSELARRVGFlfqnpDSQIccnTVREE 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGL-----SGQL---TGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 98 LLFGFKALGLDGPDADSRVDAIVE-----EFAFDPDDDpflLNRGARQLLALASIVVLAPPVVVLDEPTTGLDYRECVKV 172
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEfselgEFIYQPVKK---YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496664120 173 MDIIRRIHERGTTVVMVCHDMEVVADYAARCIVMSGGEVVDDAPTFDVLRNRE 225
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
158-212 |
3.11e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 3.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664120 158 DEPTTGL---DYRecvKVMDIIRRIHERGTTVVMVCHDMEVV--ADYaarcIV-------MSGGEVV 212
Cdd:PRK00349 858 DEPTTGLhfeDIR---KLLEVLHRLVDKGNTVVVIEHNLDVIktADW----IIdlgpeggDGGGEIV 917
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-87 |
4.02e-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: 4.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 28 GEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQVLIDGVPTSDLRTSELARRVGFLFQNPDS 87
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
31-143 |
4.31e-04 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 41.12 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 31 VAFVGTNGAGKSTTMRLMN-GLLKPDAGQVLIDgvPTSDL--RTSELARRVG-----FLFQNPDSQICCNtvreelLFGF 102
Cdd:COG3505 2 VLVIGPTGSGKTVGLVIPNlTQLARGESVVVTD--PKGDLaeLTAGFRRRAGydvyvFDPFDPERSHRWN------PLDE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 496664120 103 KAlglDGPDADSRVDAIVEEFAFDPDDDPFLLNRgARQLLA 143
Cdd:COG3505 74 IR---DPADAQELAEALIPALGGGGGGDPFWREA-ARALLA 110
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-58 |
6.74e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 6.74e-04
10 20 30
....*....|....*....|....*....|....*..
gi 496664120 22 SFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQ 58
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE 59
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-227 |
7.67e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDG--SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKP-DAGQVLIDGvptsdlrTSELARRV 78
Cdd:PLN03232 615 ISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG-------SVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 79 GFLFQnpdsqiccNTVREELLFGFKAlgldgpdADSRVDAIVEEFAFDPDDDPFL-------------LNRGARQLLALA 145
Cdd:PLN03232 688 SWIFN--------ATVRENILFGSDF-------ESERYWRAIDVTALQHDLDLLPgrdlteigergvnISGGQKQRVSMA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 146 SIVVLAPPVVVLDEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVAdYAARCIVMSGGEVVDDApTFDVLRNRE 225
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEG-TFAELSKSG 830
|
..
gi 496664120 226 TL 227
Cdd:PLN03232 831 SL 832
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
158-212 |
9.92e-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: 9.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVV--ADYaarcIV-------MSGGEVV 212
Cdd:cd03270 164 DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIraADH----VIdigpgagVHGGEIV 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-59 |
2.67e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 496664120 13 GSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV 59
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
158-227 |
2.81e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664120 158 DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVV--ADYaarcIV-------MSGGEVVDDAPTFDVLRNRETL 227
Cdd:COG0178 512 DEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIraADY----IIdigpgagEHGGEVVAQGTPEEILKNPDSL 586
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-59 |
5.41e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 5.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 496664120 7 VHASYdGSAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDAGQV 59
Cdd:PRK10636 318 VSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-101 |
5.64e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.18 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 2 IEFRDVHASYDGSA--PILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLMNGLLKPDA-GQVLIDGvptsdlrtselarRV 78
Cdd:PLN03130 615 ISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG-------------TV 681
|
90 100
....*....|....*....|...
gi 496664120 79 GFLFQNpdSQICCNTVREELLFG 101
Cdd:PLN03130 682 AYVPQV--SWIFNATVRDNILFG 702
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-48 |
5.90e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.09 E-value: 5.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 496664120 2 IEFRDVHASYDG--SAPILKGVSFTIRDGEFVAFVGTNGAGKSTTMRLM 48
Cdd:PTZ00265 1166 IEIMDVNFRYISrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL 1214
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
134-201 |
8.14e-03 |
|
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: 36.18 E-value: 8.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496664120 134 LNRGARQLLALASIVVLAPPVVVL----DEPTTGLDYRECVKVMDIIRRIHERGTTVVMVCHDMEVVADYAA 201
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPlyilDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADK 149
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-223 |
9.70e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 37.16 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 32 AFVGTNGAGKSTTMRLMNGLLKPDAG------QVLIDGVPTSDLRTSElaRRVGFLFQnpDSQICCN-TVREELLFGFKa 104
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICLPPEK--RRIGYVFQ--DARLFPHyKVRGNLRYGMA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664120 105 lgldgPDADSRVDAIVEEFAFDPdddpfLLNR-------GARQLLALASIVVLAPPVVVLDEPTTGLDY---REcvkVMD 174
Cdd:PRK11144 103 -----KSMVAQFDKIVALLGIEP-----LLDRypgslsgGEKQRVAIGRALLTAPELLLMDEPLASLDLprkRE---LLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496664120 175 IIRRI-HERGTTVVMVCHDMEVVADYAARCIVMSGGEVVddapTFDVLRN 223
Cdd:PRK11144 170 YLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVK----AFGPLEE 215
|
|
| |
