|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
23-275 |
8.13e-138 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 388.26 E-value: 8.13e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 23 KVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQM 102
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV---DG--QDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:COG3638 76 RRLRRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLN 261
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
250
....*....|....
gi 490526215 262 DTIIQDIYSDESPE 275
Cdd:COG3638 236 DAVLREIYGGEAEE 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
25-269 |
7.08e-111 |
|
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: 319.90 E-value: 7.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRK 104
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-----DGTDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLNDT 263
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
....*.
gi 490526215 264 IIQDIY 269
Cdd:cd03256 236 VLDEIY 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-269 |
4.46e-107 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 310.38 E-value: 4.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHdngetQNIAALTTKQMR 103
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEG-----TDITKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLND 262
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
....*..
gi 490526215 263 TIIQDIY 269
Cdd:TIGR02315 236 EVLRHIY 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
22-252 |
1.72e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 209.13 E-value: 1.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKS---QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAALT 98
Cdd:COG1136 2 SPLLELRNLTKSYGTgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL-IDG----QDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 TKQMRKWRAQ-CGMIFQDFCLVPRLDVMTNVLLGRLsytstlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGG 177
Cdd:COG1136 77 ERELARLRRRhIGFVFQFFNLLPELTALENVALPLL--------LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLvKDYCTRVIGIAHGRII 252
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPEL-AARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
25-251 |
1.56e-66 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 206.19 E-value: 1.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR---VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQ 101
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV-----DGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRA-QCGMIFQDFCLVPRLDVMTNVLLGRLsytstlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:cd03255 76 LAAFRRrHIGFVFQSFNLLPDLTALENVELPLL--------LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKdYCTRVIGIAHGRI 251
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-269 |
9.23e-63 |
|
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: 197.96 E-value: 9.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetQNIAALTTKQMR 103
Cdd:COG1120 1 MLEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV--LLDG---RDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAqcgMIFQDFCLVPRLDVMTNVLLGRLSYTStlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:COG1120 75 RRIA---YVPQEPPAPFGLTVRELVALGRYPHLG----LFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS-MLN 261
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEeVLT 227
|
....*...
gi 490526215 262 DTIIQDIY 269
Cdd:COG1120 228 PELLEEVY 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-269 |
1.13e-61 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 195.62 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKsQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTI-----PSSAGEIInyhdnGETQNIAA 96
Cdd:PRK09984 2 QTIIRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSHIELL-----GRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQMRKWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:PRK09984 76 RLARDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
250
....*....|....
gi 490526215 256 HPSMLNDTIIQDIY 269
Cdd:PRK09984 236 SSQQFDNERFDHLY 249
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-256 |
8.81e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.80 E-value: 8.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQMR 103
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV---NG--QDLSRLKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLLG-RLSYTStlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYENVALPlRVTGKS---------RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGH 256
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
25-278 |
3.11e-59 |
|
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: 187.92 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYhdNGETqniaaLTTKQMRK 104
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL-V--DGKD-----ITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQD-----FCLVPRLDVM---TNvlLGrLSytstlksffkifADQDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:COG1122 73 LRRKVGLVFQNpddqlFAPTVEEDVAfgpEN--LG-LP------------REEIRERVEEALELVGLEHLADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGH 256
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
250 260
....*....|....*....|..
gi 490526215 257 PsmlndtiiQDIYSDEspELLH 278
Cdd:COG1122 218 P--------REVFSDY--ELLE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-255 |
6.57e-57 |
|
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: 190.11 E-value: 6.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 11 ADYPAVVLESRKKVLSVKGLVKAY----KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYH 86
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL-FD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 87 DngetQNIAALTTKQMRKWRAQCGMIFQD--FCLVPRLDVMTNVLLGrlsytstLKSFFKIFADQDRARAIELLQWLNML 164
Cdd:COG1123 326 G----KDLTKLSRRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEP-------LRLHGLLSRAERRERVAELLERVGLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 165 PHALQR--AEnLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCT 241
Cdd:COG1123 395 PDLADRypHE-LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrELGLTYLFISHDLAVVRYIAD 473
|
250
....*....|....
gi 490526215 242 RVIGIAHGRIIFDG 255
Cdd:COG1123 474 RVAVMYDGRIVEDG 487
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
25-269 |
1.51e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.42 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaalTTKQMR 103
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGED----------VARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLLgrlsytstLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:COG1131 70 EVRRRIGYVPQEPALYPDLTVRENLRF--------FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLNDT 263
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
....*.
gi 490526215 264 IIQDIY 269
Cdd:COG1131 222 LLEDVF 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-258 |
2.37e-54 |
|
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: 175.70 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGEtqniaALTTKQMRK 104
Cdd:cd03219 1 LEVRGLTKRFGG-LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV---LFDGE-----DITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wRAQCGMI--FQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQD--RARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:cd03219 72 -IARLGIGrtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-251 |
4.08e-54 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 174.64 E-value: 4.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIaalTTKQMRK 104
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII---DGLKLTD---DKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03262 74 LRQKVGMVFQQFNLFPHLTVLENITLA-------PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-278 |
1.68e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 173.74 E-value: 1.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 23 KVLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqNIAALTTKQM 102
Cdd:COG1121 5 PAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV----------RLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKWRA---QCGMIFQDFCL-VprLDVmtnVLLGRLSYtstlKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQ 178
Cdd:COG1121 74 RRRIGyvpQRAEVDWDFPItV--RDV---VLMGRYGR----RGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAhGRIIFDGHPS 258
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPE 223
|
250 260
....*....|....*....|.
gi 490526215 259 -MLNDTIIQDIYSDESPELLH 278
Cdd:COG1121 224 eVLTPENLSRAYGGPVALLAH 244
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
24-260 |
2.24e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 173.26 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAAlTTKQMR 103
Cdd:COG1126 1 MIEIENLHKSFGDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT-VDG----EDLTD-SKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLLGRLsytsTLKsffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:COG1126 74 KLRRKVGMVFQQFNLFPHLTVLENVTLAPI----KVK---KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSML 260
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-252 |
1.63e-52 |
|
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: 170.76 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAY---KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAALTTK 100
Cdd:cd03257 1 LLEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII-FDG----KDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QMRKWRAQCGMIFQD--FCLVPRLDVMTNVllgrlsyTSTLKSFFKIFADQDRARAIELL--------QWLNMLPHALqr 170
Cdd:cd03257 76 LRKIRRKEIQMVFQDpmSSLNPRMTIGEQI-------AEPLRIHGKLSKKEARKEAVLLLlvgvglpeEVLNRYPHEL-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 aenlSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHG 249
Cdd:cd03257 147 ----SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
...
gi 490526215 250 RII 252
Cdd:cd03257 223 KIV 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-252 |
9.68e-52 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 168.91 E-value: 9.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHR---VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTK 100
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-----DGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QMRKWRAQCGMIFQDFCLVPRLDVMTNVLLgrlsytsTLKSFFKIFADQDRaRAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVAL-------PLEIAGVPKAEIEE-RVLELLELVGLEDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
20-263 |
9.28e-51 |
|
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: 166.69 E-value: 9.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAALTT 99
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL-VDG----QDITGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKWRAQCGMIFQDFCLvprLDVMT---NVLLGrlsytstLKSFFKIFADQDRARAIELLQWLNmLPHALQR--AEnL 174
Cdd:COG1127 75 KELYELRRRIGMLFQGGAL---FDSLTvfeNVAFP-------LREHTDLSEAEIRELVLEKLELVG-LPGAADKmpSE-L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIF 253
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|
gi 490526215 254 DGHPSMLNDT 263
Cdd:COG1127 223 EGTPEELLAS 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
26-250 |
2.31e-50 |
|
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: 164.56 E-value: 2.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGEtqniaaLTTKQMRK 104
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV--LVDGKD------LTKLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQD-----FCLVPRLDVMTNVLLGRLSytstlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQM 179
Cdd:cd03225 73 LRRKVGLVFQNpddqfFGPTVEEEVAFGLENLGLP------------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 180 QRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
25-255 |
4.59e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 167.95 E-value: 4.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKS---QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQ 101
Cdd:COG1135 2 IELENLSKTFPTkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV---DG--VDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQCGMIFQDFCLVPRLDVMTNVLLG-RLSYTStlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:COG1135 77 LRAARRKIGMIFQHFNLLSSRTVAENVALPlEIAGVP---------KAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIseND---IAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelgLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
24-272 |
9.46e-50 |
|
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: 164.26 E-value: 9.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaalTTKQM 102
Cdd:COG4555 1 MIEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlIDGED----------VRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKWRAQCGMIFQDFCLVPRLDVMTNvllgrLSYTSTLksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:COG4555 70 REARRQIGVLPDERGLYDRLTVREN-----IRYFAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSM--- 259
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDElre 221
|
250
....*....|....*....
gi 490526215 260 ------LNDTIIQDIYSDE 272
Cdd:COG4555 222 eigeenLEDAFVALIGSEE 240
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-257 |
6.93e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 162.52 E-value: 6.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAALTTKQmr 103
Cdd:COG0411 4 LLEVRGLTKRFGG-LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDG----RDITGLPPHR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwRAQCGMI--FQDFCLVPRLDVMTNVLLGRL-----SYTSTLKSFFKIFADQD--RARAIELLQWLNMLPHALQRAENL 174
Cdd:COG0411 76 --IARLGIArtFQNPRLFPELTVLENVLVAAHarlgrGLLAALLRLPRARREEReaRERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIF 253
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
....
gi 490526215 254 DGHP 257
Cdd:COG0411 234 EGTP 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
25-250 |
8.52e-49 |
|
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: 159.66 E-value: 8.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKsQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIaalTTKQMRK 104
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI---DGEDLTD---LEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstlksffkifadqdraraiellqwlnmlphalqraenLSGGQMQRVAI 184
Cdd:cd03229 74 LRRRIGMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-255 |
1.70e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.95 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLN-GTIPSSaGE--IINYHDNGETQNiaalTTKQ 101
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNlLEMPRS-GTlnIAGNHFDFSKTP----SDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQCGMIFQDFCLVPRLDVMTNVL------LGrLSytstlksffkifADQDRARAIELLQWLNMLPHALQRAENLS 175
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPHLTVQQNLIeapcrvLG-LS------------KDQALARAEKLLERLRLKPYADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
25-251 |
2.21e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.90 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNgetqniaALTTKQMRK 104
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-LDGK-------PLSAMPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPrlD-VMTNvllgrLSYTSTLKSffkifADQDRARAIELLQWLNMLPHALQR-AENLSGGQMQRV 182
Cdd:COG4619 72 WRRQVAYVPQEPALWG--GtVRDN-----LPFPFQLRE-----RKFDRERALELLERLGLPPDILDKpVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
31-251 |
8.89e-47 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 155.64 E-value: 8.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQMRKWRAQCG 110
Cdd:cd03292 7 TKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV---NG--QDVSDLRGRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 111 MIFQDFCLVPRLDVMTNVLLG-RLSYTStlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMM 189
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFAlEVTGVP---------PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 190 QNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-227 |
2.65e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.02 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYKS---QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqniaa 96
Cdd:COG1116 3 AAAPALELRGVSKRFPTgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQMRKWRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKsFFKIFADQDRARAIELLQ------WLNMLPHAlqr 170
Cdd:COG1116 70 VDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALG-------LE-LRGVPKAERRERARELLElvglagFEDAYPHQ--- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 171 aenLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVV 227
Cdd:COG1116 139 ---LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVL 193
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-255 |
2.97e-46 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 154.23 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqNIAALTTKQMRKW 105
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI----------RVFGKPLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RA---QCGMIFQDFCLvprlDVMTNVLLGRLSYtstlKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:cd03235 70 IGyvpQRRSIDRDFPI----SVRDVVLMGLYGH----KGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHgRIIFDG 255
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-252 |
3.20e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.17 E-value: 3.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLN-GTIPSSaGE--IINYHDNGETQniaaLTTKQ 101
Cdd:COG4161 3 IQLKNINCFYGS-HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlLETPDS-GQlnIAGHQFDFSQK----PSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSffkifadQDRARAIELLQWLNMLPHALQRAENLSGGQMQR 181
Cdd:COG4161 77 IRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKE-------QAREKAMKLLARLRLTDKADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
26-255 |
3.29e-46 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 152.97 E-value: 3.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKsQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGetQNIAALTTKQMRKW 105
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---LLDG--KDLASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAqcgmifqdfcLVPrldvmtnvllgrlsytstlksffkifadQdrarAIELLqwlNMLPHALQRAENLSGGQMQRVAIC 185
Cdd:cd03214 75 IA----------YVP----------------------------Q----ALELL---GLAHLADRPFNELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 186 RAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-257 |
9.57e-46 |
|
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: 153.81 E-value: 9.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRK 104
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-----DGEDISGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03261 75 LRRRMGMLFQSGALFDSLTVFENVAFP-------LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMN---TLQKisENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDlirSLKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-252 |
1.28e-45 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 153.81 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR---VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGEtqniaALTTKQ 101
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEV---TFDGR-----PVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQCGMIFQDfclvPRLDV---MTnvlLGRlsytsTLKSFFKIFA-DQDRARAIELLQ-------WLNMLPHALqr 170
Cdd:COG1124 74 RKAFRRRVQMVFQD----PYASLhprHT---VDR-----ILAEPLRIHGlPDREERIAELLEqvglppsFLDRYPHQL-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 aenlSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHG 249
Cdd:COG1124 140 ----SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
...
gi 490526215 250 RII 252
Cdd:COG1124 216 RIV 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-260 |
1.21e-44 |
|
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: 158.38 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqnIAALTTKQmr 103
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVD------LSDLDPAS-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kWRAQCGMIFQDfclvPRL---DVMTNVLLGRLSYTstlksffkifaDQDRARAIE---LLQWLNMLPHALQ-----RAE 172
Cdd:COG4988 409 -WRRQIAWVPQN----PYLfagTIRENLRLGRPDAS-----------DEELEAALEaagLDEFVAALPDGLDtplgeGGR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVKDyCTRVIGIAHGRII 252
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLALLAQ-ADRILVLDDGRIV 550
|
....*...
gi 490526215 253 FDGHPSML 260
Cdd:COG4988 551 EQGTHEEL 558
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
32-250 |
2.33e-44 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 149.32 E-value: 2.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 32 KAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQMRKWRAQCGM 111
Cdd:TIGR02673 9 KAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI---AG--EDVNRLRGRQLPLLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 112 IFQDFCLVPRLDVMTNVLLG-RLSYTSTLKSffkifadqdRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQ 190
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENVALPlEVRGKKEREI---------QRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 191 NPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
28-263 |
1.42e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 148.32 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 28 KGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIAALTTKQMRKwra 107
Cdd:PRK09493 5 KNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV---DGLKVNDPKVDERLIRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 108 QCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSffkifadQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRA 187
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKE-------EAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 188 MMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLNDT 263
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
25-233 |
2.54e-43 |
|
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: 146.85 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKS---QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqniaalttkQ 101
Cdd:cd03293 1 LEVRNVSKTYGGgggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV---DGE----------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKsFFKIFADQDRARAIELLQWLNmlphaLQRAEN-----LSG 176
Cdd:cd03293 68 VTGPGPDRGYVFQQDALLPWLTVLDNVALG-------LE-LQGVPKAEARERAEELLELVG-----LSGFENayphqLSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSV 233
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDI 192
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-257 |
3.36e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.91 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQ-HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSA---GEIinyHDNGetQNIAALTT 99
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEV---LLDG--RDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKwraQCGMIFQD----FCLVPRLDVMTNVLLGRlsytstlksffKIFADQDRARAIELLQWLNMLPHALQRAENLS 175
Cdd:COG1123 79 ALRGR---RIGMVFQDpmtqLNPVTVGDQIAEALENL-----------GLSRAEARARVLELLEAVGLERRLDRYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFD 254
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
...
gi 490526215 255 GHP 257
Cdd:COG1123 225 GPP 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
25-252 |
4.46e-43 |
|
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: 146.13 E-value: 4.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INyhdngeTQNIAALTTKQMR 103
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlID------GRDVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwraqCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFfKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:cd03259 74 -----IGMVFQDYALFPHLTVAENIAFG-------LKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-262 |
1.11e-42 |
|
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: 145.27 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAALTTKQmrk 104
Cdd:cd03224 1 LEVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR-FDG----RDITGLPPHE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wRAQCGMIF--QDFCLVPRLDVMTNVLLGRlsytstlksffKIFADQDRARAIELLqwLNMLPhAL-----QRAENLSGG 177
Cdd:cd03224 72 -RARAGIGYvpEGRRIFPELTVEENLLLGA-----------YARRRAKRKARLERV--YELFP-RLkerrkQLAGTLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
....*
gi 490526215 258 SMLND 262
Cdd:cd03224 217 AELLA 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-244 |
3.38e-41 |
|
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: 144.43 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQH---RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPS---SAGEIInYHDngetQNIAAL 97
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIL-FDG----EDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 98 TTKQMRKWR-AQCGMIFQDfclvprldvmtnvllgrlSYTS-------------TLKSFFKIFADQDRARAIELLQWLNm 163
Cdd:COG0444 76 SEKELRKIRgREIQMIFQD------------------PMTSlnpvmtvgdqiaePLRIHGGLSKAEARERAIELLERVG- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 164 LPHALQRAEN----LSGGQMQRVAICRAMMQNPKILLADEPVASLDPknTTR--IMNTLQKI-SENDIAVVVNLHSVNLV 236
Cdd:COG0444 137 LPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDV--TIQaqILNLLKDLqRELGLAILFITHDLGVV 214
|
....*...
gi 490526215 237 KDYCTRVI 244
Cdd:COG0444 215 AEIADRVA 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-202 |
3.43e-41 |
|
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: 139.32 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngeTQNIAALTTKQMRKWRAQCGMIFQDFCLVP 120
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI--------LLDGQDLTDDERKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RLDVMTNVLLGRLsytstlksFFKIFADQDRARAIELLQWLNMLP----HALQRAENLSGGQMQRVAICRAMMQNPKILL 196
Cdd:pfam00005 73 RLTVRENLRLGLL--------LKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 490526215 197 ADEPVA 202
Cdd:pfam00005 145 LDEPTA 150
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
37-258 |
5.59e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.59 E-value: 5.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INyhdngeTQNIAALTTKQMRKWRAQCGMIFQ- 114
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVtID------GRDITAKKKKKLKDLRKKVGLVFQf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 ------------DFCLVPRldvmtNvllgrlsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAE-NLSGGQMQR 181
Cdd:TIGR04521 91 pehqlfeetvykDIAFGPK-----N---------------LGLSEEEAEERVKEALELVGLDEEYLERSPfELSGGQMRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPR 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
28-256 |
8.88e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 143.79 E-value: 8.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 28 KGLVKAYKSQHR---VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQMRK 104
Cdd:PRK11153 5 KNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV---DG--QDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLG-RLSYTStlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPlELAGTP---------KAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGH 256
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
27-246 |
2.42e-40 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 138.90 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQMRKW- 105
Cdd:TIGR03608 1 LKNISKKFGD-KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL---NG--QETPPLNSKKASKFr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDFCLVPRLDVMTNVLLGrLSYTstlksffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAIC 185
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLG-LKYK-------KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 186 RAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSvNLVKDYCTRVIGI 246
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-255 |
4.02e-40 |
|
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: 138.48 E-value: 4.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFvAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaalTTKQMR 103
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIrIDGQD----------VLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVmtnvlLGRLSYTSTLKsffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:cd03264 69 KLRRRIGYLPQEFGVYPNFTV-----REFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIaVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
25-250 |
4.04e-40 |
|
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: 137.13 E-value: 4.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaaLTTKQM 102
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVD---------LRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKWRAQCGMIFQDFCLvprldvmtnvllgrlsYTSTLksffkifadqdraraiellqwlnmlphalqrAEN-LSGGQMQR 181
Cdd:cd03228 72 ESLRKNIAYVPQDPFL----------------FSGTI-------------------------------RENiLSGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVnLHSVNLVKDyCTRVIGIAHGR 250
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVI-AHRLSTIRD-ADRIIVLDDGR 171
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
37-269 |
6.39e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.10 E-value: 6.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGetQNIAALTTKQMRKWRA----QCGMI 112
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV---RLNG--RPLAAWSPWELARRRAvlpqHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 113 FqDFclvPRLDVmtnVLLGRLSYTSTlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQ-- 190
Cdd:COG4559 88 F-PF---TVEEV---VALGRAPHGSS--------AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 191 -----NPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP-SMLNDTI 264
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPeEVLTDEL 232
|
....*
gi 490526215 265 IQDIY 269
Cdd:COG4559 233 LERVY 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
25-251 |
8.54e-40 |
|
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: 136.37 E-value: 8.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDNGetqniaalttKQMR 103
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkVLGKDIK----------KEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVllgrlsytstlksffkifadqdraraiellqwlnmlphalqraeNLSGGQMQRVA 183
Cdd:cd03230 70 EVKRRIGYLPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-255 |
1.07e-39 |
|
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: 146.52 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetQNIAALTTKQmr 103
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI--LIDG---IDLRQIDPAS-- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kWRAQCGMIFQDfclvPRL---DVMTNVLLGRLSytstlksffkifADQDR----ARAIELLQWLNMLPHALQ-----RA 171
Cdd:COG2274 547 -LRRQIGVVLQD----VFLfsgTIRENITLGDPD------------ATDEEiieaARLAGLHDFIEALPMGYDtvvgeGG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 172 ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVKDyCTRVIGIAHGRI 251
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA-HRLSTIRL-ADRIIVLDKGRI 687
|
....
gi 490526215 252 IFDG 255
Cdd:COG2274 688 VEDG 691
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-260 |
2.16e-39 |
|
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: 144.14 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqnIAALTTKQm 102
Cdd:COG4987 334 LELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItLGGVD------LRDLDEDD- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 rkWRAQCGMIFQDfclvPRL---DVMTNVLLGRLSytstlksffkifADQDRARAI----ELLQWLNMLPHAL-----QR 170
Cdd:COG4987 407 --LRRRIAVVPQR----PHLfdtTLRENLRLARPD------------ATDEELWAAlervGLGDWLAALPDGLdtwlgEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 AENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLvkDYCTRVIGIAHGR 250
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL--ERMDRILVLEDGR 546
|
250
....*....|
gi 490526215 251 IIFDGHPSML 260
Cdd:COG4987 547 IVEQGTHEEL 556
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-250 |
3.97e-39 |
|
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: 133.91 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaaLTTKQMRK 104
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlIDGKD---------IAKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQdfclvprldvmtnvllgrlsytstlksffkifadqdraraiellqwlnmlphalqraenLSGGQMQRVAI 184
Cdd:cd00267 71 LRRRIGYVPQ-----------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
33-252 |
1.31e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 139.53 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 33 AYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-InyhdNGetQNIAALTTKQmrkWRAQCGM 111
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlI----DG--VDIRDLTLES---LRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 112 IFQDFCLVPRlDVMTNVLLGRLSytstlksffkifADQDR----ARAIELLQWLNMLPHAL-----QRAENLSGGQMQRV 182
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYGRPD------------ATDEEveeaAKAAQAHEFIEALPDGYdtvvgERGVNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVnLHSVNLVKDyCTRVIGIAHGRII 252
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI-AHRLSTIRN-ADRILVLDDGRIV 553
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
27-255 |
1.31e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.95 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLN-------GTIPSSAGEIINYHDNGETQNiaaltt 99
Cdd:PRK11264 6 VKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeaGTIRVGDITIDTARSLSQQKG------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 kQMRKWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKsffkifaDQDRARAIELLQWLNMLPHALQRAENLSGGQM 179
Cdd:PRK11264 79 -LIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPK-------EEATARARELLAKVGLAGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 180 QRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-258 |
1.64e-37 |
|
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: 132.17 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 19 ESRKKVLSVKGLVKAYKS-QHRV--LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGetQNIA 95
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTgAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV---RLAG--QDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 96 ALTTKQMRKWRAQC-GMIFQDFCLVPRLDVMTNVLL-----GRlsytstlksffkifaDQDRARAIELLQWLNmLPHALQ 169
Cdd:COG4181 78 ALDEDARARLRARHvGFVFQSFQLLPTLTALENVMLplelaGR---------------RDARARARALLERVG-LGHRLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 170 RAEN-LSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVkDYCTRVIGIA 247
Cdd:COG4181 142 HYPAqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALA-ARCDRVLRLR 220
|
250
....*....|.
gi 490526215 248 HGRIIFDGHPS 258
Cdd:COG4181 221 AGRLVEDTAAT 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-269 |
2.88e-37 |
|
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: 131.64 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDngetQNIAALTTKQmr 103
Cdd:COG0410 3 MLEVENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR-FDG----EDITGLPPHR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwRAQCGMifqdfCLVP-------RLDVMTNVLLGRlsytstlksffkiFADQDRARAIELLQW-LNMLPhAL-----QR 170
Cdd:COG0410 75 --IARLGI-----GYVPegrrifpSLTVEENLLLGA-------------YARRDRAEVRADLERvYELFP-RLkerrrQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 AENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
250 260
....*....|....*....|
gi 490526215 251 IIFDGHPS-MLNDTIIQDIY 269
Cdd:COG0410 214 IVLEGTAAeLLADPEVREAY 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
25-207 |
3.94e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INyhdnGetQNIAALTTKQmr 103
Cdd:COG3842 6 LELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlLD----G--RDVTGLPPEK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwRaQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKsFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:COG3842 77 --R-NVGMVFQDYALFPHLTVAENVAFG-------LR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180
....*....|....*....|....
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPK 207
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAK 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-227 |
1.41e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYhdNGETQNIAalTTKQMR 103
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-L--DGEPVRFR--SPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwRAQCGMIFQDFCLVPRLDVMTNVLLGRLsytstLKSFFKIFADQDRARAIELLQWLNM--LPHAlqRAENLSGGQMQR 181
Cdd:COG1129 78 --AAGIAIIHQELNLVPNLSVAENIFLGRE-----PRRGGLIDWRAMRRRARELLARLGLdiDPDT--PVGDLSVAQQQL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVV 227
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-269 |
1.73e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.58 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGetQNIAALTTKQMR 103
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---RLNG--RPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAqcgMIFQDFCLVPRLDVMTNVLLGRLSYTStlksffkifaDQDRARAIellqwlnmLPHALQRAE----------N 173
Cdd:PRK13548 76 RRRA---VLPQHSSLSFPFTVEEVVAMGRAPHGL----------SRAEDDAL--------VAAALAQVDlahlagrdypQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 174 LSGGQMQRVAICRAMMQ------NPKILLADEPVASLDPKNTTRIMNTL-QKISENDIAVVVNLHSVNLVKDYCTRVIGI 246
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVVLHDLNLAARYADRIVLL 214
|
250 260
....*....|....*....|....
gi 490526215 247 AHGRIIFDGHPS-MLNDTIIQDIY 269
Cdd:PRK13548 215 HQGRLVADGTPAeVLTPETLRRVY 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
34-260 |
1.83e-35 |
|
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: 126.96 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 34 YKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetQNIAALTTKQMRKwraQCGMIF 113
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI--LIDG---IDIRDISRKSLRS---MIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 QDFCLVPRlDVMTNVLLGRLSytstlksffkifADQDR----ARAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAI 184
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGRPN------------ATDEEvieaAKEAGAHDFIMKLPNGYDtvlgeNGGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVKDyCTRVIGIAHGRIIFDGHPSML 260
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-260 |
5.78e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.64 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYksQHRVLdNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTTKQmRK 104
Cdd:COG3840 2 LRLDDLTYRY--GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW---NG--QDLTALPPAE-RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraqCGMIFQDFCLVPRLDVMTNVLLG-----RLSytstlksffkifaDQDRARAIELLQWLNmLPHALQRA-ENLSGGQ 178
Cdd:COG3840 73 ----VSMLFQENNLFPHLTVAQNIGLGlrpglKLT-------------AEQRAQVEQALERVG-LAGLLDRLpGQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
...
gi 490526215 258 SML 260
Cdd:COG3840 215 AAL 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-254 |
6.65e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 126.35 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKS----QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNgetQNIAALTTK 100
Cdd:COG1101 2 LELKNLSKTFNPgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL--IDG---KDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QmrkwRAQ-CGMIFQDFCL--VPRLDVMTNVLL-----GRLSYTSTLKSffkifadQDRARAIELLQWLNM-LPHAL-QR 170
Cdd:COG1101 77 K----RAKyIGRVFQDPMMgtAPSMTIEENLALayrrgKRRGLRRGLTK-------KRRELFRELLATLGLgLENRLdTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 AENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMN-TLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHG 249
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
....*
gi 490526215 250 RIIFD 254
Cdd:COG1101 226 RIILD 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-250 |
2.99e-34 |
|
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: 123.70 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHR------VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNGETQNIAAL 97
Cdd:COG4778 4 LLEVENLSKTFTLHLQggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL-VRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 98 TTKQMRKWRAQ-CGMIFQDFCLVPR---LDVMTNVLLGRlsytstlksffKIFADQDRARAIELLQWLNmLPHALQRA-- 171
Cdd:COG4778 83 SPREILALRRRtIGYVSQFLRVIPRvsaLDVVAEPLLER-----------GVDREEARARARELLARLN-LPERLWDLpp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 172 ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-252 |
8.12e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 123.64 E-value: 8.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAY-------KSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIiNYHDngetQNIAA 96
Cdd:PRK10419 4 LNVSGLSHHYahgglsgKHQHQtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV-SWRG----EPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQMRKWRAQCGMIFQD-FCLV-PRLDVmtnvllgRLSYTSTLKSFFKIFADQDRARAIELLQWLNMLP-HALQRAEN 173
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDsISAVnPRKTV-------REIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 174 LSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
25-207 |
8.64e-34 |
|
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: 122.73 E-value: 8.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHdngetQNIAALTTkqmrk 104
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-----KDITNLPP----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLGRlsytsTLKsffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03300 70 HKRPVNTVFQNYALFPHLTVFENIAFGL-----RLK---KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180
....*....|....*....|...
gi 490526215 185 CRAMMQNPKILLADEPVASLDPK 207
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLK 164
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
25-260 |
2.36e-33 |
|
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: 121.07 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKS-QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaalTTKQM 102
Cdd:cd03263 1 LQIRNLTKTYKKgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYS----------IRTDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKWRAQCGMIFQDFCLVPRLDVMTNVLL-GRLsytstlKSFFKifaDQDRARAIELLQWLNMLPHALQRAENLSGGQMQR 181
Cdd:cd03263 71 KAARQSLGYCPQFDALFDELTVREHLRFyARL------KGLPK---SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDiAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSML 260
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-273 |
1.61e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 120.23 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDNGETQNIaalttKQM 102
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtVDGLDTLDEENL-----WEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKwraQCGMIFQD---------------FCL----VPRldvmtnvllgrlsytstlksffkifaDQDRARAIELLQWLNM 163
Cdd:TIGR04520 76 RK---KVGMVFQNpdnqfvgatveddvaFGLenlgVPR--------------------------EEMRKRVDEALKLVGM 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 164 LPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDyCTR 242
Cdd:TIGR04520 127 EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADR 205
|
250 260 270
....*....|....*....|....*....|.
gi 490526215 243 VIGIAHGRIIFDGHPsmlndtiiQDIYSDES 273
Cdd:TIGR04520 206 VIVMNKGKIVAEGTP--------REIFSQVE 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
25-252 |
1.79e-32 |
|
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: 118.82 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKsQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEiinyHDNGET----QNIAALTTK 100
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA----PDEGEVlldgKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QMRkWRAQCGMIFQDFCLVPrLDVMTNVLLGrlsytstlksfFKIFADQDRARAIELLQWlnmlphALQRAE-------- 172
Cdd:cd03260 76 VLE-LRRRVGMVFQKPNPFP-GSIYDNVAYG-----------LRLHGIKLKEELDERVEE------ALRKAAlwdevkdr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 ----NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISeNDIAVVVNLHSVNLVKDYCTRVIGIAH 248
Cdd:cd03260 137 lhalGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARVADRTAFLLN 215
|
....
gi 490526215 249 GRII 252
Cdd:cd03260 216 GRLV 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-205 |
1.80e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 121.38 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAY---------KSQH-RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYhdng 89
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrTVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL-F---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 90 ETQNIAALTTKQMRKWRAQCGMIFQD--FCLVPRLDVMTNVLLGrlsytstlksfFKIFADQDRA----RAIELLQWLNM 163
Cdd:COG4608 78 DGQDITGLSGRELRPLRRRMQMVFQDpyASLNPRMTVGDIIAEP-----------LRIHGLASKAerreRVAELLELVGL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490526215 164 LPHALQR-AENLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:COG4608 147 RPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-260 |
2.41e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 119.69 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLN-------GTIPSSAGEIINYHDNGETQNIAal 97
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpseGSIVVNGQTINLVRDKDGQLKVA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 98 TTKQMRKWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSffkifadQDRARAIELLQWLNMLPHALQR-AENLSG 176
Cdd:PRK10619 83 DKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQ-------EARERAVKYLAKVGIDERAQGKyPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGH 256
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
....
gi 490526215 257 PSML 260
Cdd:PRK10619 236 PEQL 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
25-207 |
2.45e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 121.72 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetQNIAALTTKQmRK 104
Cdd:COG3839 4 LELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI--LIGG---RDVTDLPPKD-RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraqCGMIFQDFCLVPRLDVMTNVLLGrLSYTSTLKsffkifADQDR--ARAIELLQwlnmLPHALQR-AENLSGGQMQR 181
Cdd:COG3839 77 ----IAMVFQSYALYPHMTVYENIAFP-LKLRKVPK------AEIDRrvREAAELLG----LEDLLDRkPKQLSGGQRQR 141
|
170 180
....*....|....*....|....*.
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPK 207
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
43-206 |
2.58e-32 |
|
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: 119.67 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRKWRAQ-CGMIFQDFCLVPR 121
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-----DGQDIAAMSRKELRELRRKkISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 122 LDVMTNVLLGrLSYTStlksffkIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPV 201
Cdd:cd03294 117 RTVLENVAFG-LEVQG-------VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
....*
gi 490526215 202 ASLDP 206
Cdd:cd03294 189 SALDP 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-205 |
2.72e-32 |
|
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: 124.41 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 14 PAVVLESRKKVLSVKGLVKAY----------KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSaGEII 83
Cdd:COG4172 265 PRPVPPDAPPLLEARDLKVWFpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 84 nYHDngetQNIAALTTKQMRKWRAQCGMIFQD-F-CLVPRLDVMTNVLLGRLSYTSTLKsffkifADQDRARAIELLQWL 161
Cdd:COG4172 344 -FDG----QDLDGLSRRALRPLRRRMQVVFQDpFgSLSPRMTVGQIIAEGLRVHGPGLS------AAERRARVAEALEEV 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490526215 162 NMLPHALQR--AEnLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:COG4172 413 GLDPAARHRypHE-FSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
25-254 |
3.04e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 124.84 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKS---QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEiinYHDNGetQNIAALTTKQ 101
Cdd:PRK10535 5 LELKDIRRSYPSgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT---YRVAG--QDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQ-CGMIFQDFCLVPRLDVMTNVLLGRLsYTSTLKSffkifadQDRARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:PRK10535 80 LAQLRREhFGFIFQRYHLLSHLTAAQNVEVPAV-YAGLERK-------QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSvNLVKDYCTRVIGIAHGRIIFD 254
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRN 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
41-271 |
6.47e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.16 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAG--EIINYHDNGETQNiaalttKQMRKWRAQCGMIFQdfcl 118
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtiTIAGYHITPETGN------KNLKKLRKKVSLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRLDVMTNVLLGRLSYTStlksffKIFADQDRARAIELLQWLNMLPHALQRAE----NLSGGQMQRVAICRAMMQNPKI 194
Cdd:PRK13641 93 FPEAQLFENTVLKDVEFGP------KNFGFSEDEAKEKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPsmlndtiiQDIYSD 271
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP--------KEIFSD 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-272 |
6.62e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 6.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETqniAALTTKQMR 103
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI---KGEP---IKYDKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQ---DFCLVPRldVMTNVLLGRLSytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:PRK13639 75 EVRKTVGIVFQnpdDQLFAPT--VEEDVAFGPLN--------LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSml 260
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK-- 222
|
250
....*....|..
gi 490526215 261 ndtiiqDIYSDE 272
Cdd:PRK13639 223 ------EVFSDI 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-269 |
7.49e-32 |
|
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: 117.64 E-value: 7.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaaLTTKQMR 103
Cdd:cd03218 1 LRAENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlLDGQD---------ITKLPMH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KwRAQCGMIF--QDFCLVPRLDVMTNVLLgrlsytstLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQR 181
Cdd:cd03218 71 K-RARLGIGYlpQEASIFRKLTVEENILA--------VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS-ML 260
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEeIA 221
|
....*....
gi 490526215 261 NDTIIQDIY 269
Cdd:cd03218 222 ANELVRKVY 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-275 |
1.58e-31 |
|
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: 116.67 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrvLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqNIAALTTKQMRK 104
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL---NGK--DITNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraqcGMIFQDFCLVPRLDVMTNvllgrLSYTSTLKSFFKIfadQDRARAIELLQWLNmLPHALQR-AENLSGGQMQRVA 183
Cdd:cd03299 74 -----SYVPQNYALFPHMTVYKN-----IAYGLKKRKVDKK---EIERKVLEIAEMLG-IDHLLNRkPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPsmlnd 262
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP----- 214
|
250
....*....|...
gi 490526215 263 tiiQDIYSDESPE 275
Cdd:cd03299 215 ---EEVFKKPKNE 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-257 |
2.48e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 119.95 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGEtqNIAALTTKQMRK 104
Cdd:PRK09536 4 IDVSDLSVEFGDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV---LVAGD--DVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraQCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:PRK09536 78 ---RVASVPQDTSLSFEFDVRQVVEMGRTPHRSR----FDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
24-228 |
2.60e-31 |
|
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: 115.27 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEiINYHDNGETQNIAAlttkqmr 103
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-VLWNGEPIRDARED------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kWRAQCGMIFQDFCLVPRLDVMTNvllgrlsytstLKSFFKIF-ADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:COG4133 73 -YRRRLAYLGHADGLKPELTVREN-----------LRFWAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV 228
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-254 |
2.64e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 116.70 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdNGETQNIAAlttkqmrk 104
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL----AGTAPLAEA-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFFkifadqdRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:PRK11247 80 -REDTRLMFQDARLLPWKKVIDNVGLG-------LKGQW-------RDAALQALAAVGLADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 185 CRAMMQNPKILLADEPVASLDPknTTRImnTLQKISEN-----DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFD 254
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDA--LTRI--EMQDLIESlwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-205 |
2.84e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.89 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAY---KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngeTQNIAALTTKQ 101
Cdd:COG4525 4 LTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI--------TLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 mrkwrAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKsFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQR 181
Cdd:COG4525 76 -----ADRGVVFQKDALLPWLNVLDNVAFG-------LR-LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180
....*....|....*....|....
gi 490526215 182 VAICRAMMQNPKILLADEPVASLD 205
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALD 166
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
24-258 |
3.57e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 116.44 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLN-------GTIpSSAGEIINYHDNGETQNIAA 96
Cdd:COG4598 8 ALEVRDLHKSFGD-LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINlletpdsGEI-RVGGEEIRLKPDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 lTTKQMRKWRAQCGMIFQDFCLVPRLDVMTNVLLGRLSytstlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:COG4598 86 -DRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVH-------VLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGH 256
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
..
gi 490526215 257 PS 258
Cdd:COG4598 238 PA 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-258 |
4.73e-31 |
|
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: 120.68 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGT--IPSSAGEIInYHD--------------- 87
Cdd:TIGR03269 1 IEVKNLTKKFDGK-EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRII-YHValcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 88 -------NGETQNIAA----LTTKQMRKWRAQCGMIFQ-DFCLVPRLDVMTNVL--LGRLSYTstlksffkifADQDRAR 153
Cdd:TIGR03269 79 gepcpvcGGTLEPEEVdfwnLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLeaLEEIGYE----------GKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 154 AIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQK-ISENDIAVVVNLHS 232
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*.
gi 490526215 233 VNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPD 254
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-237 |
8.19e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.91 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAY---KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIAA 96
Cdd:PRK11629 1 MNKILLQCDNLCKRYqegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIF---NGQPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQMRKWRaQCGMIFQDFCLVPRLDVMTNVLLGRLsytstlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:PRK11629 78 SAAKAELRNQ-KLGFIYQFHHLLPDFTALENVAMPLL--------IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVK 237
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAK 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-263 |
8.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.72 E-value: 8.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYKSQH----RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEII----NYHDNGETQNIAALT 98
Cdd:PRK13651 5 VKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkDEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 T------------KQMRKWRAQCGMIFQ--DFCLVPRlDVMTNVLLGRLSYTSTlksffKIFADQDRARAIELLQwlnmL 164
Cdd:PRK13651 85 EklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVS-----KEEAKKRAAKYIELVG----L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 165 PHA-LQRAE-NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTR 242
Cdd:PRK13651 155 DESyLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
250 260
....*....|....*....|..
gi 490526215 243 VIGIAHGRIIFDGHP-SMLNDT 263
Cdd:PRK13651 235 TIFFKDGKIIKDGDTyDILSDN 256
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
25-206 |
9.69e-31 |
|
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: 114.71 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqNIAALTTKQMRK 104
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI---DGE--DIREQDPVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraQCGMIFQDFCLVPRLDVMTNVllgrlsytSTLKSFFKIFADQDRARAIELLQWLNMLP-HALQR-AENLSGGQMQRV 182
Cdd:cd03295 76 ---KIGYVIQQIGLFPHMTVEENI--------ALVPKLLKWPKEKIRERADELLALVGLDPaEFADRyPHELSGGQQQRV 144
|
170 180
....*....|....*....|....
gi 490526215 183 AICRAMMQNPKILLADEPVASLDP 206
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDP 168
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-252 |
1.11e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.52 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETQNIAALttkqMRK 104
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---LVDGKEVSFASP----RDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQdfclvprldvmtnvllgrlsytstlksffkifadqdraraiellqwlnmlphalqraenLSGGQMQRVAI 184
Cdd:cd03216 73 RRAGIAMVYQ-----------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-252 |
1.30e-30 |
|
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: 113.51 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNgetqNIAAlttkqmRKW 105
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-LNGK----PIKA------KER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDfclvprldvmtnvlLGRLSYTSTLKSFFKIFADQ---DRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:cd03226 70 RKSIGYVMQD--------------VDYQLFTDSVREELLLGLKEldaGNEQAETVLKDLDLYALKERHPLSLSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
25-255 |
1.58e-30 |
|
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: 113.53 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKsQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETQNIAAlttkqmrk 104
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV---LFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wRAQCGMIFQDFCLVPRLDVMTNvllgrLSYTSTLKSFFKIFAdqdRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03269 69 -RNRIGYLPEERGLYPKMKVIDQ-----LVYLAQLKGLKKEEA---RRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
39-264 |
2.86e-30 |
|
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: 115.18 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGE-IINYHDngetqniaalTTKQMRKWRAQCGMIFQDFC 117
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTaRVAGYD----------VVREPRKVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 LVPRLDVMTNVLL-GRLsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILL 196
Cdd:TIGR01188 77 VDEDLTGRENLEMmGRL---------YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 197 ADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLNDTI 264
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRL 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-272 |
3.62e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.45 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQmr 103
Cdd:PRK10895 3 TLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-----DDEDISLLPLHA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLlgrlsytSTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK10895 75 RARRGIGYLPQEASIFRRLSVYDNLM-------AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS-MLND 262
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTeILQD 227
|
250
....*....|
gi 490526215 263 TIIQDIYSDE 272
Cdd:PRK10895 228 EHVKRVYLGE 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-255 |
7.06e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.91 E-value: 7.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYK-SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGETQNIaalttkQMRKW 105
Cdd:cd03245 5 FRNVSFSYPnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV--LLDGTDIRQL------DPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDfclvPRL---DVMTNVLLGRLSYTstlksffkifaDQDRARAIELL---QWLNMLPHALQ-----RAENL 174
Cdd:cd03245 77 RRNIGYVPQD----VTLfygTLRDNITLGAPLAD-----------DERILRAAELAgvtDFVNKHPNGLDlqigeRGRGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVkDYCTRVIGIAHGRIIFD 254
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT-HRPSLL-DLVDRIIVMDSGRIVAD 219
|
.
gi 490526215 255 G 255
Cdd:cd03245 220 G 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-255 |
7.13e-30 |
|
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: 112.00 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIhAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDNGETQNIAALTTKQMRkwraqCGMIFQDFCLVPR 121
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvLNGTVLFDSRKKINLPPQQRK-----IGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 122 LDVMTNVLLGrlsytstLKsffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPV 201
Cdd:cd03297 90 LNVRENLAFG-------LK---RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 202 ASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-258 |
8.16e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.05 E-value: 8.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-InyhdNGETQNI----AALt 98
Cdd:COG3845 5 ALELRGITKRFGG-VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlI----DGKPVRIrsprDAI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 tkqmrkwRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFFKIFADQDRARA--IELLQ--WLNMLPHAlqRAENL 174
Cdd:COG3845 79 -------ALGIGMVHQHFMLVPNLTVAENIVLG-------LEPTKGGRLDRKAARAriRELSEryGLDVDPDA--KVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFD 254
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
....
gi 490526215 255 GHPS 258
Cdd:COG3845 223 VDTA 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-207 |
8.21e-30 |
|
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: 111.58 E-value: 8.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqniaaLTTKQMRK 104
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY-------------IGGRDVTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQ---CGMIFQDFCLVPRLDVMTNvllgrLSYTSTLKSFFKIFADQDRARAIELLQwlnmLPHALQR-AENLSGGQMQ 180
Cdd:cd03301 67 LPPKdrdIAMVFQNYALYPHMTVYDN-----IAFGLKLRKVPKDEIDERVREVAELLQ----IEHLLDRkPKQLSGGQRQ 137
|
170 180
....*....|....*....|....*..
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPK 207
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAK 164
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
44-251 |
1.30e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 114.44 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 44 INFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETQNIAA----LTTKQMRkwraqCGMIFQDFCLV 119
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI---VLNGRTLFDSRkgifLPPEKRR-----IGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTNVLLGRlsytstlksfFKIFADQDRARAIELLQWLNmLPHALQRAEN-LSGGQMQRVAICRAMMQNPKILLAD 198
Cdd:TIGR02142 88 PHLSVRGNLRYGM----------KRARPSERRISFERVIELLG-IGHLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490526215 199 EPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHaEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
34-235 |
1.40e-29 |
|
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: 110.59 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 34 YKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNGETqniaALTTKQMRKWRAQCGMIF 113
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVL--IDGEPL----DYSRKGLLERRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 Q---DFCLVPrlDVMTNVLLGRLSytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQ 190
Cdd:TIGR01166 75 QdpdDQLFAA--DVDQDVAFGPLN--------LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAM 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490526215 191 NPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNL 235
Cdd:TIGR01166 145 RPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
27-260 |
1.68e-29 |
|
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: 110.92 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGE-IINYHDngetqniaalTTKQMRKW 105
Cdd:cd03265 3 VENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHD----------VVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDFCLVPRLDVMTNVLL-GRLsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIhARL---------YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSML 260
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-231 |
1.93e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 116.31 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 15 AVVLESRKKVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngeTQNI 94
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV--------TLDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 95 AALTTKQMRKWRAQCGMIFQDfclvPRL---DVMTNVLLGRLSYTstlksffkifaDQDRARAIE---LLQWLNMLPHAL 168
Cdd:TIGR02868 397 VPVSSLDQDEVRRRVSVCAQD----AHLfdtTVRENLRLARPDAT-----------DEELWAALErvgLADWLRALPDGL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 169 Q-----RAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:TIGR02868 462 DtvlgeGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
39-258 |
5.56e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqNIAALTTKqMRKWRAQCGMIFQ---- 114
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII---DGV--DITDKKVK-LSDIRKKVGLVFQypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 ---------DFCLVPRldvmtNvlLGrLSYTSTLKSFFkifadqdraRAIELLQwLNMLPHALQRAENLSGGQMQRVAIC 185
Cdd:PRK13637 95 qlfeetiekDIAFGPI-----N--LG-LSEEEIENRVK---------RAMNIVG-LDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490526215 186 RAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-228 |
5.96e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 115.08 E-value: 5.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 17 VLESRKKVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETqnIAA 96
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV---NGVP--LAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQmrkWRAQCGMIFQDFCLVPRlDVMTNVLLGRLSYTSTlksffkifADQDRARAIELLQWLNMLPHALQ-----RA 171
Cdd:TIGR02857 389 ADADS---WRDQIAWVPQHPFLFAG-TIAENIRLARPDASDA--------EIREALERAGLDEFVAALPQGLDtpigeGG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 172 ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV 228
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV 513
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
26-269 |
7.24e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.17 E-value: 7.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDNGET------QNIAALT 98
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVATTpsrelaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 tkqmrkwraqcgmifQDFCLVPRLDVMTNVLLGRLSYTS---TlksffkifaDQDRARAIELLQWLNMLPHALQRAENLS 175
Cdd:COG4604 82 ---------------QENHINSRLTVRELVAFGRFPYSKgrlT---------AEDREIIDEAIAYLDLEDLADRYLDELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFD 254
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
250
....*....|....*.
gi 490526215 255 GHPS-MLNDTIIQDIY 269
Cdd:COG4604 218 GTPEeIITPEVLSDIY 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-252 |
7.55e-29 |
|
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: 109.94 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVL-------NGTIpssageIINYHDNgETQNIaalttkqmRKWRAQC 109
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEI------LLDGVDI-RDLNL--------RWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 110 GMIFQDfclvPRL---DVMTNVLLGRLSYTSTLksffkifaDQDRARAIELLQWLNMLPHAL-----QRAENLSGGQMQR 181
Cdd:cd03249 80 GLVSQE----PVLfdgTIAENIRYGKPDATDEE--------VEEAAKKANIHDFIMSLPDGYdtlvgERGSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVKDyCTRVIGIAHGRII 252
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIA-HRLSTIRN-ADLIAVLQNGQVV 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
38-256 |
8.79e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 114.94 E-value: 8.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 38 HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngetqNIAaLTTKQMRKWRAQCGMIFQDfc 117
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKIN--------GIE-LRELDPESWRKHLSWVGQN-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 lvPRL---DVMTNVLLGRLSYTstlksffkifaDQDRARAIE---LLQWLNMLPHALQ-----RAENLSGGQMQRVAICR 186
Cdd:PRK11174 432 --PQLphgTLRDNVLLGNPDAS-----------DEQLQQALEnawVSEFLPLLPQGLDtpigdQAAGLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 187 AMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVKDyCTRVIGIAHGRIIFDGH 256
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLEDLAQ-WDQIWVMQDGQIVQQGD 566
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-266 |
1.14e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 109.15 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQmrk 104
Cdd:TIGR03410 1 LEVSNLNVYYGQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL-----DGEDITKLPPHE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wRAQCG--------MIFqdfclvPRLDVMTNVLLGrlsytstlksfFKIFADQDRARAIELLQWLNMLPHALQR-AENLS 175
Cdd:TIGR03410 72 -RARAGiayvpqgrEIF------PRLTVEENLLTG-----------LAALPRRSRKIPDEIYELFPVLKEMLGRrGGDLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFD 254
Cdd:TIGR03410 134 GGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVAS 213
|
250
....*....|..
gi 490526215 255 GHPSMLNDTIIQ 266
Cdd:TIGR03410 214 GAGDELDEDKVR 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-251 |
1.23e-28 |
|
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: 107.30 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAY-KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetqniAALTTKQMR 103
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--RLDG------ADISQWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDfclvprldvmtnVLLgrlsYTSTLksffkifadqdraraiellqwlnmlphalqrAEN-LSGGQMQRV 182
Cdd:cd03246 73 ELGDHVGYLPQD------------DEL----FSGSI-------------------------------AENiLSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDyCTRVIGIAHGRI 251
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-255 |
1.52e-28 |
|
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: 109.40 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGlVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINY--HDNGETqNIAALttkq 101
Cdd:COG1119 3 LLELRN-VTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgERRGGE-DVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 mrkwRAQCGMIFQDfcLVPRLDVMTNVL----------LGRlsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRA 171
Cdd:COG1119 77 ----RKRIGLVSPA--LQLRFPRDETVLdvvlsgffdsIGL----------YREPTDEQRERARELLELLGLAHLADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 172 ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
....*
gi 490526215 251 IIFDG 255
Cdd:COG1119 221 VVAAG 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-207 |
1.61e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.85 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVlDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqnIAALTTKQMR 103
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM----------LDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFfKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK11607 88 PYQRPINMMFQSYALFPHMTVEQNIAFG-------LKQD-KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
|
170 180
....*....|....*....|....
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPK 207
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKK 183
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
35-255 |
1.66e-28 |
|
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: 107.64 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLngtipssAGEIINYHDNGETQNIAalTTKQMRKWRAQCGMIFQ 114
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGVSGEVLING--RPLDKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 DFCLVPRLDVMTNvllgrLSYTSTLKSffkifadqdraraiellqwlnmlphalqraenLSGGQMQRVAICRAMMQNPKI 194
Cdd:cd03213 90 DDILHPTLTVRET-----LMFAAKLRG--------------------------------LSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSV-NLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-255 |
2.42e-28 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 108.34 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaaLTTKQMRKWRAQCGMIFQDFCL 118
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlVDGHD---------LALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRlDVMTNVLLGRlsytsTLKSFFKIFADQDRARAIELLQwlnMLPHAL-----QRAENLSGGQMQRVAICRAMMQNPK 193
Cdd:cd03252 88 FNR-SIRDNIALAD-----PGMSMERVIEAAKLAGAHDFIS---ELPEGYdtivgEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 194 ILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVnLHSVNLVKDyCTRVIGIAHGRIIFDG 255
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIII-AHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-258 |
2.46e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIAAlttKQMR 103
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF---DGKPIDYSR---KGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDfclvPRLDVMTNVLLGRLSYTSTlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK13636 79 KLRESVGMVFQD----PDNQLFSASVYQDVSFGAV---NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-258 |
3.61e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqNIAALTTK 100
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI----------TVGGMVLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QMRKW--RAQCGMIFQD---------------FCL----VPRLDVMTnvllgrlsytstlksffkifadqdraRAIELLQ 159
Cdd:PRK13635 73 EETVWdvRRQVGMVFQNpdnqfvgatvqddvaFGLenigVPREEMVE--------------------------RVDQALR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 160 WLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKD 238
Cdd:PRK13635 127 QVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ 206
|
250 260
....*....|....*....|
gi 490526215 239 yCTRVIGIAHGRIIFDGHPS 258
Cdd:PRK13635 207 -ADRVIVMNKGEILEEGTPE 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
43-257 |
3.81e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 110.58 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGET-QNIAALTTkqMRKWRAQCGMIFQDFCLVPR 121
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI---RLGGEVlQDSARGIF--LPPHRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 122 LDVMTNVLLGRlsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPV 201
Cdd:COG4148 92 LSVRGNLLYGR----------KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 202 ASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:COG4148 162 AALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPL 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
40-257 |
5.07e-28 |
|
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: 107.19 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNgetQNIAALttkQMRKWRAQCGMIFQDfclv 119
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL--IDG---VDISKI---GLHDLRSRISIIPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLdvmtnvllgrlsYTSTLKS---FFKIFADQDRARAIE---LLQWLNMLPHALQ-----RAENLSGGQMQRVAICRAM 188
Cdd:cd03244 87 PVL------------FSGTIRSnldPFGEYSDEELWQALErvgLKEFVESLPGGLDtvveeGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 189 MQNPKILLADEPVASLDPKNTTRIMNTLQkiSE-NDIAVVVNLHSVNLVKDYcTRVIGIAHGRIIFDGHP 257
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIR--EAfKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-267 |
5.95e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.42 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaaLTTKQM 102
Cdd:COG1137 3 TLEAENLVKSYGKR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfLDGED---------ITHLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKwRAQCGM--------IFQdfclvpRLDVMTNVLLgrlsytsTLKsFFKIFADQDRARAIELLQWLNMLPHALQRAENL 174
Cdd:COG1137 73 HK-RARLGIgylpqeasIFR------KLTVEDNILA-------VLE-LRKLSKKEREERLEELLEEFGITHLRKSKAYSL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFD 254
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
250
....*....|...
gi 490526215 255 GHPsmlnDTIIQD 267
Cdd:COG1137 218 GTP----EEILNN 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-255 |
9.60e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.27 E-value: 9.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGEtqniaALTTKQMR 103
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV---LWDGE-----PLDPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KW------RAqcgmifqdfcLVPRLDVMTNVL-LGRLSYTStlksffkifADQDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:COG4152 72 RIgylpeeRG----------LYPKMKVGEQLVyLARLKGLS---------KAEAKRRADEWLERLGLGDRANKKVEELSK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
25-207 |
1.20e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.08 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETqniaALTTKQMRK 104
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL---NGRD----LFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wRaQCGMIFQDFCLVPRLDVMTNVLLGrlsytstLKSFfKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:COG1118 75 -R-RVGFVFQHYALFPHMTVAENIAFG-------LRVR-PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVAL 144
|
170 180
....*....|....*....|...
gi 490526215 185 CRAMMQNPKILLADEPVASLDPK 207
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAK 167
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
36-255 |
1.30e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.88 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 36 SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGETQNI--AALttkqmrkwRAQCGMIF 113
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSV--LLDGVDIRQIdpADL--------RRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 QDfclvPRL---DVMTNVLLGRLSYTstlksffkifaDQDRARAIE---LLQWLNMLPHAL-----QRAENLSGGQMQRV 182
Cdd:TIGR03375 546 QD----PRLfygTLRDNIALGAPYAD-----------DEEILRAAElagVTEFVRRHPDGLdmqigERGRSLSGGQRQAV 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEnDIAVVVNLHSVNLVkDYCTRVIGIAHGRIIFDG 255
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA-GKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADG 681
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
25-255 |
2.67e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 105.14 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAY---KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngETQNIAALttKQ 101
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-------TVDGFDVV--KE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKWRAQCGMIFQDFCLVPRLDVMTNVL-LGRLsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDRLTARENLEyFAGL---------YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-248 |
2.91e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 105.25 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAY---KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGetQNIAALT 98
Cdd:PRK10584 4 ENIVEVHHLKKSVgqgEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEV---SLVG--QPLHQMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 TKQMRKWRAQ-CGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKsffkifadQDRARAIELLQWLNMLPHALQRAENLSGG 177
Cdd:PRK10584 79 EEARAKLRAKhVGFVFQSFMLIPTLNALENVELPALLRGESSR--------QSRNGAKALLEQLGLGKRLDHLPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTlqkisendiavvvnLHSVNlvKDYCTRVIGIAH 248
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL--------------LFSLN--REHGTTLILVTH 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
27-263 |
4.36e-27 |
|
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: 105.11 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETqniAALTTKQMRkwr 106
Cdd:cd03296 5 VRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF---GGED---ATDVPVQER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 107 aQCGMIFQDFCLVPRLDVMTNVLLG-RLSYTSTLKSffkifADQDRARAIELLQ-----WL-NMLPHalqraeNLSGGQM 179
Cdd:cd03296 75 -NVGFVFQHYALFRHMTVFDNVAFGlRVKPRSERPP-----EAEIRAKVHELLKlvqldWLaDRYPA------QLSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 180 QRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
....*
gi 490526215 259 MLNDT 263
Cdd:cd03296 223 EVYDH 227
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
41-206 |
4.48e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 108.27 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INyhdngeTQNIAALTTKQMRKWRAQC-GMIFQDFCL 118
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVlID------GEDITKLSKKELRELRRKKmSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRLDVMTNVLLGrlsytstLKsffkiFADQDRA----RAIE------LLQWLNMLPHALqraenlSGGQMQRVAICRAM 188
Cdd:COG4175 117 LPHRTVLENVAFG-------LE-----IQGVPKAerreRAREalelvgLAGWEDSYPDEL------SGGMQQRVGLARAL 178
|
170
....*....|....*...
gi 490526215 189 MQNPKILLADEPVASLDP 206
Cdd:COG4175 179 ATDPDILLMDEAFSALDP 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
25-255 |
5.08e-27 |
|
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: 104.22 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNGETQNIAALttkqmrk 104
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-FDGKSYQKNIEAL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wrAQCGMIFQDFCLVPRLDVMTNVLLGRLSYtstlksffkifaDQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:cd03268 72 --RRIGALIEAPGFYPNLTARENLRLLARLL------------GIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-257 |
5.62e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKS-----QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGETQNiaa 96
Cdd:PRK13633 2 NEMIKCKNVSYKYESneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV--YVDGLDTSD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 ltTKQMRKWRAQCGMIFQ--DFCLVPRLdVMTNVLLGrlsytstlKSFFKIFADQDRARAIELLQWLNMLPHALQRAENL 174
Cdd:PRK13633 77 --EENLWDIRNKAGMVFQnpDNQIVATI-VEEDVAFG--------PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKDyCTRVIGIAHGRIIF 253
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgITIILITHYMEEAVE-ADRIIVMDSGKVVM 224
|
....
gi 490526215 254 DGHP 257
Cdd:PRK13633 225 EGTP 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-255 |
6.86e-27 |
|
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: 104.11 E-value: 6.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 48 IHAGEFVAIIGRSGAGKSTLLHVLNG-TIPSSAGEIINYHDNGetqniaalttkQMRKWRAQCGMIFQDFCLVPRLDVMT 126
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVT-----------AAPPADRPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 127 NVLLGRlsyTSTLKsffkiFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDP 206
Cdd:cd03298 90 NVGLGL---SPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490526215 207 KNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03298 162 ALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-257 |
1.07e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.69 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKSQHRVlDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQ 101
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL-----RGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MrkwrAQCGMI--FQDFCLVPRLDVMTNVLLG--RLSYTSTLKSFFKIFA-----DQDRARAIELLQWLNMLPHALQRAE 172
Cdd:PRK11300 77 I----ARMGVVrtFQHVRLFREMTVIENLLVAqhQQLKTGLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
....*.
gi 490526215 252 IFDGHP 257
Cdd:PRK11300 233 LANGTP 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-231 |
1.55e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.22 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTI-----PSSAGEIinYHDNgetQNIAALT 98
Cdd:PRK14247 3 KIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEV--YLDG---QDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 TKQMRKwRAQcgMIFQDFCLVPRLDVMTNVLLGrLSYTSTLKSFFKIfadQDRAR-AIELLQWLNMLPHALQR-AENLSG 176
Cdd:PRK14247 77 VIELRR-RVQ--MVFQIPNPIPNLSIFENVALG-LKLNRLVKSKKEL---QERVRwALEKAQLWDEVKDRLDApAGKLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIsENDIAVVVNLH 231
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTH 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-207 |
1.90e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTT 99
Cdd:PRK09452 10 SLSPLVELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML---DG--QDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMrkwraQCGMIFQDFCLVPRLDVMTNVLLG-RLSytstlksffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQ 178
Cdd:PRK09452 84 ENR-----HVNTVFQSYALFPHMTVFENVAFGlRMQ---------KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQ 149
|
170 180
....*....|....*....|....*....
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLDPK 207
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-271 |
1.91e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhDNGETQNIAALTTKQMRKWRAQCGMIFQ-- 114
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV----TIGERVITAGKKNKKLKPLRKKVGIVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 -----------DFCLVPrldvmTNvllgrlsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAE-NLSGGQMQRV 182
Cdd:PRK13634 95 ehqlfeetvekDICFGP-----MN---------------FGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMN---TLQKisENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPsm 259
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP-- 230
|
250
....*....|..
gi 490526215 260 lndtiiQDIYSD 271
Cdd:PRK13634 231 ------REIFAD 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-276 |
2.31e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.44 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdnGETQNIAALTTKQMRKWRAQCGMIFQdfcl 118
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV----DDTLITSTSKNKDIKQIRKKVGLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRLDVMTNVLLGRLSYTStlkSFFKIFADQDRARAIELLQWLNMLPHALQRAE-NLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK13649 93 FPESQLFEETVLKDVAFGP---QNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSmlndTIIQDIYSDESPEL 276
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK----DIFQDVDFLEEKQL 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-252 |
4.10e-26 |
|
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: 106.69 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKS---QHRVLDNINFEIHAGEFVAIIGRSGAGKS-TLLHVLnGTIPSSAGEI---INYHDngetQNIAA 96
Cdd:COG4172 6 LLSVEDLSVAFGQgggTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAHPsgsILFDG----QDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQMRKWR-AQCGMIFQDfclvPrldvMT--NVLlgrlsYT------STLKSFFKIFADQDRARAIELL--------- 158
Cdd:COG4172 81 LSERELRRIRgNRIAMIFQE----P----MTslNPL-----HTigkqiaEVLRLHRGLSGAAARARALELLervgipdpe 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 159 QWLNMLPHalQraenLSGGQMQRVAICRAMMQNPKILLADEPVASLDPknTTR-----IMNTLQKisENDIAVVVNLHSV 233
Cdd:COG4172 148 RRLDAYPH--Q----LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--TVQaqildLLKDLQR--ELGMALLLITHDL 217
|
250
....*....|....*....
gi 490526215 234 NLVKDYCTRVIGIAHGRII 252
Cdd:COG4172 218 GVVRRFADRVAVMRQGEIV 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-251 |
4.96e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.88 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 32 KAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqnIAALTTKQMRKWRAQCG 110
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwFSGHD------ITRLKNREVPFLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 111 MIFQDFCLVPRLDVMTNVLLGRLSYTSTlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQ 190
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPLIIAGAS--------GDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 191 NPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-262 |
5.89e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGtipssageiINYHDNGETQNIAALTTKQMR 103
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG---------IYLPQRGRVKVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KW-RAQCGMIFQD-----FCLVPRLDVMTNVLLGRLSytstlksffkifADQDRARAIELLQWLNMLPHALQRAENLSGG 177
Cdd:PRK13647 75 KWvRSKVGLVFQDpddqvFSSTVWDDVAFGPVNMGLD------------KDEVERRVEEALKAVRMWDFRDKPPYHLSYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
....*
gi 490526215 258 SMLND 262
Cdd:PRK13647 223 SLLTD 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-222 |
7.15e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.42 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLvKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNG---TIPSSA--GEIInYHD---NGET 91
Cdd:COG1117 7 TLEPKIEVRNL-NVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARveGEIL-LDGediYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 92 QNIAALttkqmrkwRAQCGMIFQdfclVPRLDVMT---NVLLGrlsytstlksfFKIFADQDRARAIELLQWlnmlphAL 168
Cdd:COG1117 85 VDVVEL--------RRRVGMVFQ----KPNPFPKSiydNVAYG-----------LRLHGIKSKSELDEIVEE------SL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 169 QRAE--------------NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN 222
Cdd:COG1117 136 RKAAlwdevkdrlkksalGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
40-260 |
8.54e-26 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 101.54 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqnIAALTTKQMRKwraQCGMIFQDFCL 118
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlIDGHD------VRDYTLASLRR---QIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRlDVMTNVLLGRLSytstlksffkifADQDR----ARAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAICRAMM 189
Cdd:cd03251 88 FND-TVAENIAYGRPG------------ATREEveeaARAANAHEFIMELPEGYDtvigeRGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 190 QNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVnLHSVNLVKDyCTRVIGIAHGRIIFDG-HPSML 260
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTTFVI-AHRLSTIEN-ADRIVVLEDGKIVERGtHEELL 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-252 |
8.70e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.78 E-value: 8.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIP--SSAGEIInyhdnGETQNIAALTTKQ 101
Cdd:PRK13549 5 LLEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEII-----FEGEELQASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRkwRAQCGMIFQDFCLVPRLDVMTNVLLGRlsytsTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQR 181
Cdd:PRK13549 79 TE--RAGIAIIHQELALVKELSVLENIFLGN-----EITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
39-258 |
8.79e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 8.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhDNGETQNIAALTTKQMRKWRAQCGMIFQdfcl 118
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV----TVGDIVVSSTSKQKEIKPVRKKVGVVFQ---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRLDVMTNVLLGRLSYTStlkSFFKIFADQDRARAIELLQWLNMLPHALQRAE-NLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK13643 92 FPESQLFEETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:PRK13643 169 DEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-255 |
1.03e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.94 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 28 KGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKST----LLHVLNgtipsSAGEIinYHDNgetQNIAALTTKQMR 103
Cdd:PRK15134 289 KGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEI--WFDG---QPLHNLNRRQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQD--FCLVPRLDVMTNVLLGRLSYTSTLKsffkifADQDRARAIELLQWLNMLPHALQR--AEnLSGGQM 179
Cdd:PRK15134 359 PVRHRIQVVFQDpnSSLNPRLNVLQIIEEGLRVHQPTLS------AAQREQQVIAVMEEVGLDPETRHRypAE-FSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 180 QRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISE-NDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-255 |
1.10e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 101.25 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTI-PSSageiinyhdnGETQNIAALTTKQMRK 104
Cdd:cd03267 22 SLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTS----------GEVRVAGLVPWKRRKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIF-QDFCLVPRLDVMTNVLLgrlsytstLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:cd03267 92 FLRRIGVVFgQKTQLWWDLPVIDSFYL--------LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-244 |
1.34e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.25 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 17 VLESRKKVLSVKGL-----VKAYKS-------QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIIN 84
Cdd:PRK15079 1 VTEGKKVLLEVADLkvhfdIKDGKQwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 85 yhdNGetQNIAALTTKQMRKWRAQCGMIFQD--FCLVPRldvMTnvlLGRLsYTSTLKSFF-KIFADQDRARAIELLQWL 161
Cdd:PRK15079 81 ---LG--KDLLGMKDDEWRAVRSDIQMIFQDplASLNPR---MT---IGEI-IAEPLRTYHpKLSRQEVKDRVKAMMLKV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 162 NMLPHALQR-AENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDY 239
Cdd:PRK15079 149 GLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHI 228
|
....*
gi 490526215 240 CTRVI 244
Cdd:PRK15079 229 SDRVL 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-260 |
2.19e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhDNGETQNIAALTTKQMRKWRAQCGMIFQdf 116
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV----TVDDITITHKTKDKYIRPVRKRIGMVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 117 clVPRL-----DVMTNVLLGRLSytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAE-NLSGGQMQRVAICRAMMQ 190
Cdd:PRK13646 93 --FPESqlfedTVEREIIFGPKN--------FKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 191 NPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSML 260
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
33-260 |
2.45e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 100.38 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 33 AYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetQNIAALTTKQMRKwraQCGMI 112
Cdd:cd03253 9 AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI--LIDG---QDIREVTLDSLRR---AIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 113 FQDFCLVPRlDVMTNVLLGRLSYTstlksffkifaDQD---RARAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAI 184
Cdd:cd03253 81 PQDTVLFND-TIGYNIRYGRPDAT-----------DEEvieAAKAAQIHDKIMRFPDGYDtivgeRGLKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVKDyCTRVIGIAHGRIIFDGHPSML 260
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-260 |
4.72e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 45 NFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIAALTtkqmrkwRAQCGMIFQDFCLVPRLDV 124
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL---NGQDHTTTPPS-------RRPVSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 125 MTNVLLGrlsytstLKSFFKIFADQ-----DRARAIELLQWLNMLPHALqraenlSGGQMQRVAICRAMMQNPKILLADE 199
Cdd:PRK10771 89 AQNIGLG-------LNPGLKLNAAQreklhAIARQMGIEDLLARLPGQL------SGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 200 PVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSML 260
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-257 |
5.24e-25 |
|
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: 103.73 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 17 VLESRKKVLSVKGLVKAYKSQHR----VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGEtQ 92
Cdd:TIGR03269 272 EVEVGEPIIKVRNVSKRYISVDRgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV--NVRVGD-E 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 93 NIAALTTKQMRKWRAQ--CGMIFQDFCLVPRLDVMTNVL----------LGRLSYTSTLKSffkIFADQDRARAIellqw 160
Cdd:TIGR03269 349 WVDMTKPGPDGRGRAKryIGILHQEYDLYPHRTVLDNLTeaiglelpdeLARMKAVITLKM---VGFDEEKAEEI----- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 161 LNMLPHalqraeNLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISE--NDIAVVVNlHSVNLVKD 238
Cdd:TIGR03269 421 LDKYPD------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVS-HDMDFVLD 493
|
250
....*....|....*....
gi 490526215 239 YCTRVIGIAHGRIIFDGHP 257
Cdd:TIGR03269 494 VCDRAALMRDGKIVKIGDP 512
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
45-251 |
1.56e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 97.62 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 45 NFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngeTQNIAALTTkqMRKWRAQCGMIFQDFCLVPRLDV 124
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI--------KVNDQSHTG--LAPYQRPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 125 MTNVLLGrlsytstLKSFFKIFADQ-----DRARAIELLQWLNMLPhalqraENLSGGQMQRVAICRAMMQNPKILLADE 199
Cdd:TIGR01277 88 RQNIGLG-------LHPGLKLNAEQqekvvDAAQQVGIADYLDRLP------EQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490526215 200 PVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLcSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-205 |
4.27e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.88 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 15 AVVLESR--KKVLSVK-GLVKAyKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGET 91
Cdd:PRK11308 3 QPLLQAIdlKKHYPVKrGLFKP-ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGEL--YYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 92 QNIAALTTKQMRKwRAQcgMIFQD--FCLVPRLDVMTnVLLGRLSYTSTLKsffkifADQDRARAIELLQWLNMLPHALQ 169
Cdd:PRK11308 80 LKADPEAQKLLRQ-KIQ--IVFQNpyGSLNPRKKVGQ-ILEEPLLINTSLS------AAERREKALAMMAKVGLRPEHYD 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 490526215 170 RAENL-SGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PRK11308 150 RYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-251 |
4.56e-24 |
|
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: 95.58 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLvkaykSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETqnIAALTTKQ 101
Cdd:cd03215 2 EPVLEVRGL-----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL---DGKP--VTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKwraqCGMIF-----QDFCLVPRLDVMTNVLLGRLsytstlksffkifadqdraraiellqwlnmlphalqraenLSG 176
Cdd:cd03215 72 AIR----AGIAYvpedrKREGLVLDLSVAENIALSSL----------------------------------------LSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVvnLHSVNL--VKDYCTRVIGIAHGRI 251
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVL--LISSELdeLLGLCDRILVMYEGRI 182
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-205 |
7.76e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqnIAALTTKQMRKW 105
Cdd:PRK11000 5 TLRNVTKAYGDVV-ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF----------IGEKRMNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDFCLVPRLDVMTNvllgrLSYTSTLKSFFKIFADQDRARAIELLQwlnmLPHALQR-AENLSGGQMQRVAI 184
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAEN-----MSFGLKLAGAKKEEINQRVNQVAEVLQ----LAHLLDRkPKALSGGQRQRVAI 144
|
170 180
....*....|....*....|.
gi 490526215 185 CRAMMQNPKILLADEPVASLD 205
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-274 |
8.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 21 RKKVLSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYhdnGETqnIAALTT 99
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID---GIT--ISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKwraQCGMIFQDfclvPrldvmTNVLLGrlsytSTLK-----SFFKIFADQDRARAI--ELLQWLNMLPHALQRAE 172
Cdd:PRK13632 79 KEIRK---KIGIIFQN----P-----DNQFIG-----ATVEddiafGLENKKVPPKKMKDIidDLAKKVGMEDYLDKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPK---NTTRIMNTLQKisENDIAVVVNLHSVNLVKDyCTRVIGIAHG 249
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKgkrEIKKIMVDLRK--TRKKTLISITHDMDEAIL-ADKVIVFSEG 218
|
250 260
....*....|....*....|....*..
gi 490526215 250 RIIFDGHPS-MLNDT-IIQDIYSDeSP 274
Cdd:PRK13632 219 KLIAQGKPKeILNNKeILEKAKID-SP 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-255 |
1.20e-23 |
|
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: 95.68 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 5 LRKLTVaDYPAVVLESRKKVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIIN 84
Cdd:cd03220 3 LENVSK-SYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 85 yhdngeTQNIAALTTkqmrkwraqCGMIFQdfclvPRLDVMTNV-LLGRL-----SYTSTLKSFFKIFAdqdraraiELL 158
Cdd:cd03220 82 ------RGRVSSLLG---------LGGGFN-----PELTGRENIyLNGRLlglsrKEIDEKIDEIIEFS--------ELG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 159 QWLNMlphalqRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKD 238
Cdd:cd03220 134 DFIDL------PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKR 207
|
250
....*....|....*..
gi 490526215 239 YCTRVIGIAHGRIIFDG 255
Cdd:cd03220 208 LCDRALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
39-269 |
1.39e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.60 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETQNI----AALTtkqmrkwrAQCGMIFQ 114
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI---LIDGQEMRFasttAALA--------AGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 DFCLVPRLDVMTNVLLGRLSytstlKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKI 194
Cdd:PRK11288 87 ELHLVPEMTVAENLYLGQLP-----HKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIfDGHPSML---NDTI------- 264
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV-ATFDDMAqvdRDQLvqamvgr 240
|
....*.
gi 490526215 265 -IQDIY 269
Cdd:PRK11288 241 eIGDIY 246
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
37-206 |
2.45e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.47 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIP---SSAGEIINyhdNGetQNIAALTTKQMRkwraqCGMIF 113
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLL---NG--RRLTALPAEQRR-----IGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 QDFCLVPRLDVMTNVLLGrlsytstLKSffKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPK 193
Cdd:COG4136 83 QDDLLFPHLSVGENLAFA-------LPP--TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170
....*....|...
gi 490526215 194 ILLADEPVASLDP 206
Cdd:COG4136 154 ALLLDEPFSKLDA 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-205 |
3.39e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqniaALTTKQMRK 104
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-------------TLDGKPVEG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIFQDFCLVPRLDVMTNVLLG-RLSYTSTlksffkifaDQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK11248 68 PGAERGVVFQNEGLLPWRNVQDNVAFGlQLAGVEK---------MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVG 138
|
170 180
....*....|....*....|..
gi 490526215 184 ICRAMMQNPKILLADEPVASLD 205
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALD 160
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-234 |
3.49e-23 |
|
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: 94.45 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNG-TIPSSAGEIInyhdngETQNIAALTTKQMrkwraqcgMIFQDFCLV 119
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVIL------EGKQITEPGPDRM--------VVFQNYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTNVLLGRLSYTSTLKSffkifaDQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADE 199
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLPDLSK------SERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 490526215 200 PVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVN 234
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIwEEHRVTVLMVTHDVD 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-250 |
7.24e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.56 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 19 ESRKKVLSVKGLVKAYKSQH---RVLDNINFEIHAGEFVAIIGRSGAGKS----TLLHVL--NGTIPSSAgeiinyHDNG 89
Cdd:PRK09473 7 QQADALLDVKDLRVTFSTPDgdvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGRIGGSA------TFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 90 etQNIAALTTKQMRKWRA-QCGMIFQD--FCLVPRLDV---MTNVLL--GRLSYTSTLKSFFKIFadqDRARAIELLQWL 161
Cdd:PRK09473 81 --REILNLPEKELNKLRAeQISMIFQDpmTSLNPYMRVgeqLMEVLMlhKGMSKAEAFEESVRML---DAVKMPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 162 NMLPHalqraeNLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYC 240
Cdd:PRK09473 156 KMYPH------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGIC 229
|
250
....*....|
gi 490526215 241 TRVIGIAHGR 250
Cdd:PRK09473 230 DKVLVMYAGR 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-252 |
8.84e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 15 AVVLESRKK-------VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHD 87
Cdd:COG3845 241 EVLLRVEKApaepgevVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI---RL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 88 NGetQNIAALTTKQMRkwraQCGMIF-----QDFCLVPRLDVMTNVLLGRLsYTSTLKSFFKIFADQDRARAIELLQWLN 162
Cdd:COG3845 318 DG--EDITGLSPRERR----RLGVAYipedrLGRGLVPDMSVAENLILGRY-RRPPFSRGGFLDRKAIRAFAEELIEEFD 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 163 -MLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVvnLHSVNL--VKDY 239
Cdd:COG3845 391 vRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVL--LISEDLdeILAL 468
|
250
....*....|...
gi 490526215 240 CTRVIGIAHGRII 252
Cdd:COG3845 469 SDRIAVMYEGRIV 481
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-255 |
9.29e-23 |
|
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: 91.99 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGETQNIAALTTKQMr 103
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--TLDGVPVSDLEKALSSLI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwraqcGMIFQDfclvPRLdvmtnvllgrlsYTSTLKSffkifadqdraraiellqwlNMlphalqrAENLSGGQMQRVA 183
Cdd:cd03247 78 ------SVLNQR----PYL------------FDTTLRN--------------------NL-------GRRFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLvkDYCTRVIGIAHGRIIFDG 255
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGI--EHMDKILFLENGKIIMQG 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-242 |
1.63e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 38 HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdNGETQNIAALTTKQMRkwraqcgmifqdfc 117
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGGARVAYVPQRSE-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 lVPR---LDVMTNVLLGRLSYTSTLKSFFKifadQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKI 194
Cdd:NF040873 66 -VPDslpLTVRDLVAMGRWARRGLWRRLTR----DDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVK--DYCTR 242
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRraDPCVL 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-258 |
2.14e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNgetQNIAALTTKQMrk 104
Cdd:PRK11231 3 LRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF--LGD---KPISMLSSRQL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wrAQCGMIFQDFCLVPR-LDVMTNVLLGRLSYTStlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK11231 75 --ARRLALLPQHHLTPEgITVRELVAYGRSPWLS----LWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
39-231 |
6.00e-22 |
|
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: 91.18 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSA---GEIINyhdNGETQNIAalttkqmrKWRAQCGMIFQD 115
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILF---NGQPRKPD--------QFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 FCLVPRLDVMTNvllgrLSYTSTLKSFFKIFADQDRAR-AIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKI 194
Cdd:cd03234 90 DILLPGLTVRET-----LTYTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-276 |
6.11e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETqniaalTTKQMR 103
Cdd:PRK13537 7 PIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI---SLCGEP------VPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPRLDVMTNVLL-GRlsytstlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRV 182
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLLVfGR---------YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLND 262
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
250
....*....|....*...
gi 490526215 263 TIIQ----DIYSDESPEL 276
Cdd:PRK13537 228 SEIGcdviEIYGPDPVAL 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-252 |
6.27e-22 |
|
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: 94.89 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIP--SSAGEIInyhdnGETQNIAALTTKQ 101
Cdd:TIGR02633 1 LLEMKGIVKTFGGV-KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIY-----WSGSPLKASNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRkwRAQCGMIFQDFCLVPRLDVMTNVLLGRlsyTSTLKSFFKIFADQDRaRAIELLQWLNM--LPHALQRAEnLSGGQM 179
Cdd:TIGR02633 75 TE--RAGIVIIHQELTLVPELSVAENIFLGN---EITLPGGRMAYNAMYL-RAKNLLRELQLdaDNVTRPVGD-YGGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 180 QRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-257 |
8.92e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.61 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKS----QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI------INYHDNGETQN 93
Cdd:PRK13631 21 ILRVKNLYCVFDEkqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 94 IAALT--TKQMRKWRAQCGMIFQ--DFCLVpRLDVMTNVLLGRLSytstlksfFKIFADQDRARAIELLQWLNMLPHALQ 169
Cdd:PRK13631 101 TNPYSkkIKNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVA--------LGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 170 RAE-NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAH 248
Cdd:PRK13631 172 RSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
....*....
gi 490526215 249 GRIIFDGHP 257
Cdd:PRK13631 252 GKILKTGTP 260
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-221 |
9.69e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.86 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 19 ESRKKVLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaal 97
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGED---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 98 TTKQMRKWRAQCgMIFQDFCLVPRLDVMTNVLLGrlsytstLKsFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGG 177
Cdd:PRK11432 70 VTHRSIQQRDIC-MVFQSYALFPHMSLGENVGYG-------LK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDpKNTTRIMNtlQKISE 221
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLD-ANLRRSMR--EKIRE 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-200 |
1.62e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNGETqnIAALTtkqmrkwr 106
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--IPKGLR--IGYLP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 107 aqcgmifQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKI--------------------FADQD----RARAIELLQWLN 162
Cdd:COG0488 68 -------QEPPLDDDLTVLDTVLDGDAELRALEAELEELeaklaepdedlerlaelqeeFEALGgweaEARAEEILSGLG 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 490526215 163 MLPHALQRA-ENLSGGQMQRVAICRAMMQNPKILLADEP 200
Cdd:COG0488 141 FPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
56-275 |
2.51e-21 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 91.40 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 56 IIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNGETQNIAAlttkqmrkWRAQCGMIFQDFCLVPRLDVMTNVLLGrlsy 135
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM--LDGEDVTNVPP--------HLRHINMVFQSYALFPHMTVEENVAFG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 136 tstLKsFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNT 215
Cdd:TIGR01187 67 ---LK-MRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 216 LQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPsmlndtiiQDIYSDESPE 275
Cdd:TIGR01187 143 LKTIQEQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP--------EEIYEEPANL 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-257 |
3.60e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 32 KAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIAALttkqmrkwraqcGM 111
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV---NGRVSALLEL------------GA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 112 IFQdfclvPRLDVMTNV-----LLGrLSYTSTLKSFFKI--FAdqdraraiELLQWLNMlPhalqrAENLSGGQMQRVAI 184
Cdd:COG1134 98 GFH-----PELTGRENIylngrLLG-LSRKEIDEKFDEIveFA--------ELGDFIDQ-P-----VKTYSSGMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:COG1134 158 AVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-268 |
4.29e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.42 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdNGETQNIAALTT 99
Cdd:PRK15439 7 TAPPLLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----EIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRkwraQCG--MIFQDFCLVPRLDVMTNVLLGRLSYTSTLKsffkifadqdraRAIELLQWLN--MLPHALqrAENLS 175
Cdd:PRK15439 81 AKAH----QLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQ------------KMKQLLAALGcqLDLDSS--AGSLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PRK15439 143 VADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
250
....*....|....
gi 490526215 256 HPSMLN-DTIIQDI 268
Cdd:PRK15439 223 KTADLStDDIIQAI 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-258 |
4.71e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSS---AGEIINyhdNGEtqniaALTTKQMRkwrAQCGM 111
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLL---NGM-----PIDAKEMR---AISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 112 IFQDFCLVPRLDVmtnvlLGRLSYTSTLKSFFKIFADQDRARAIELLQWLNMLPHA------LQRAENLSGGQMQRVAIC 185
Cdd:TIGR00955 104 VQQDDLFIPTLTV-----REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490526215 186 RAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLH--SVNLvkdYC--TRVIGIAHGRIIFDGHPS 258
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSEL---FElfDKIILMAEGRVAYLGSPD 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-252 |
5.88e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKSQHRVLDNINFEIHA----------GEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGet 91
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF---NG-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 92 QNIAALTTKQMRKWRAQCGMIFQD--FCLVPRLDVMTNVLlgrlsytSTLKSFFKIFADQDRARAIELLQWLNMLP-HAL 168
Cdd:PRK10261 386 QRIDTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIM-------EPLRVHGLLPGKAAAARVAWLLERVGLLPeHAW 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 169 QRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIA 247
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMY 538
|
....*
gi 490526215 248 HGRII 252
Cdd:PRK10261 539 LGQIV 543
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-267 |
6.76e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDN-GETQNIAALTTKQMR 103
Cdd:PRK11701 7 LSVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-YRMRdGQLRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 K-WRAQCGMIFQDfclvPRLDVMTNVLLG-----RLSYTSTlKSFFKIfadqdRARAielLQWLNMLPHALQRAENL--- 174
Cdd:PRK11701 85 RlLRTEWGFVHQH----PRDGLRMQVSAGgnigeRLMAVGA-RHYGDI-----RATA---GDWLERVEIDAARIDDLptt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 -SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQK-ISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRII 252
Cdd:PRK11701 152 fSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250
....*....|....*
gi 490526215 253 FDGhpsmLNDTIIQD 267
Cdd:PRK11701 232 ESG----LTDQVLDD 242
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-222 |
6.84e-21 |
|
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: 91.81 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 10 VADYP-AVVLESRKKVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INyhd 87
Cdd:COG5265 342 VADAPdAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlID--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 88 nGetQNIAALTTKQMRkwrAQCGMIFQDfclvprldvmT---------NVLLGRLSytstlksffkifADQDR----ARA 154
Cdd:COG5265 419 -G--QDIRDVTQASLR---AAIGIVPQD----------TvlfndtiayNIAYGRPD------------ASEEEveaaARA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 155 IELLQWLNMLPHALQ-----RAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN 222
Cdd:COG5265 471 AQIHDFIESLPDGYDtrvgeRGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG 543
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
50-269 |
8.21e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 8.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 50 AGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRKwraQCGMIFQDfclVPRLDVMTN-- 127
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL-----DAQPLESWSSKAFAR---KVAYLPQQ---LPAAEGMTVre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 128 -VLLGRLSYTSTLKSFfkifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDP 206
Cdd:PRK10575 105 lVAIGRYPWHGALGRF----GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 207 KNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS-MLNDTIIQDIY 269
Cdd:PRK10575 181 AHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAeLMRGETLEQIY 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-207 |
8.81e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.29 E-value: 8.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI------INYHDNGEtQNIAalt 98
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrvVNELEPAD-RDIA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 tkqmrkwraqcgMIFQDFCLVPRLDVMTNvllgrLSYTSTLKSFFKifADQDR-----ARAIELLQWLNMLPHAlqraen 173
Cdd:PRK11650 80 ------------MVFQNYALYPHMSVREN-----MAYGLKIRGMPK--AEIEErvaeaARILELEPLLDRKPRE------ 134
|
170 180 190
....*....|....*....|....*....|....
gi 490526215 174 LSGGQMQRVAICRAMMQNPKILLADEPVASLDPK 207
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-262 |
9.34e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYKsqhrvldNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTT 99
Cdd:PRK10070 30 SKEQILEKTGLSLGVK-------DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-----DGVDIAKISD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRK-WRAQCGMIFQDFCLVPRLDVMTNVLLGRlsytstlkSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQ 178
Cdd:PRK10070 98 AELREvRRKKIAMVFQSFALMPHMTVLDNTAFGM--------ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
....*.
gi 490526215 258 -SMLND 262
Cdd:PRK10070 250 dEILNN 255
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-276 |
1.15e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 29 GLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetQNIAALTTKQMRKWRAQ 108
Cdd:PRK13536 46 GVSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---------TVLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 109 CGMIFQDFCLVPRLDVMTNVLL-GRlsytstlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRA 187
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVfGR---------YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 188 MMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLNDTIIQ- 266
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGc 266
|
250
....*....|...
gi 490526215 267 ---DIYSDESPEL 276
Cdd:PRK13536 267 qviEIYGGDPHEL 279
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-256 |
1.82e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.79 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVK------AYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-InyhdngETQNIAALTT 99
Cdd:PRK13657 331 VKGAVEfddvsfSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlI------DGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKwraQCGMIFQDFCLVPRlDVMTNVLLGRLSYTSTlksffKIFADQDRARAIELL--QWLNMLPHALQRAENLSGG 177
Cdd:PRK13657 405 ASLRR---NIAVVFQDAGLFNR-SIEDNIRVGRPDATDE-----EMRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVnLHSVNLVKDyCTRVIGIAHGRIIFDGH 256
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
39-205 |
1.95e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIiNYHDngetQNIAALTTKQMRkwraqCGMIFQDFCL 118
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-RFHG----TDVSRLHARDRK-----VGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRLDVMTNVLLGrlsytstlksfFKIFADQDR--ARAI--ELLQWLNM--LPHALQR-AENLSGGQMQRVAICRAMMQN 191
Cdd:PRK10851 86 FRHMTVFDNIAFG-----------LTVLPRRERpnAAAIkaKVTQLLEMvqLAHLADRyPAQLSGGQKQRVALARALAVE 154
|
170
....*....|....
gi 490526215 192 PKILLADEPVASLD 205
Cdd:PRK10851 155 PQILLLDEPFGALD 168
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-250 |
2.41e-20 |
|
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: 86.37 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 36 SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqniaalttkqmrkwraqcgmifqd 115
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV--------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 fclvprldvmtnVLLGRLSYTS--------TLKS---FFKIFaDQDR-ARAIE---LLQWLNMLPHALQ-----RAENLS 175
Cdd:cd03250 63 ------------SVPGSIAYVSqepwiqngTIREnilFGKPF-DEERyEKVIKacaLEPDLEILPDGDLteigeKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIM-NTLQKISENDIAVVVNLHSVNLVKdYCTRVIGIAHGR 250
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
38-269 |
3.22e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.57 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 38 HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSA--------GEIINyhdNGETqnIAALTTKQMRKWRA-- 107
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTL---NGEP--LAAIDAPRLARLRAvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 108 ----QCGMIFQdfclvprldVMTNVLLGRLSYTSTLKSffkiFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK13547 89 pqaaQPAFAFS---------AREIVLLGRYPHARRAGA----LTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQ---------NPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIF 253
Cdd:PRK13547 156 FARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|....*..
gi 490526215 254 DGHPS-MLNDTIIQDIY 269
Cdd:PRK13547 236 HGAPAdVLTPAHIARCY 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-228 |
3.78e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLvKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLN---GTIP--SSAGEIINyhdNGetQNIAA 96
Cdd:PRK14239 3 EPILQVSDL-SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVY---NG--HNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTK--QMRKwraQCGMIFQDFCLVPrLDVMTNVLLGrlsytstlksfFKIFADQDRARAIELLQ--------WLNMLPH 166
Cdd:PRK14239 77 PRTDtvDLRK---EIGMVFQQPNPFP-MSIYENVVYG-----------LRLKGIKDKQVLDEAVEkslkgasiWDEVKDR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 167 ALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV 228
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-268 |
5.22e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHD-NGETQNIAAltt 99
Cdd:PRK09700 3 TPYISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItINNINyNKLDHKLAA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 kqmrkwRAQCGMIFQDFCLVPRLDVMTNVLLGRLsytsTLKSFFKI-FAD--QDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:PRK09700 79 ------QLGIGIIYQELSVIDELTVLENLYIGRH----LTKKVCGVnIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTR---IMNTLQKISEndiAVVVNLHSVNLVKDYCTRVIGIAHGRIIF 253
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYlflIMNQLRKEGT---AIVYISHKLAEIRRICDRYTVMKDGSSVC 225
|
250
....*....|....*
gi 490526215 254 DGhpsMLNDTIIQDI 268
Cdd:PRK09700 226 SG---MVSDVSNDDI 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-235 |
7.52e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.94 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 14 PAVVLESRKKVLSVKGLVKAY-KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetq 92
Cdd:TIGR01842 306 PAMPLPEPEGHLSVENVTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV---------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 93 niaALTTKQMRKWRAQ-----CGMIFQDFCLVPRlDVMTNVLLGRLSYTSTlksffKIFADQDRARAIELLQwlnMLPHA 167
Cdd:TIGR01842 376 ---RLDGADLKQWDREtfgkhIGYLPQDVELFPG-TVAENIARFGENADPE-----KIIEAAKLAGVHELIL---RLPDG 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 168 LQ-----RAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNL 235
Cdd:TIGR01842 444 YDtvigpGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSL 516
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-232 |
8.81e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.05 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSA-----GEIINYHDNGETQNIAALTTkqmrkw 105
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDFCLVPRLDVMTNVLLGrLSYTSTLKSFFKI-----FADQDRARAIELLQWLNMLPhalqraENLSGGQMQ 180
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELderveWALKKAALWDEVKDRLNDYP------SNLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIsENDIAVVVNLHS 232
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHS 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-251 |
9.44e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKS--QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHDngetqniaALTT 99
Cdd:PRK13650 2 SNIIEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD--------LLTE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKWRAQCGMIFQ--DFCLVPRlDVMTNVLLGRLSYTSTLKSFfkifadqdRARAIELLQWLNMLPHALQRAENLSGG 177
Cdd:PRK13650 74 ENVWDIRHKIGMVFQnpDNQFVGA-TVEDDVAFGLENKGIPHEEM--------KERVNEALELVGMQDFKEREPARLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISE-NDIAVVVNLHSVNLVKdYCTRVIGIAHGRI 251
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-255 |
1.02e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYK-------SQH-RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHdngetq 92
Cdd:PRK15112 2 ETLLEVRNLSKTFRyrtgwfrRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELlIDDH------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 93 niaALTTKQMRkWRAQC-GMIFQD--FCLVPRLDVmTNVLLGRLSYTSTLKsffkifADQDRARAIELLQWLNMLP-HAL 168
Cdd:PRK15112 76 ---PLHFGDYS-YRSQRiRMIFQDpsTSLNPRQRI-SQILDFPLRLNTDLE------PEQREKQIIETLRQVGLLPdHAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 169 QRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISE-NDIAVVVNLHSVNLVKDYCTRVIGIA 247
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMH 224
|
....*...
gi 490526215 248 HGRIIFDG 255
Cdd:PRK15112 225 QGEVVERG 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-257 |
1.35e-19 |
|
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: 84.39 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQ-HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGetQNIAaltTKQMR 103
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI---EIDG--IDIS---TIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDfclvPRLdvmtnvllgrlsYTSTLKSFFKIFADQDRARAIELLQwlnmlphALQRAENLSGGQMQRVA 183
Cdd:cd03369 79 DLRSSLTIIPQD----PTL------------FSGTIRSNLDPFDEYSDEEIYGALR-------VSEGGLNLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKiSENDIAVVVNLHSVNLVKDyCTRVIGIAHGRIIFDGHP 257
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-228 |
1.36e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 6 RKLTvADYPAVVLESRKKVLSVKGLvkaykSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-IN 84
Cdd:COG1129 239 RELE-DLFPKRAAAPGEVVLEVEGL-----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 85 yhdnGETQNIAalTTKQMRKwraqCGMIF-----QDFCLVPRLDVMTNVLLGRLSytsTLKSFFKIFADQDRARAIELLQ 159
Cdd:COG1129 313 ----GKPVRIR--SPRDAIR----AGIAYvpedrKGEGLVLDLSIRENITLASLD---RLSRGGLLDRRRERALAEEYIK 379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 160 WLNM-LPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPvasldpkntTR---------IMNTLQKISENDIAVVV 228
Cdd:COG1129 380 RLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP---------TRgidvgakaeIYRLIRELAAEGKAVIV 449
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-255 |
1.99e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 26 SVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqNIAALT-TKQMRK 104
Cdd:COG4586 23 ALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV----------RVLGYVpFKRRKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCGMIF-Q------DfclVPRLDvmtnvllgrlSYTsTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGG 177
Cdd:COG4586 93 FARRIGVVFgQrsqlwwD---LPAID----------SFR-LLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
40-269 |
2.70e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGETQNIAaltTKQMRKwraQCGMIFQDFCLV 119
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV--WLDGEHIQHYA---SKEVAR---RIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTNVLLGRLSYtstlKSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADE 199
Cdd:PRK10253 94 GDITVQELVARGRYPH----QPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 200 PVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP-SMLNDTIIQDIY 269
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPkEIVTAELIERIY 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-239 |
2.82e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNgTIPSSAGEI-INYHDNGETQNIAALTTkQMR 103
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVrVEGRVEFFNQNIYERRV-NLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQDFCLVPrLDVMTNVLLGrlsyTSTLKSFFKIFADQDRARAIELLQWLNMLPHALQR-AENLSGGQMQRV 182
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYG----VKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 183 AICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI---SENDIAVVV-NLHSVNLVKDY 239
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrSELTMVIVShNLHQVSRLSDF 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-200 |
3.39e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYKSqHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdNGETQNIAALTtkQ 101
Cdd:COG0488 313 KKVLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK----LGETVKIGYFD--Q 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MrkwraqcgmifQDFcLVPRLDVMTNVLLGRlsytstlksffkifadqDRARAIELLQWL-NML---PHALQRAENLSGG 177
Cdd:COG0488 386 H-----------QEE-LDPDKTVLDELRDGA-----------------PGGTEQEVRGYLgRFLfsgDDAFKPVGVLSGG 436
|
170 180
....*....|....*....|...
gi 490526215 178 QMQRVAICRAMMQNPKILLADEP 200
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEP 459
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-260 |
4.12e-19 |
|
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: 87.31 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMrkwRAQCGMIFQDFCLv 119
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-----DGLNIAKIGLHDL---RFKITIIPQDPVL- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 prldvmtnvllgrlsYTSTLK---SFFKIFADQDRARAIELLQ---WLNMLPHAL-----QRAENLSGGQMQRVAICRAM 188
Cdd:TIGR00957 1372 ---------------FSGSLRmnlDPFSQYSDEEVWWALELAHlktFVSALPDKLdhecaEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 189 MQNPKILLADEPVASLDPKNTTRIMNTLQKISEnDIAVVVNLHSVNLVKDYcTRVIGIAHGRIIFDGHPSML 260
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
41-268 |
6.60e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.88 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngeTQNIAALTTKQMRKWRAQCGMIFQDfclvP 120
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-------VSGIDTGDFSKLQGIRKLVGIVFQN----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RLDVMTNVLLGRLSYTSTLKSF--FKIFADQDRARA-IELLQWLNMLPhalqraENLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK13644 87 ETQFVGRTVEEDLAFGPENLCLppIEIRKRVDRALAeIGLEKYRHRSP------KTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDyCTRVIGIAHGRIIFDGHP-SMLNDTIIQDI 268
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPeNVLSDVSLQTL 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-251 |
7.32e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 82.90 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVK------AY--KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqniaALT 98
Cdd:cd03248 8 LKGIVKfqnvtfAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGK-----PIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 TKQMRKWRAQCGMIFQDFCLVPRlDVMTNVllgrlSYTSTLKSFFKIFADQDRARAIELLQWLNMLPH--ALQRAENLSG 176
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFAR-SLQDNI-----AYGLQSCSFECVKEAAQKAHAHSFISELASGYDteVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDiAVVVNLHSVNLVkDYCTRVIGIAHGRI 251
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR-TVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
31-269 |
8.17e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNGETQniaALTTKQMRkwraqcg 110
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV-FDGKDITD---WQTAKIMR------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 111 mifQDFCLVP-------RLDVMTNVLLG-----RLSYTSTLKSFFKIFADQDRARAiellqwlnmlphalQRAENLSGGQ 178
Cdd:PRK11614 80 ---EAVAIVPegrrvfsRMTVEENLAMGgffaeRDQFQERIKWVYELFPRLHERRI--------------QRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIF-DGHP 257
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLeDTGD 222
|
250
....*....|..
gi 490526215 258 SMLNDTIIQDIY 269
Cdd:PRK11614 223 ALLANEAVRSAY 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
39-255 |
9.95e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGtIPS---SAGEIINyhdNGEtqNIAALTTKQmrkwRAQCG--MIF 113
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKyevTSGSILL---DGE--DILELSPDE----RARAGifLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 QDfclVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDRARaiELLQWLNMLPHALQRA--ENLSGGQMQRVAICRAMMQN 191
Cdd:COG0396 84 QY---PVEIPGVSVSNFLRTALNARRGEELSAREFLKLLK--EKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 192 PKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVkDY--CTRVIGIAHGRIIFDG 255
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRIL-DYikPDFVHVLVDGRIVKSG 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-228 |
1.07e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.54 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetQNIAALTTKQMRK 104
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI--RLDG---RPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAqcgMIFQDfCLVPRLDVMTNVLLGRlsytstlksffKIFADQ--DRARAIELLQWLNMLPHAL-----QRAENLSGG 177
Cdd:PRK10790 416 GVA---MVQQD-PVVLADTFLANVTLGR-----------DISEEQvwQALETVQLAELARSLPDGLytplgEQGNNLSVG 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490526215 178 QMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV 228
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
40-244 |
1.52e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRKWRAQCgmiFQdfclv 119
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-----EGEDISTLKPEIYRQQVSYC---AQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 prldvmTNVLLGRLSYtSTLKSFFKIFADQ-DRARAIELLQWLNMLPHALQRAEN-LSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK10247 89 ------TPTLFGDTVY-DNLIFPWQIRNQQpDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490526215 198 DEPVASLDPKNtTRIMNTL--QKISENDIAVVVNLHSVNLVKdYCTRVI 244
Cdd:PRK10247 162 DEITSALDESN-KHNVNEIihRYVREQNIAVLWVTHDKDEIN-HADKVI 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-257 |
1.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNGETQNIAALttKQMRKWRAQCGMIFQdf 116
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI-VGDYAIPANLKKI--KEVKRLRKEIGLVFQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 117 clVPRLDVMTNVLLGRLSYTSTlksffKIFADQDRA--RAIELLQWLNMLPHALQRAE-NLSGGQMQRVAICRAMMQNPK 193
Cdd:PRK13645 98 --FPEYQLFQETIEKDIAFGPV-----NLGENKQEAykKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 194 ILLADEPVASLDPKNTTRIMNTLQKISEND----IAVVVNLHSVNLVKDyctRVIGIAHGRIIFDGHP 257
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYkkriIMVTHNMDQVLRIAD---EVIVMHEGKVISIGSP 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-232 |
2.51e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.39 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDNGETQNIAALTTKQMRkwraqCGMIFQDFCLVPR 121
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvLNGRVLFDAEKGICLPPEKRR-----IGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 122 LDVMTNVLLGrlsYTSTLKSFFkifadqdrARAIELL---QWLNMLPHALqraenlSGGQMQRVAICRAMMQNPKILLAD 198
Cdd:PRK11144 91 YKVRGNLRYG---MAKSMVAQF--------DKIVALLgiePLLDRYPGSL------SGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190
....*....|....*....|....*....|....*
gi 490526215 199 EPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHS 232
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREiNIPILYVSHS 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-260 |
3.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 23 KVLSVKGLVKAYKSQHRV--LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETqniaaLTTK 100
Cdd:PRK13642 3 KILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---KIDGEL-----LTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QMRKWRAQCGMIFQDfclvPRLDVMTNVLLGRLSYTSTLKSffkIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQ 180
Cdd:PRK13642 75 NVWNLRRKIGMVFQN----PDNQFVGATVEDDVAFGMENQG---IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 181 RVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNL-HSVNLVKDyCTRVIGIAHGRIIFDGHPSM 259
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSItHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
.
gi 490526215 260 L 260
Cdd:PRK13642 227 L 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-257 |
5.17e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.39 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqniaALTTKQMR 103
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI---RGE-----PITKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQD-----FCLVPRLDVM---TNVLLGRLSYTSTLKSFFKIFADQD-RARAiellqwlnmlPHalqraeNL 174
Cdd:PRK13652 75 EVRKFVGLVFQNpddqiFSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEElRDRV----------PH------HL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIF 253
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
....
gi 490526215 254 DGHP 257
Cdd:PRK13652 219 YGTV 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-255 |
6.70e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 83.26 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetqniAALttkqmR 103
Cdd:COG4618 331 LSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV--RLDG------ADL-----S 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KW-RAQCGMIF----QDFCLVP--------RldvmtnvllgrlsytstlksffkiFADQDRARAIEllqwlnmlphALQR 170
Cdd:COG4618 398 QWdREELGRHIgylpQDVELFDgtiaeniaR------------------------FGDADPEKVVA----------AAKL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 A---------------------ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVN 229
Cdd:COG4618 444 AgvhemilrlpdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVI 523
|
250 260
....*....|....*....|....*.
gi 490526215 230 LHSVNLVKdYCTRVIGIAHGRIIFDG 255
Cdd:COG4618 524 THRPSLLA-AVDKLLVLRDGRVQAFG 548
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-240 |
1.18e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqNIAALTTKQMRK 104
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI----------SILGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 -----WRAQCGMIFQDFclvPRLdVMTNVLLGRLSYTStlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQM 179
Cdd:PRK15056 77 knlvaYVPQSEEVDWSF---PVL-VEDVVMMGRYGHMG----WLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490526215 180 QRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYC 240
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-273 |
1.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 80.61 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYK-SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGtipssageIINYHDNGETQNIA--- 95
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--------LLLPDDNPNSKITVdgi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 96 ALTTKQMRKWRAQCGMIFQ--DFCLVPRlDVMTNVLLGRLSYTSTLKSFFKIFADqdraraieLLQWLNMLPHALQRAEN 173
Cdd:PRK13640 73 TLTAKTVWDIREKVGIVFQnpDNQFVGA-TVGDDVAFGLENRAVPRPEMIKIVRD--------VLADVGMLDYIDSEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 174 LSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVkDYCTRVIGIAHGRII 252
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
250 260
....*....|....*....|.
gi 490526215 253 FDGHPsmlndtiiQDIYSDES 273
Cdd:PRK13640 223 AQGSP--------VEIFSKVE 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-255 |
4.09e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.79 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIpSSAGEIINYHDNGETQNIAALTTKQMRKW-RAQCGMIF 113
Cdd:PRK11022 17 SAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVMAEKLEFNGQDLQRISEKERRNLvGAEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 QDfclvprldVMTNVllgRLSYTSTLKSFFKIFADQD------RARAIELLQW---------LNMLPHalqraeNLSGGQ 178
Cdd:PRK11022 96 QD--------PMTSL---NPCYTVGFQIMEAIKVHQGgnkktrRQRAIDLLNQvgipdpasrLDVYPH------QLSGGM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-262 |
5.53e-17 |
|
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: 77.18 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLvKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGtIPS---SAGEIINyhdngETQNIAALTTKQ 101
Cdd:cd03217 1 LEIKDL-HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevTEGEILF-----KGEDITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 mrkwRAQCGmIFQDFCLVPRLDVMTNvllgrlsytstlksffkifadqdraraIELLQWLNmlphalqraENLSGGQMQR 181
Cdd:cd03217 74 ----RARLG-IFLAFQYPPEIPGVKN---------------------------ADFLRYVN---------EGFSGGEKKR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVkDYC--TRVIGIAHGRIIFDGHPSM 259
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLL-DYIkpDRVHVLYDGRIVKSGDKEL 191
|
...
gi 490526215 260 LND 262
Cdd:cd03217 192 ALE 194
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
39-240 |
7.83e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.79 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAgeIIN---YHDNGetQNIAALTTKQMRKW-RAQCGMIFQ 114
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--HVTadrFRWNG--IDLLKLSPRERRKIiGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 D--FCLVPRLDVMTNvlLGRLSYTSTLKSFFKIFADQDRARAIELL---------QWLNMLPHalqraeNLSGGQMQRVA 183
Cdd:COG4170 97 EpsSCLDPSAKIGDQ--LIEAIPSWTFKGKWWQRFKWRKKRAIELLhrvgikdhkDIMNSYPH------ELTEGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRI------MNTLQKIS----ENDIAVVVNL-HSVNLVkdYC 240
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIfrllarLNQLQGTSilliSHDLESISQWaDTITVL--YC 234
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
25-255 |
8.17e-17 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 77.05 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHrVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNGEtqniaaLTTKQMRK 104
Cdd:TIGR03740 1 LETKNLSKRFGKQT-AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEII--FDGHP------WTRKDLHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraqCGMIFQDFCLVPRLDVMTNVLLgrlsyTSTLKSFfkifadqDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAI 184
Cdd:TIGR03740 72 ----IGSLIESPPLYENLTARENLKV-----HTTLLGL-------PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGI 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLH---SVNLVKDYctrvIGIAH-GRIIFDG 255
Cdd:TIGR03740 136 AIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHilsEVQQLADH----IGIISeGVLGYQG 206
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-239 |
8.41e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 16 VVLESRKkvLSVkglvkaYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHV---LNGTIPSSAGE-IINYHDnget 91
Cdd:PRK14243 9 TVLRTEN--LNV------YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEgKVTFHG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 92 QNIAALTTKQMrKWRAQCGMIFQDFCLVPRlDVMTNVLLG-RLSYtstlksfFKIFADQDRARAI-ELLQWLNMLPHALQ 169
Cdd:PRK14243 77 KNLYAPDVDPV-EVRRRIGMVFQKPNPFPK-SIYDNIAYGaRING-------YKGDMDELVERSLrQAALWDEVKDKLKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 170 RAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV--NLHSVNLVKDY 239
Cdd:PRK14243 148 SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVthNMQQAARVSDM 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
41-228 |
1.17e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqniaaLTTKQMRKWRAQCGMIFQDFCLV 119
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlLDGHD---------LRDYTLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PrlDVMTNvllgRLSYTSTlksffKIFADQDRARAIEL---LQWLNMLPHALQRA--EN---LSGGQMQRVAICRAMMQN 191
Cdd:PRK11176 430 N--DTIAN----NIAYART-----EQYSREQIEEAARMayaMDFINKMDNGLDTVigENgvlLSGGQRQRIAIARALLRD 498
|
170 180 190
....*....|....*....|....*....|....*..
gi 490526215 192 PKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV 228
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-262 |
1.19e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGEtqNIAALTTKQMRKWRAQCGMIFQDFCLV 119
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF---DGE--NIPAMSRSRLYTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTNVLLGRLSYT----STLKSFFKIfadqdRARAIELLQWLNMLPhalqrAEnLSGGQMQRVAICRAMMQNPKIL 195
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTqlpaPLLHSTVMM-----KLEAVGLRGAAKLMP-----SE-LSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 196 LADEPVASLDPKNttriMNTLQK-ISENDIAV----VVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLND 262
Cdd:PRK11831 166 MFDEPFVGQDPIT----MGVLVKlISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-205 |
1.55e-16 |
|
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: 79.21 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqniAALTTKqmr 103
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----------PQPGIK--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwraqCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKI---FADQD---------RARAIELLQ----W-----LN 162
Cdd:TIGR03719 70 -----VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEIsakYAEPDadfdklaaeQAELQEIIDaadaWdldsqLE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490526215 163 MLPHAL------QRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:TIGR03719 145 IAMDALrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-266 |
2.06e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETQNIAALTTKQmr 103
Cdd:PRK10762 4 LLQLKGIDKAFPGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI---LYLGKEVTFNGPKSSQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwRAQCGMIFQDFCLVPRLDVMTNVLLGRlSYTSTlksFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:PRK10762 78 --EAGIGIIHQELNLIPQLTIAENIFLGR-EFVNR---FGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLN-D 262
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTeD 231
|
....
gi 490526215 263 TIIQ 266
Cdd:PRK10762 232 SLIE 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-244 |
2.81e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 38 HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNGEtqniaalttkqmrkwraqcgMIF--QD 115
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-RPAGAR--------------------VLFlpQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 fclvPRLdvmtnvLLGRL----SYTSTLKSFfkifadqDRARAIELLQWLNmLPHALQRAEN-------LSGGQMQRVAI 184
Cdd:COG4178 435 ----PYL------PLGTLrealLYPATAEAF-------SDAELREALEAVG-LGHLAERLDEeadwdqvLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKiSENDIAVVVNLHSVNLVkDYCTRVI 244
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLA-AFHDRVL 554
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-260 |
4.29e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGeiinYHDNGET--QNIAALTTKQMRKWRAQCGMIFQDFC 117
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG----YRYSGDVllGGRSIFNYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 LVPrLDVMTNVLLGRLSYTSTLKSFFKIFAdqdRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK14271 112 PFP-MSIMDNVLAGVRAHKLVPRKEFRGVA---QARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENdIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSML 260
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-273 |
6.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetQNIAALTTKQMRKWRAQCGMIFQDfclvP 120
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF--------YNNQAITDDNFEKLRKHIGIVFQN----P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RldvmtNVLLGrlsytSTLK---SF----FKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPK 193
Cdd:PRK13648 93 D-----NQFVG-----SIVKydvAFglenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 194 ILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVN--LVKDYctrVIGIAHGRIIFDGHPsmlndtiiQDIYS 270
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSeaMEADH---VIVMNKGTVYKEGTP--------TEIFD 231
|
...
gi 490526215 271 DES 273
Cdd:PRK13648 232 HAE 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-213 |
9.60e-16 |
|
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: 73.55 E-value: 9.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAyKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDNGETQNIaalttkqmr 103
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAEQRDE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kWRAQCGMIFQDFCLVPRLDVMTNVllgrlsytstlkSFFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVA 183
Cdd:TIGR01189 71 -PHENILYLGHLPGLKPELSALENL------------HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLA 137
|
170 180 190
....*....|....*....|....*....|
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIM 213
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-256 |
1.14e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAY-KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INyhdngeTQNIAALTTKQM 102
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIlLN------GQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RkwraqcgmifQDFCLVP-RLDVmtnvllgrlsYTSTLKSFFKIFADQ-DRARAIELLQWLNmLPHALQRAENL------ 174
Cdd:PRK11160 413 R----------QAISVVSqRVHL----------FSATLRDNLLLAAPNaSDEALIEVLQQVG-LEKLLEDDKGLnawlge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 175 -----SGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVNLVkDYCTRVIGIAHG 249
Cdd:PRK11160 472 ggrqlSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HRLTGL-EQFDRICVMDNG 549
|
....*..
gi 490526215 250 RIIFDGH 256
Cdd:PRK11160 550 QIIEQGT 556
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
40-255 |
1.24e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIpssageiinyHDNGETQNIAALTTKQMRKWRAQCGMIFQDFCLV 119
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI----------QGNNFTGTILANNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVM-TNVLLGRLSYTSTLKSFFKIFADQDRARAIELLQWLN-MLPHALQRAenLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PLN03211 153 PHLTVReTLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENtIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHS-VNLVKDYCTRVIGIAHGRIIFDG 255
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-258 |
1.28e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.49 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSaGEIinyHDNGetQNIAALTTKQMRKWRAqcgMIFQDFCLVP 120
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEI---LLNG--RPLSDWSAAELARHRA---YLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RLDVMTNVLLGRlsytstlksffkifadQDRARAIELLQWLNMLPHALQRAE-------NLSGGQMQRVAICRAMMQ--- 190
Cdd:COG4138 83 AMPVFQYLALHQ----------------PAGASSEAVEQLLAQLAEALGLEDklsrpltQLSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 191 --NP--KILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPS 258
Cdd:COG4138 147 tiNPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
43-257 |
1.66e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIHAgeFVAIIGRSGAGKSTLLHVLNGTIPSSAGEII------NYHDNGetqnIAALttkqmrkwRAQCGMIFQDf 116
Cdd:PRK13638 21 NLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkplDYSKRG----LLAL--------RQQVATVFQD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 117 clvPRLDVMTNVLLGRLSYTstLKSFFkiFADQDRARAI-ELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKIL 195
Cdd:PRK13638 86 ---PEQQIFYTDIDSDIAFS--LRNLG--VPEAEITRRVdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 196 LADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-239 |
3.19e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 34 YKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGET----QNIAALTTKQMRKwraQC 109
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI---KVDGKVlyfgKDIFQIDAIKLRK---EV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 110 GMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDrARAIELlqWLNMLPHALQRAENLSGGQMQRVAICRAMM 189
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEC-LRKVGL--WKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490526215 190 QNPKILLADEPVASLDPKNTTRIMNTLQKIsENDIAVVV---NLHSVNLVKDY 239
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIvshNPQQVARVADY 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-252 |
3.39e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQ---HRVLDNINFEIHAGEFVAIIGRSGAGKS-TLLHVLnGTIPSS-----AGEIInYHDngetQNIA 95
Cdd:PRK15134 6 LAIENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPpvvypSGDIR-FHG----ESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 96 ALTTKQMRKWRA-QCGMIFQD--FCLVPrLDVMTNVLLGRLSYTSTLKsffkifadQDRARAiELLQWLNM--LPHALQR 170
Cdd:PRK15134 80 HASEQTLRGVRGnKIAMIFQEpmVSLNP-LHTLEKQLYEVLSLHRGMR--------REAARG-EILNCLDRvgIRQAAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 AEN----LSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIG 245
Cdd:PRK15134 150 LTDyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAV 229
|
....*..
gi 490526215 246 IAHGRII 252
Cdd:PRK15134 230 MQNGRCV 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-255 |
9.59e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQHRVLD---NINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-----INYHDNGETQNIA 95
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAavrNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 96 ALTTKQMRKWR-AQCGMIFQD--FCLVPRLDVMTNV-----LLGRLSYTSTLKSFFKIFadqDRARAIELLQWLNMLPHa 167
Cdd:PRK10261 92 EQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIaesirLHQGASREEAMVEAKRML---DQVRIPEAQTILSRYPH- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 168 lqraeNLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIM---NTLQKisENDIAVVVNLHSVNLVKDYCTRVI 244
Cdd:PRK10261 168 -----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILqliKVLQK--EMSMGVIFITHDMGVVAEIADRVL 240
|
250
....*....|.
gi 490526215 245 GIAHGRIIFDG 255
Cdd:PRK10261 241 VMYQGEAVETG 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
36-218 |
1.12e-14 |
|
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: 69.88 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 36 SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHdngetqniaalttkqmrkwrAQCGMIFqd 115
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-MP--------------------EGEDLLF-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 fclVPRLDVMTnvlLGRLsytstlksffkifadqdraRAIELLQWlnmlphalqrAENLSGGQMQRVAICRAMMQNPKIL 195
Cdd:cd03223 69 ---LPQRPYLP---LGTL-------------------REQLIYPW----------DDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180
....*....|....*....|...
gi 490526215 196 LADEPVASLDPKNTTRIMNTLQK 218
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE 136
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-263 |
1.23e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.59 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEiINYHDngetqniAALTTKQMRKWRAQCGMIFQ 114
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD-IRFHD-------IPLTKLQLDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 dfclVPRL---DVMTNVLLGRLSYTSTlksffKIfadQDRARAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAICR 186
Cdd:PRK10789 397 ----TPFLfsdTVANNIALGRPDATQQ-----EI---EHVARLASVHDDILRLPQGYDtevgeRGVMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 187 AMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDiAVVVNLHSVNLVKDyCTRVIGIAHGRIIFDG-HPSMLNDT 263
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR-TVIISAHRLSALTE-ASEILVMQHGHIAQRGnHDQLAQQS 540
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-240 |
1.55e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI------INYHDNGEtqniaALttkqmrkwRAQCGMI 112
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeIDFKSSKE-----AL--------ENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 113 FQDFCLVPRLDVMTNVLLGRLSytstLKSFF-----------KIFADQDraraiellqwLNMLPHalQRAENLSGGQMQR 181
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYP----TKGMFvdqdkmyrdtkAIFDELD----------IDIDPR--AKVATLSVSQMQM 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYC 240
Cdd:PRK10982 143 IEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLC 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
40-228 |
1.98e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInYHDNGETQNIaalttkQMRKWRAQCGMIFQDFCL- 118
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-INDSHNLKDI------NLKWWRSKIGVVSQDPLLf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 --------------VPRLDVMTNVL------------------------LGRLSYTST------LKSFFKIFADQDR--- 151
Cdd:PTZ00265 473 snsiknnikyslysLKDLEALSNYYnedgndsqenknkrnscrakcagdLNDMSNTTDsnelieMRKNYQTIKDSEVvdv 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 152 ARAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQ--KISENDI 224
Cdd:PTZ00265 553 SKKVLIHDFVSALPDKYEtlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRI 632
|
....
gi 490526215 225 AVVV 228
Cdd:PTZ00265 633 TIII 636
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-232 |
2.18e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLvKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHDNGETQNIaalttkqmr 103
Cdd:PRK13539 2 MLEGEDL-ACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 kwRAQCGMI-FQDFClVPRLDVMTNVllgrlsytstlkSFFKIFADQDRARAIELLQWLNmLPHALQR-AENLSGGQMQR 181
Cdd:PRK13539 72 --AEACHYLgHRNAM-KPALTVAENL------------EFWAAFLGGEELDIAAALEAVG-LAPLAHLpFGYLSAGQKRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHS 232
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-204 |
2.20e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAyksqhrvLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIP--SSAGEIInYhdNGETQniaalttkQMRKWRA- 107
Cdd:NF040905 14 VKA-------LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEIL-F--DGEVC--------RFKDIRDs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 108 -QCG--MIFQDFCLVPRLDVMTNVLLGrlsytSTLKSFFKIFADQDRARAIELLQ--WLNMLPHALqrAENLSGGQMQRV 182
Cdd:NF040905 76 eALGivIIHQELALIPYLSIAENIFLG-----NERAKRGVIDWNETNRRARELLAkvGLDESPDTL--VTDIGVGKQQLV 148
|
170 180
....*....|....*....|..
gi 490526215 183 AICRAMMQNPKILLADEPVASL 204
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAAL 170
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-262 |
2.91e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLvKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTiPS---SAGEIINYHdngetQNIAA 96
Cdd:CHL00131 3 KNKPILEIKNL-HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAykiLEGDILFKG-----ESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQmrkwRAQCGmIFQDFCLVPRLDVMTNVLLGRLSYTSTLK----------SFFKIFAdqdraraiELLQWLNMLPH 166
Cdd:CHL00131 76 LEPEE----RAHLG-IFLAFQYPIEIPGVSNADFLRLAYNSKRKfqglpeldplEFLEIIN--------EKLKLVGMDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 167 ALQRA--ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNL----VKDYc 240
Cdd:CHL00131 143 FLSRNvnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLldyiKPDY- 221
|
250 260
....*....|....*....|..
gi 490526215 241 trVIGIAHGRIIFDGHPSMLND 262
Cdd:CHL00131 222 --VHVMQNGKIIKTGDAELAKE 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-262 |
4.98e-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: 71.97 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHDNGETqNIAALttkqmrkw 105
Cdd:TIGR01257 931 VKNLVKIFEPSGRpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAV-------- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDFCLVPRLDVMTNVLlgrlsYTSTLKSffkifADQDRAR-AIELLQWLNMLPHAL-QRAENLSGGQMQRVA 183
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHIL-----FYAQLKG-----RSWEEAQlEMEAMLEDTGLHHKRnEEAQDLSGGMQRKLS 1071
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 184 ICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDiAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHPSMLND 262
Cdd:TIGR01257 1072 VAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR-TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-257 |
5.92e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 44 INFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSaGEIinyHDNGetQNIAALTTKQMRKWRAqcgMIFQDFCLVPRLD 123
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSI---QFAG--QPLEAWSAAELARHRA---YLSQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 124 VMTNVLLGRLSYTSTlksffkifadQDRARAIELLQWLNMLPHALQR-AENLSGGQMQRVAICRAMMQ-----NP--KIL 195
Cdd:PRK03695 86 VFQYLTLHQPDKTRT----------EAVASALNEVAEALGLDDKLGRsVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 196 LADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIIFDGHP 257
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-205 |
6.26e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 6 RKLTvADYPAVVLESRKKVLSVKGLvkaykSQHRVlDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI--- 82
Cdd:PRK10762 240 RKLE-DQYPRLDKAPGEVRLKVDNL-----SGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtld 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 83 -----INYHDNGETQNIAALTtkQMRKWRAqcgmifqdfcLVPRLDVMTNVLLGRLSYTStlKSFFKIFADQDRARAIEL 157
Cdd:PRK10762 313 ghevvTRSPQDGLANGIVYIS--EDRKRDG----------LVLGMSVKENMSLTALRYFS--RAGGSLKHADEQQAVSDF 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490526215 158 LQWLNM-LPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PRK10762 379 IRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
25-250 |
1.04e-13 |
|
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: 66.70 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdNGETQNIAALttkqmrk 104
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT----WGSTVKIGYF------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 wraqcgmifqdfclvprldvmtnvllgrlsytstlksffkifadqdraraiellqwlnmlphalqraENLSGGQMQRVAI 184
Cdd:cd03221 69 -------------------------------------------------------------------EQLSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 185 CRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKIsenDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY---PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-255 |
1.75e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 13 YPAVVLESRKKV----LSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI------ 82
Cdd:PRK15064 304 NPFIRFEQDKKLhrnaLEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsena 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 83 -INY------HDNGETQNIaaltTKQMRKWRAQCGmifqdfclvprLDVMTNVLLGRLSYTstlksffkifadQDRARai 155
Cdd:PRK15064 383 nIGYyaqdhaYDFENDLTL----FDWMSQWRQEGD-----------DEQAVRGTLGRLLFS------------QDDIK-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 156 ellqwlnmlphalQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVvnlHSVNL 235
Cdd:PRK15064 434 -------------KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVS---HDREF 497
|
250 260
....*....|....*....|.
gi 490526215 236 VKDYCTRVIGIAHGRII-FDG 255
Cdd:PRK15064 498 VSSLATRIIEITPDGVVdFSG 518
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-206 |
4.35e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 5 LRKLTVADY----PAVVLESRKKVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAG 80
Cdd:PRK10522 299 LNKLALAPYkaefPRPQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 81 EIinYHDNgetqniAALTTKQMRKWRAQCGMIFQDFCLVPRLdvmtnvlLGrlsytstlksffkifaDQDRARAIELLQ- 159
Cdd:PRK10522 379 EI--LLDG------KPVTAEQPEDYRKLFSAVFTDFHLFDQL-------LG----------------PEGKPANPALVEk 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 160 WLNML--PHALQRAEN------LSGGQMQRVAICRAMMQNPKILLADEPVASLDP 206
Cdd:PRK10522 428 WLERLkmAHKLELEDGrisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
38-205 |
4.37e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 38 HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETqniaalttkqMRKWRAQcgmiFQDfc 117
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV---LWQGEP----------IRRQRDE----YHQ-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 lvprldvmtNVL-LG-------RLSYTSTLKSFFKIFADQDRARAIELLQWLN-----MLPhalqrAENLSGGQMQRVAI 184
Cdd:PRK13538 75 ---------DLLyLGhqpgiktELTALENLRFYQRLHGPGDDEALWEALAQVGlagfeDVP-----VRQLSAGQQRRVAL 140
|
170 180
....*....|....*....|.
gi 490526215 185 CRAMMQNPKILLADEPVASLD 205
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAID 161
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-205 |
6.46e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 36 SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHDngetQNIAALttkQMRKWRAQCGMIFqD 115
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD----LIVARL---QQDPPRNVEGTVY-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 FC---------LVPR-----LDVMTNV---LLGRLSytstlksffKIFADQDRA-------RAIELLQWLNMLPHALQRA 171
Cdd:PRK11147 86 FVaegieeqaeYLKRyhdisHLVETDPsekNLNELA---------KLQEQLDHHnlwqlenRINEVLAQLGLDPDAALSS 156
|
170 180 190
....*....|....*....|....*....|....
gi 490526215 172 enLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PRK11147 157 --LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-233 |
8.90e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.40 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR-VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNgTIPSSAGEIinyHDNGETQNIAALttkqmR 103
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRaVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEI---QIDGVSWNSVTL-----Q 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQdfclvprldvmtNVLLGRLSYTSTLKSFFKiFADQDRARAIE---LLQWLNMLPHAL--QRAEN---LS 175
Cdd:TIGR01271 1289 TWRKAFGVIPQ------------KVFIFSGTFRKNLDPYEQ-WSDEEIWKVAEevgLKSVIEQFPDKLdfVLVDGgyvLS 1355
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLqKISENDIAVVVNLHSV 233
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL-KQSFSNCTVILSEHRV 1412
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-217 |
2.08e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGeiinyhdngetqniAALTTKQMRKWRAQCGMIFQ 114
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD--------------ASVVIRGTVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 dfclvprLDVMTNVLLGrlsytstlkSFFkifaDQDR-ARAIE---LLQWLNMLP-HAL----QRAENLSGGQMQRVAIC 185
Cdd:PLN03130 693 -------ATVRDNILFG---------SPF----DPERyERAIDvtaLQHDLDLLPgGDLteigERGVNISGGQKQRVSMA 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490526215 186 RAMMQNPKILLADEPVASLDP---------------KNTTRIMNTLQ 217
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAhvgrqvfdkcikdelRGKTRVLVTNQ 799
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-251 |
2.46e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQmrkwRAQCGMIF-----QDFC 117
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIML-----NGKEINALSTAQ----RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 LVPRLDVMTNVLlgrlSYTSTLKSFFkIFADQDRARAIELLQWLNM-LPHALQRAENLSGGQMQRVAICRAMMQNPKILL 196
Cdd:PRK15439 352 LYLDAPLAWNVC----ALTHNRRGFW-IKPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 197 ADEPVASLDPKNTTRIMNTLQKISENDIAVVV---NLHSVNLVKDyctRVIGIAHGRI 251
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFissDLEEIEQMAD---RVLVMHQGEI 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
41-233 |
4.10e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 63.89 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHDNGETQNIAALTTKQmrkwRAQCGMIFQDFCLVp 120
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN----RYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RLDVMTNVLLGrlsyTSTLKSFFKIFADqdrarAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAICRAMMQNPKIL 195
Cdd:cd03290 92 NATVEENITFG----SPFNKQRYKAVTD-----ACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490526215 196 LADEPVASLDPKNTTRIMNT--LQKISENDIAVVVNLHSV 233
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKL 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-249 |
4.49e-12 |
|
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: 64.31 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 51 GEFVAIIGRSGAGKSTLLHVLNGTI---------PSSAGEIINYHDNGETQN-IAALTTKQMRkwraqCGMIFQDFCLVP 120
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddPPDWDEILDEFRGSELQNyFTKLLEGDVK-----VIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 R-LDVMTNVLLGRLSYTSTLKsffkifadqdraraiELLQWLNmLPHALQRA-ENLSGGQMQRVAICRAMMQNPKILLAD 198
Cdd:cd03236 101 KaVKGKVGELLKKKDERGKLD---------------ELVDQLE-LRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490526215 199 EPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNlVKDYCTRVIGIAHG 249
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA-VLDYLSDYIHCLYG 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
37-236 |
2.36e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqniaalttkqmRKWRAQCGMIFQDF 116
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------------RNGKLRIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 117 CLVPRLDVmtnvllgrlsytsTLKSFFKI---FADQDRARAIELLQWLNMLPHALQRaenLSGGQMQRVAICRAMMQNPK 193
Cdd:PRK09544 77 YLDTTLPL-------------TVNRFLRLrpgTKKEDILPALKRVQAGHLIDAPMQK---LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490526215 194 ILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLV 236
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLV 184
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-205 |
2.88e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 19 ESRKKVLSVKGLVKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLngtipssAGEIINYhdNGETQNIAALT 98
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVDKEF--EGEARPAPGIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 tkqmrkwraqCGMIFQDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKI---FADQD---------RARAIELLQWLNM--L 164
Cdd:PRK11819 72 ----------VGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIyaaYAEPDadfdalaaeQGELQEIIDAADAwdL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490526215 165 PHALQRA-------------ENLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PRK11819 142 DSQLEIAmdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-258 |
3.23e-11 |
|
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: 62.04 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 47 EIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI------INYhdngETQNIAAlttKQMRKWRAQCGMIFQDFCLVP 120
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeieldtVSY----KPQYIKA---DYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 rldvmtnvllgrlsytstlksFFKIfadqdraraiELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEP 200
Cdd:cd03237 94 ---------------------YFKT----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 201 VASLDPKNTTRIMNTLQKISEND--IAVVVNlHSVnLVKDYctrvigIAHGRIIFDGHPS 258
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNekTAFVVE-HDI-IMIDY------LADRLIVFEGEPS 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-249 |
3.54e-11 |
|
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: 63.49 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKAYK-SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEiinyhdngetqniAALT 98
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD-------------ATVA 1999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 TKQMRkwrAQCGMIFQDFCLVPRLDVMTNVLLGR--LSYTSTLKSffkIFADQDRARAIELLQWLNMLPHALQRAENLSG 176
Cdd:TIGR01257 2000 GKSIL---TNISDVHQNMGYCPQFDAIDDLLTGRehLYLYARLRG---VPAEEIEKVANWSIQSLGLSLYADRLAGTYSG 2073
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490526215 177 GQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHG 249
Cdd:TIGR01257 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-263 |
4.35e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 61.79 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAY-KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIpSSAGEIinyHDNGETQNiaaltTKQMR 103
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDI---QIDGVSWN-----SVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 104 KWRAQCGMIFQD---FCLVPRLDV-----MTNVLLGRLSYTSTLKSFFKIFADQdraraiellqwLNMLphALQRAENLS 175
Cdd:cd03289 74 KWRKAFGVIPQKvfiFSGTFRKNLdpygkWSDEEIWKVAEEVGLKSVIEQFPGQ-----------LDFV--LVDGGCVLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLqKISENDIAVVVNLHSVNLVKDyCTRVIGIAHGRI-IFD 254
Cdd:cd03289 141 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL-KQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVrQYD 218
|
....*....
gi 490526215 255 GHPSMLNDT 263
Cdd:cd03289 219 SIQKLLNEK 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-255 |
4.80e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSageiinyhdngETqniAALTTKQMRKWRAQCGMIFQ 114
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA-----------ET---SSVVIRGSVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 dfclvprLDVMTNVLLGrlsytstlksffKIFADQDRARAIE---LLQWLNMLP-HAL----QRAENLSGGQMQRVAICR 186
Cdd:PLN03232 693 -------ATVRENILFG------------SDFESERYWRAIDvtaLQHDLDLLPgRDLteigERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 187 AMMQNPKILLADEPVASLDPKNTTRIMNTLQK---ISENDIAVVVNLHSVNLVKdyctRVIGIAHGRIIFDG 255
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdelKGKTRVLVTNQLHFLPLMD----RIILVSEGMIKEEG 821
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-243 |
4.90e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 36 SQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRKWRAQcgmIFQD 115
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQS-----QFSHITRLSFEQLQKLVSD---EWQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 fclvprldvmTNVLLGRLSYTSTLKSFFKIFADQ--DRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPK 193
Cdd:PRK10938 86 ----------NNTDMLSPGEDDTGRTTAEIIQDEvkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490526215 194 ILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRV 243
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFA 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-270 |
1.04e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.66 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 27 VKGLVK------AYKSQ--HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyHDNgetQNIAALT 98
Cdd:TIGR00958 475 LEGLIEfqdvsfSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL--LDG---VPLVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 99 TKQMRKwraQCGMIFQDFCLVPRlDVMTNVLLGRLSYTSTlksffKIFADQDRARAIELLQWL------NMLPHALQrae 172
Cdd:TIGR00958 550 HHYLHR---QVALVGQEPVLFSG-SVRENIAYGLTDTPDE-----EIMAAAKAANAHDFIMEFpngydtEVGEKGSQ--- 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 nLSGGQMQRVAICRAMMQNPKILLADEPVASLDpkntTRIMNTLQKI-SENDIAVVVNLHSVNLVKDyCTRVIGIAHGRI 251
Cdd:TIGR00958 618 -LSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESrSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
250
....*....|....*....
gi 490526215 252 IFDGHPSMLNDTiiQDIYS 270
Cdd:TIGR00958 692 VEMGTHKQLMED--QGCYK 708
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-221 |
1.18e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 23 KVLSVKGLVKAYKsqHRVL-DNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdNGETQNIAALttKQ 101
Cdd:TIGR03719 321 KVIEAENLTKAFG--DKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE----IGETVKLAYV--DQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRK--------WRAQCGMifQDFCLVPRLDVMTNVLLGRLSYTStlksffkifADQDraraiellqwlnmlphalQRAEN 173
Cdd:TIGR03719 393 SRDaldpnktvWEEISGG--LDIIKLGKREIPSRAYVGRFNFKG---------SDQQ------------------KKVGQ 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490526215 174 LSGGQMQRVAICRAMMQNPKILLADEPVASLDpknttriMNTLQKISE 221
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALEE 484
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-255 |
1.21e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.29 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 22 KKVLSVKGLVKAYkSQHRVLDNINFEIHAGEFVAIIGRSGAGKStllhvlNGTIPSSageiINYHDNGEtqniaalttkq 101
Cdd:NF000106 11 RNAVEVRGLVKHF-GEVKAVDGVDLDVREGTVLGVLGP*GAA**------RGALPAH----V*GPDAGR----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 mRKWRaqcgmiFQDFCLVPR-----LDVMTNVLLGRLSYTSTLKSFFKIFADQD------RARAIELLQWLNMLPHALQR 170
Cdd:NF000106 69 -RPWR------F*TWCANRRalrrtIG*HRPVR*GRRESFSGRENLYMIGR*LDlsrkdaRARADELLERFSLTEAAGRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 AENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGR 250
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
....*
gi 490526215 251 IIFDG 255
Cdd:NF000106 222 VIADG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
39-251 |
1.21e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIP-SSAGEIinYHDNGEtqniaaLTTKQMRK-WRAQCGMIFQD- 115
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEI--FIDGKP------VKIRNPQQaIAQGIAMVPEDr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 --FCLVPRLDVMTNVLLgrlsytSTLKSFFKIFADQDRARAIELLQWLNML----PHALQRAENLSGGQMQRVAICRAMM 189
Cdd:PRK13549 348 krDGIVPVMGVGKNITL------AALDRFTGGSRIDDAAELKTILESIQRLkvktASPELAIARLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 190 QNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV---NLHSVNLVKDyctRVIGIAHGRI 251
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVissELPEVLGLSD---RVLVMHEGKL 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-238 |
1.60e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 37 QHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLngtipssAGEIINYHDNGetqniaalttkqmrKWRAQCGMIFQDF 116
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------AGALKGTPVAG--------------CVDVPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 117 CLVPRLDvmtnvllgrlsytstlksffkifADQDRARAIELLQ--WLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKI 194
Cdd:COG2401 101 SLIDAIG-----------------------RKGDFKDAVELLNavGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKIS-ENDIAVVVNLHSVNLVKD 238
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVATHHYDVIDD 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-215 |
2.70e-10 |
|
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: 60.73 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETqniaALTTKQmrKWRAQCGMifqdfclvp 120
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---HMKGSV----AYVPQQ--AWIQNDSL--------- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RLDVMTNVLLGRLSYTSTLKsffkifadqdrarAIELLQWLNMLPHALQ-----RAENLSGGQMQRVAICRAMMQNPKIL 195
Cdd:TIGR00957 716 RENILFGKALNEKYYQQVLE-------------ACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190
....*....|....*....|....*....|....*..
gi 490526215 196 LADEPVASLDP-----------------KNTTRIMNT 215
Cdd:TIGR00957 783 LFDDPLSAVDAhvgkhifehvigpegvlKNKTRILVT 819
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
40-231 |
3.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIaaltTKQMRKWRAQCGMIFQDFCLV 119
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF-----ERQSI----KKDLCTYQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTNVLLGrLSYTSTlksffkifadqdrARAIELLQWLNMLPHALQRAEN-LSGGQMQRVAICRAMMQNPKILLAD 198
Cdd:PRK13540 87 PYLTLRENCLYD-IHFSPG-------------AVGITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|...
gi 490526215 199 EPVASLDPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
51-249 |
3.29e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 51 GEFVAIIGRSGAGKSTLLHVLNGTI---------PSSAGEIINYHDNGETQN-IAALTTKQMR---KwraqcgmiFQDFC 117
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSWDEVLKRFRGTELQDyFKKLANGEIKvahK--------PQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 LVPR-LDVMTNVLLGRlsytstlksffkifADQdRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILL 196
Cdd:COG1245 171 LIPKvFKGTVRELLEK--------------VDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490526215 197 ADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVkDYCTRVIGIAHG 249
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAIL-DYLADYVHILYG 287
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
40-231 |
3.30e-10 |
|
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: 58.27 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngetqniaalttKQMRKWRAQCGMIFQDFCLV 119
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL----------------LNGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTnvllGRLSYTSTLKsFFKifADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADE 199
Cdd:cd03231 79 GHAPGIK----TTLSVLENLR-FWH--ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 490526215 200 PVASLDPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
42-206 |
3.92e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 42 DNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGE------IINYHDngetqnIAAlttkqmrkwRAQCGMIFQD 115
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqPVDAGD------IAT---------RRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 FCLVPRLDVMTNVLL-GRLsytstlksfFKIFADQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKI 194
Cdd:NF033858 348 FSLYGELTVRQNLELhARL---------FHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170
....*....|..
gi 490526215 195 LLADEPVASLDP 206
Cdd:NF033858 419 LILDEPTSGVDP 430
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-206 |
4.43e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.81 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAYKSQHR----VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNgetqniAALTTK 100
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI--LLDG------QPVTAD 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 QMRKWRAQCGMIFQDFCLVPRldvmtnvLLGrlsytstlksffkIFADQDRARAIELLQWLNMlPHALQRAE------NL 174
Cdd:COG4615 400 NREAYRQLFSAVFSDFHLFDR-------LLG-------------LDGEADPARARELLERLEL-DHKVSVEDgrfsttDL 458
|
170 180 190
....*....|....*....|....*....|..
gi 490526215 175 SGGQMQRVAICRAMMQNPKILLADEPVASLDP 206
Cdd:COG4615 459 SQGQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-265 |
5.48e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 20 SRKKVLSVKGLVKayKSQHRVlDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIAAlTT 99
Cdd:PRK09700 261 AHETVFEVRNVTS--RDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL---NGKDISPRS-PL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKwraqcGMIF-----QDFCLVPRLDVMTNVLLGRLSYTSTLKSFFKIFADQDRARAIELLQ-WLNMLPHAL-QRAE 172
Cdd:PRK09700 334 DAVKK-----GMAYitesrRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQReLLALKCHSVnQNIT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI- 251
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLt 488
|
250
....*....|....*
gi 490526215 252 -IFDGHPSMLNDTII 265
Cdd:PRK09700 489 qILTNRDDMSEEEIM 503
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
51-249 |
7.66e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 51 GEFVAIIGRSGAGKSTLLHVLNGTI---------PSSAGEIINYHDNGETQN-IAALTTKQMR---KwraqcgmiFQDFC 117
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELipnlgdyeeEPSWDEVLKRFRGTELQNyFKKLYNGEIKvvhK--------PQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 LVPRldvmtnVLLGRLSytSTLKSffkifADQdRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK13409 171 LIPK------VFKGKVR--ELLKK-----VDE-RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENDIAVVVNlHSVnLVKDYCTRVIGIAHG 249
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVVE-HDL-AVLDYLADNVHIAYG 286
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-208 |
1.03e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSS-AGEIINY---HDNGET-----QNIAALTTKQMRKWRAQC 109
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFgrrRGSGETiwdikKHIGYVSSSLHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 110 GMIfqdfclvprldvmtNVLLgrlsytstlKSFFK---IF-ADQDRARAIELlQWLNMLPHALQRAE----NLSGGQMQR 181
Cdd:PRK10938 354 SVR--------------NVIL---------SGFFDsigIYqAVSDRQQKLAQ-QWLDILGIDKRTADapfhSLSWGQQRL 409
|
170 180
....*....|....*....|....*..
gi 490526215 182 VAICRAMMQNPKILLADEPVASLDPKN 208
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLN 436
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-263 |
1.16e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqnIAALTTKQMRKwraqcgmifqDFCL 118
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImIDDCD------VAKFGLTDLRR----------VLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 VPRLDVMtnvllgrlsYTSTLKSFFKIFADQDRARAIELLQWLNML------PHAL-----QRAENLSGGQMQRVAICRA 187
Cdd:PLN03232 1315 IPQSPVL---------FSGTVRFNIDPFSEHNDADLWEALERAHIKdvidrnPFGLdaevsEGGENFSVGQRQLLSLARA 1385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 188 MMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVnLHSVNLVKDyCTRVIGIAHGRIIFDGHPSML--NDT 263
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVI-AHRLNTIID-CDKILVLSSGQVLEYDSPQELlsRDT 1461
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-258 |
2.23e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 47 EIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-----INYhdngETQNIAALTTKQMRKWRAQCGMIFQDfclvpr 121
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkISY----KPQYIKPDYDGTVEDLLRSITDDLGS------ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 122 ldvmtnvllgrlsytstlkSFFKIfadqdraraiELLQWLNmLPHALQR-AENLSGGQMQRVAICRAMMQNPKILLADEP 200
Cdd:PRK13409 431 -------------------SYYKS----------EIIKPLQ-LERLLDKnVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 201 VASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLVkDYctrvigIAHGRIIFDGHPS 258
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMI-DY------ISDRLMVFEGEPG 532
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
41-267 |
2.72e-09 |
|
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: 57.53 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSS-AGEIINyhdNGETQNIaaltTKQMRKWRAQCGMIFQD---F 116
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFI---NGKPVDI----RNPAQAIRAGIAMVPEDrkrH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 117 CLVPRLDVMTNVLLgrlsytSTLKSFFKIFADQDRA------RAIELLQWLNMLPH-ALQRaenLSGGQMQRVAICRAMM 189
Cdd:TIGR02633 349 GIVPILGVGKNITL------SVLKSFCFKMRIDAAAelqiigSAIQRLKVKTASPFlPIGR---LSGGNQQKAVLAKMLL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 190 QNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRIifdgHPSMLNDTIIQD 267
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL----KGDFVNHALTQE 493
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-231 |
2.73e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.33 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNG--TIPSSAGEI-INYHDNGETqniaalttkqmrkwra 107
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEIlINGRPLDKN---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 108 qcgmiFQDFC-LVPRLDVmtnvllgrLSYTSTLksffkifadqdraraIELLQWlnmlpHALQRAenLSGGQMQRVAICR 186
Cdd:cd03232 77 -----FQRSTgYVEQQDV--------HSPNLTV---------------REALRF-----SALLRG--LSVEQRKRLTIGV 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490526215 187 AMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-255 |
3.80e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqniaalttkqmrkWRAQcgmifqDFCLV 119
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------------------WAER------SIAYV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTNvllgrlsytSTLKSFFKIFADQDRAR---AIELLQW---LNMLPHALQ-----RAENLSGGQMQRVAICRAM 188
Cdd:PTZ00243 727 PQQAWIMN---------ATVRGNILFFDEEDAARladAVRVSQLeadLAQLGGGLEteigeKGVNLSGGQKARVSLARAV 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 189 MQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLV--KDYctrVIGIAHGRIIFDG 255
Cdd:PTZ00243 798 YANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVprADY---VVALGDGRVEFSG 863
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
40-237 |
5.99e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVL-------NGTI----PSSAGEIINYHD--NGETQNIAALTTKQMRKWR 106
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkNDHHivfkNEHTNDMTNEQDyqGDEEQNVGMKNVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 107 ----AQCGMIFQ----------DFCLVPRLD-------VMTNVLLGRLSYTSTLKSFFKIFADQDRARAIELL---QWLN 162
Cdd:PTZ00265 1263 eggsGEDSTVFKnsgkilldgvDICDYNLKDlrnlfsiVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAaidEFIE 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 163 MLPHALQR-----AENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEN-DIAVVVNLHSVNLV 236
Cdd:PTZ00265 1343 SLPNKYDTnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASI 1422
|
.
gi 490526215 237 K 237
Cdd:PTZ00265 1423 K 1423
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-252 |
8.17e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.09 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 23 KVLSVKGLVKAyksQHRVL-DNINFEIHAGEFVAIIGRSGAGKS----TLLHVLNGTIPSSAGEIinyHDNGETQNIAAL 97
Cdd:PRK10418 3 QQIELRNIALQ---AAQPLvHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRV---LLDGKPVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 98 TTKQMrkwraqcGMIFQDfclvPR-----LDVM------TNVLLGRLSYTSTLKSFFKIFADQDRARAIELlqwlnmlpH 166
Cdd:PRK10418 77 RGRKI-------ATIMQN----PRsafnpLHTMhthareTCLALGKPADDATLTAALEAVGLENAARVLKL--------Y 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 167 ALQraenLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKI-SENDIAVVVNLHSVNLVKDYCTRVIG 245
Cdd:PRK10418 138 PFE----MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAV 213
|
....*..
gi 490526215 246 IAHGRII 252
Cdd:PRK10418 214 MSHGRIV 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-206 |
1.29e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKAYKSQhRVLDNINFEIHAGEFVAIIGRSGAGKSTLL--------------HVLNGTIPSSAgeiinyHdng 89
Cdd:NF033858 1 VARLEGVSHRYGKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagarkiqqgrvEVLGGDMADAR------H--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 90 etqniaalttkqmRkwRAQCgmifqdfclvPRLDVMTNVlLGR-----LSYTSTLKSFFKIF---ADQDRARAIELLQWL 161
Cdd:NF033858 71 -------------R--RAVC----------PRIAYMPQG-LGKnlyptLSVFENLDFFGRLFgqdAAERRRRIDELLRAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490526215 162 NMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDP 206
Cdd:NF033858 125 GLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-251 |
1.73e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 38 HRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngETQNIAALttkqmrkwraqcgmIFQDFC 117
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-------DIKGSAAL--------------IAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 118 LVPRLDVMTNVLLGRLSYTSTLKSFFKIFAdqdraraiELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLA 197
Cdd:PRK13545 96 LNGQLTGIENIELKGLMMGLTKEKIKEIIP--------EIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490526215 198 DEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
40-210 |
2.89e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDN--GE-TQNIAALttkqmrkwrAQCGMIFQD 115
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTAtrGDrSRFMAYL---------GHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 116 FCLVPRLDVMtNVLLGRlsytstlksffkiFADQDRARAIELlqwLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKIL 195
Cdd:PRK13543 97 LSTLENLHFL-CGLHGR-------------RAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|....*
gi 490526215 196 LADEPVASLDPKNTT 210
Cdd:PRK13543 160 LLDEPYANLDLEGIT 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-255 |
3.51e-08 |
|
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: 52.65 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 35 KSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINYHDNGETQNIAAlttkqmRKWRAQCGMIFQ 114
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFA------EKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 DFCLVPRLDVmtnvllgrlsyTSTLKsffkiFAdqdraraiellqwLNMLPHALQRAenLSGGQMQRVAICRAMMQNPKI 194
Cdd:cd03233 91 EDVHFPTLTV-----------RETLD-----FA-------------LRCKGNEFVRG--ISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 195 LLADEPVASLDPKNTTRIMNTLQKISenDIavvvnLHSVNLVKDYCT---------RVIGIAHGRIIFDG 255
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMA--DV-----LKTTTFVSLYQAsdeiydlfdKVLVLYEGRQIYYG 202
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
25-243 |
4.31e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLVKAyksqhrvLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSS---AGEIINYHDngetQNIAALTTKQ 101
Cdd:PRK15093 14 KTSDGWVKA-------VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvTADRMRFDD----IDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 102 MRKW-RAQCGMIFQD--FCLVPRLDVMTNVLLGRLSYTSTLKsFFKIFADQDRaRAIELLQWLNMLPH-ALQRA--ENLS 175
Cdd:PRK15093 83 RRKLvGHNVSMIFQEpqSCLDPSERVGRQLMQNIPGWTYKGR-WWQRFGWRKR-RAIELLHRVGIKDHkDAMRSfpYELT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 176 GGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISEND-IAVVVNLHSVNLVKDYCTRV 243
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKI 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
41-251 |
8.40e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyHDNGETQNIAAlttkqmrkwraqcgmifqDFCLVP 120
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAI------------------SAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 121 RLDVMTNVLLGRLSYTSTLKsffkifadQDRARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEP 200
Cdd:PRK13546 99 QLTGIENIEFKMLCMGFKRK--------EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490526215 201 VASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKDYCTRVIGIAHGRI 251
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
40-260 |
9.29e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-INYHDngetqnIAALTTKQMRKwraQCGMIFQdfcl 118
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIlIDGCD------ISKFGLMDLRK---VLGIIPQ---- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 119 vprldvmTNVLlgrlsYTSTLKSFFKIFADQDRARAIELLQWLNmLPHALQR------------AENLSGGQMQRVAICR 186
Cdd:PLN03130 1321 -------APVL-----FSGTVRFNLDPFNEHNDADLWESLERAH-LKDVIRRnslgldaevseaGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 187 AMMQNPKILLADEPVASLDPKNTTRIMNTlqkISE--NDIAVVVNLHSVNLVKDyCTRVIGIAHGRIIFDGHPSML 260
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKT---IREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
40-205 |
1.01e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.17 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-----INYhdNGETQNIAALTTKQmrkwraqcgmifq 114
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrISF--SSQFSWIMPGTIKE------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 dfclvprldvmtNVLLGrLSYtstlksffkifaDQDRAR----AIELLQWLNMLPHA-----LQRAENLSGGQMQRVAIC 185
Cdd:cd03291 117 ------------NIIFG-VSY------------DEYRYKsvvkACQLEEDITKFPEKdntvlGEGGITLSGGQRARISLA 171
|
170 180
....*....|....*....|
gi 490526215 186 RAMMQNPKILLADEPVASLD 205
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLD 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-205 |
1.02e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI-----INYhdNGETQNIAALTTKQmrkwraqcgmifq 114
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrISF--SPQTSWIMPGTIKD------------- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 115 dfclvprldvmtNVLLG----RLSYTSTLKsffkifadqdrarAIELLQWLNMLPHA-----LQRAENLSGGQMQRVAIC 185
Cdd:TIGR01271 506 ------------NIIFGlsydEYRYTSVIK-------------ACQLEEDIALFPEKdktvlGEGGITLSGGQRARISLA 560
|
170 180
....*....|....*....|
gi 490526215 186 RAMMQNPKILLADEPVASLD 205
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLD 580
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-257 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 47 EIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIInyhdngETQNIAalttkqmrkWRAQcgMIFQDFCLvprlDVMT 126
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD------EDLKIS---------YKPQ--YISPDYDG----TVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 127 nvLLGRLSYTSTLKSFFKIfadqdraraiELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDP 206
Cdd:COG1245 421 --FLRSANTDDFGSSYYKT----------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490526215 207 KNTTRIMNTLQKISEN-DIAVVVNLHSVNLVkDYctrvigIAHGRIIFDGHP 257
Cdd:COG1245 489 EQRLAVAKAIRRFAENrGKTAMVVDHDIYLI-DY------ISDRLMVFEGEP 533
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
40-226 |
1.51e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGeiinyhdngetqniaaLTTKQmrkwrAQCGMIFqdfclV 119
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG----------------RLTKP-----AKGKLFY-----V 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLDVMTN-VLLGRLSYTSTLKSFF-KIFADQDRARAIELLQwlnmLPHALQR----------AENLSGGQMQRVAICRA 187
Cdd:TIGR00954 521 PQRPYMTLgTLRDQIIYPDSSEDMKrRGLSDKDLEQILDNVQ----LTHILEReggwsavqdwMDVLSGGEKQRIAMARL 596
|
170 180 190
....*....|....*....|....*....|....*....
gi 490526215 188 MMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAV 226
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSV 635
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-95 |
1.80e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490526215 23 KVLSVKGLVKAYKsqHRVL-DNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhDNGETQNIA 95
Cdd:PRK11819 323 KVIEAENLSKSFG--DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----KIGETVKLA 390
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-260 |
1.94e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGetQNIAALTtkqMRKWRAQCGMIFQDfclv 119
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV---NG--REIGAYG---LRELRRQFSMIPQD---- 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 PRLdvmtnvllgrlsYTSTLKSFFKIFADQDRARAIELLQWLNMLPHALQRAE-----------NLSGGQMQRVAICRAM 188
Cdd:PTZ00243 1393 PVL------------FDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEgidsrvleggsNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 189 MQ-NPKILLADEPVASLDPKNTTRIMNTLQKISEND--IAVVVNLHSVNlvkdYCTRVIGIAHGRIIFDGHPSML 260
Cdd:PTZ00243 1461 LKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYtvITIAHRLHTVA----QYDKIIVMDHGAVAEMGSPREL 1531
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-251 |
2.60e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 25 LSVKGLvkaykSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdNGETQNIA----ALttk 100
Cdd:PRK11288 258 LRLDGL-----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL---DGKPIDIRsprdAI--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 101 qmrkwRAqcGMIfqdFC--------LVPRLDVMTNVLLGRLSYTSTLKSFfkIFADQDRARAIELLQWLNM-LPHALQRA 171
Cdd:PRK11288 327 -----RA--GIM---LCpedrkaegIIPVHSVADNINISARRHHLRAGCL--INNRWEAENADRFIRSLNIkTPSREQLI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 172 ENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVV---NLHSVNLVKDyctRVIGIAH 248
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFvssDLPEVLGVAD---RIVVMRE 471
|
...
gi 490526215 249 GRI 251
Cdd:PRK11288 472 GRI 474
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-255 |
2.86e-07 |
|
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: 49.24 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLhvlNGTIPSSageiinyhdngetqniaalttkqmrkwraqcg 110
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLYAS-------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 111 mifqdfclvprldvmtnvllGRLSYTSTLKSFFK---IFADQDRaRAIELlqWLNMLPHAlQRAENLSGGQMQRVAICRA 187
Cdd:cd03238 46 --------------------GKARLISFLPKFSRnklIFIDQLQ-FLIDV--GLGYLTLG-QKLSTLSGGELQRVKLASE 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 188 MMQNPK--ILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKdYCTRVIGIAH------GRIIFDG 255
Cdd:cd03238 102 LFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLS-SADWIIDFGPgsgksgGKVVFSG 176
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-205 |
7.45e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 24 VLSVKGLVKayKSQHRVLDnINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI------INYHDNGET-QNIAA 96
Cdd:PRK10982 250 ILEVRNLTS--LRQPSIRD-VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTItlhgkkINNHNANEAiNHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 97 LTTKQMRkwraQCGmIFQdfclvpRLDVMTNVLLgrlsytSTLKSFFKIFADQDRARAIELLQWL--NM---LPHALQRA 171
Cdd:PRK10982 327 LVTEERR----STG-IYA------YLDIGFNSLI------SNIRNYKNKVGLLDNSRMKSDTQWVidSMrvkTPGHRTQI 389
|
170 180 190
....*....|....*....|....*....|....
gi 490526215 172 ENLSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
173-258 |
2.33e-06 |
|
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: 46.80 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 173 NLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISE-NDIAVVVNLHSVnLVKDYCTRVIgiahgrI 251
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEeGKKTALVVEHDL-AVLDYLSDRI------H 143
|
....*..
gi 490526215 252 IFDGHPS 258
Cdd:cd03222 144 VFEGEPG 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-205 |
2.82e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 43 NINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinyhdngetqniaalttkqMRKWRAQCGMIFQDFclVPRL 122
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------------FRSAKVRMAVFSQHH--VDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 123 DVMTNVLLgrlsytSTLKSFFKIFADQDRARAIELLQWLNMlphALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVA 202
Cdd:PLN03073 586 DLSSNPLL------YMMRCFPGVPEQKLRAHLGSFGVTGNL---ALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
...
gi 490526215 203 SLD 205
Cdd:PLN03073 657 HLD 659
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
40-260 |
5.02e-06 |
|
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: 46.83 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIINyhdngETQNIAALTTKQMRkwrAQCGMIFQDfclv 119
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-----DGIDISKLPLHTLR---SRLSIILQD---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 120 prldvmtNVLLG---RLSYTSTLKSffkifADQDRARAIELLQWLNM---LPHAL-----QRAENLSGGQMQRVAICRAM 188
Cdd:cd03288 104 -------PILFSgsiRFNLDPECKC-----TDDRLWEALEIAQLKNMvksLPGGLdavvtEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490526215 189 MQNPKILLADEPVASLDPKNTtrimNTLQKI---SENDIAVVVNLHSVNLVKDyCTRVIGIAHGRII-FDGHPSML 260
Cdd:cd03288 172 VRKSSILIMDEATASIDMATE----NILQKVvmtAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVeCDTPENLL 242
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
41-255 |
2.28e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.56 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTL----LHV-----LNGTIPSSAGEIINYHDNGETQNIA----ALTTKQM---RK 104
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtIYAegqrrYVESLSAYARQFLGQMDKPDVDSIEglspAIAIDQKttsRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 105 WRAQCG----------MIFQDFCLVPRLDVMTNVLLGRLSytstlksffkifadqdraraiellqwlnmlphaLQR-AEN 173
Cdd:cd03270 91 PRSTVGtvteiydylrLLFARVGIRERLGFLVDVGLGYLT---------------------------------LSRsAPT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 174 LSGGQMQRVAICRAMMQNPK--ILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVK--DYctrVI----- 244
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRaaDH---VIdigpg 214
|
250
....*....|..
gi 490526215 245 -GIAHGRIIFDG 255
Cdd:cd03270 215 aGVHGGEIVAQG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
51-231 |
3.77e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 51 GEFVAIIGRSGAGKSTLLHVLNGTipSSAGEIinyhdNGETQnIAALTTKQMRKWRAQcGMIFQDFCLVPRLDVMTNVLL 130
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGR--KTGGYI-----EGDIR-ISGFPKKQETFARIS-GYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 131 G---RLSYTSTlKSFFKIFADQdrarAIELLQwLNMLPHA---LQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASL 204
Cdd:PLN03140 977 SaflRLPKEVS-KEEKMMFVDE----VMELVE-LDNLKDAivgLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*..
gi 490526215 205 DPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-205 |
5.44e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 39 RVL-DNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEII---NYHDNGETQNIAALTTKQM-------RKWRA 107
Cdd:PRK10636 14 RVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgNWQLAWVNQETPALPQPALeyvidgdREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 108 qcgmifqdfcLVPRLDVMTN--------VLLGRLSytstlksffKIFADQDRARAIELLQWLNMLPHALQR-AENLSGGQ 178
Cdd:PRK10636 94 ----------LEAQLHDANErndghaiaTIHGKLD---------AIDAWTIRSRAASLLHGLGFSNEQLERpVSDFSGGW 154
|
170 180
....*....|....*....|....*..
gi 490526215 179 MQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-200 |
8.94e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 13 YPAVVLESRKKVLSVKGLVkAYKSQHR---VLDNINFEIHAGEFVAIIGRSGAGKSTLL---------HVLNGTI----- 75
Cdd:NF040905 246 YPERTPKIGEVVFEVKNWT-VYHPLHPerkVVDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgrsygRNISGTVfkdgk 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 76 ---PSSAGEIInyhDNGetqnIAALTTKqmrkwRAQCGMIFQDfclvprlDVMTNVLLGRLSytsTLKSFFKIFADQDRA 152
Cdd:NF040905 325 evdVSTVSDAI---DAG----LAYVTED-----RKGYGLNLID-------DIKRNITLANLG---KVSRRGVIDENEEIK 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490526215 153 RAIELLQWLNM-LPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEP 200
Cdd:NF040905 383 VAEEYRKKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
171-236 |
9.93e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 9.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 171 AENLSGGqMQR----VAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLV 236
Cdd:pfam13304 234 AFELSDG-TKRllalLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-231 |
1.18e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 34 YKSQHRV-LDNINFEIHAGEFVAIIGRSGAGKSTLLHVL----NGTIPSSAGEIINYHDNGET---------QNIAALTT 99
Cdd:TIGR00956 771 IKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervTTGVITGGDRLVNGRPLDSSfqrsigyvqQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 100 KQMRKwraqcGMIFQDFCLVPrldvmtnvllgrlsytstlKSFFKIFADQDRARAIELLQwLNMLPHAL--QRAENLSGG 177
Cdd:TIGR00956 851 STVRE-----SLRFSAYLRQP-------------------KSVSKSEKMEYVEEVIKLLE-MESYADAVvgVPGEGLNVE 905
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490526215 178 QMQRVAICRAMMQNPKILL-ADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLH 231
Cdd:TIGR00956 906 QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-228 |
2.15e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 34 YKSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEIinYHDNGETQNIAalttkqmrkwRAQCGMIF 113
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI--YYKNCNINNIA----------KPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 114 QDFCLVPRLDVMTNVLLGRLSYTS--TLKSFFKIFADQDraraieLLQwlnmlphalQRAENLSGGQMQRVAICRAMMQN 191
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSaeTLYAAIHYFKLHD------LLD---------EKCYSLSSGMQKIVAIARLIACQ 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 490526215 192 PKILLADEPVASLDPKNtTRIMNTLQKISENDIAVVV 228
Cdd:PRK13541 142 SDLWLLDEVETNLSKEN-RDLLNNLIVMKANSGGIVL 177
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
2-69 |
2.17e-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: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 2 GQALRKLTVADYPAVVLESRKKVLSVKGlvkaykSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLH 69
Cdd:TIGR00630 591 GQYLSGRKKIEVPAERRPGNGKFLTLKG------ARENNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
145-205 |
2.28e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490526215 145 IFADQDRARAIELLQWLNMLPHALQRAEN-LSGGQMQRVAICRAMMQNPKILLADEPVASLD 205
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
174-257 |
2.45e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 174 LSGGQMQRVAICR----AMMQNPKILlaDEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVKdYCTRVI----- 244
Cdd:PRK00635 477 LSGGEQERTALAKhlgaELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LADRIIdigpg 553
|
90
....*....|....
gi 490526215 245 -GIAHGRIIFDGHP 257
Cdd:PRK00635 554 aGIFGGEVLFNGSP 567
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
12-69 |
4.22e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 4.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490526215 12 DYPAVVLESRKKVLSVKGlvkaykSQHRVLDNINFEIHAGEFVAIIGRSGAGKSTLLH 69
Cdd:PRK00349 602 EVPKERRKGNGKFLKLKG------ARENNLKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
40-82 |
4.83e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 4.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490526215 40 VLDNINFEIHAGEFVAIIGRSGAGKSTLLHVLNGTIPSSAGEI 82
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-220 |
7.12e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSqHRVLDNINFEihaGEFVAIIGRSGAGKSTLLH----VLNGTIPSSAGEIINYHDNGETQNIAALT----TKQM 102
Cdd:COG0419 7 LENFRS-YRDTETIDFD---DGLNLIVGPNGAGKSTILEairyALYGKARSRSKLRSDLINVGSEEASVELEfehgGKRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 103 RKWRAQcGMiFQDFCLVPRLDVMTnvLLGRLSYTSTLKSFFKIFAD---------QDRARAIELLQWLNMLPHALQRAEN 173
Cdd:COG0419 83 RIERRQ-GE-FAEFLEAKPSERKE--ALKRLLGLEIYEELKERLKEleealesalEELAELQKLKQEILAQLSGLDPIET 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490526215 174 LSGGQMQRVAICRAMMqnpkiLLADepVASLDPKNTTRIMNTLQKIS 220
Cdd:COG0419 159 LSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
41-257 |
1.75e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 41 LDNINFEIHAGEFVAIIGRSGAGKSTLLH-----------VLNGTIPSSAGEI-----------INYHDNGETQ-NIAAL 97
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrlHLKKEQPGNHDRIeglehidkvivIDQSPIGRTPrSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 98 TTKQMRKWRAqcgmIFQDFCLVPR-----LDV------MTNVLlgrlsyTSTLKSFFKIFADQDR-ARAIELLQWLNMLP 165
Cdd:cd03271 91 YTGVFDEIRE----LFCEVCKGKRynretLEVrykgksIADVL------DMTVEEALEFFENIPKiARKLQTLCDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 166 HAL-QRAENLSGGQMQRVAICRAMMQ---NPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVVVNLHSVNLVK--DY 239
Cdd:cd03271 161 IKLgQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKcaDW 240
|
250 260
....*....|....*....|....
gi 490526215 240 ctrVI------GIAHGRIIFDGHP 257
Cdd:cd03271 241 ---IIdlgpegGDGGGQVVASGTP 261
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
2-69 |
4.25e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 4.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490526215 2 GQALR-KLTVAdYPAVVLESRKKVLSVKGlvkAykSQHRvLDNINFEIHAGEFVAIIGRSGAGKSTLLH 69
Cdd:COG0178 588 GQYLSgRKRIP-VPKKRRKGNGKFLTIKG---A--RENN-LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-250 |
5.17e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.20 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 31 VKAYKSQHRVLDnINFEihaGEFVAIIGRSGAGKSTLL----HVLNGT-IPSSAGEIINYHDNGETQNiaalttkqmrkw 105
Cdd:cd03240 6 IRNIRSFHERSE-IEFF---SPLTLIVGQNGAGKTTIIealkYALTGElPPNSKGGAHDPKLIREGEV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 106 RAQCGMIFQDF----CLVPR-LDVMTNVllgrlsytstlksffkIFADQDRaraielLQWLNMLPhalqrAENLSGGQ-- 178
Cdd:cd03240 70 RAQVKLAFENAngkkYTITRsLAILENV----------------IFCHQGE------SNWPLLDM-----RGRCSGGEkv 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490526215 179 ----MQRVAICRAMMQNPKILLADEPVASLDPKNTT----RIMNTLQKISENDIAVVVnlHSVNLVK--DYCTRVIGIAH 248
Cdd:cd03240 123 laslIIRLALAETFGSNCGILALDEPTTNLDEENIEeslaEIIEERKSQKNFQLIVIT--HDEELVDaaDHIYRVEKDGR 200
|
..
gi 490526215 249 GR 250
Cdd:cd03240 201 QK 202
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
35-71 |
6.79e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.07 E-value: 6.79e-03
10 20 30
....*....|....*....|....*....|....*...
gi 490526215 35 KSQHRVLDNINFEIHAGE-FVAIIGRSGAGKSTLLHVL 71
Cdd:COG3267 26 PSHREALARLEYALAQGGgFVVLTGEVGTGKTTLLRRL 63
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
49-68 |
9.47e-03 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 36.89 E-value: 9.47e-03
|
| |
