|
Name |
Accession |
Description |
Interval |
E-value |
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-285 |
0e+00 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 570.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNL 80
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLK 240
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 323465851 241 KHYLDEPTPSLFASSLT--GFKFKENPLTIKELVDGIKKNVQGEFNE 285
Cdd:PRK13641 241 KHYLDEPATSRFASKLEkgGFKFSEMPLTIDELVDGIKNNLKGGFHE 287
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-277 |
1.10e-157 |
|
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: 439.96 E-value: 1.10e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgNKNLKK 82
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKK-KKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:TIGR04521 80 LRKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEK 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 323465851 242 HYLDEPTPSLFASSLT--GFKFKENPLTIKELVDGIKK 277
Cdd:TIGR04521 240 IGLDVPEITELARKLKekGLPVPKDPLTVEEAADEILK 277
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-282 |
9.08e-138 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 390.15 E-value: 9.08e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNL 80
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:PRK13634 81 KPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWL 239
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 323465851 240 KKHYLDEPTPSLFASSL---TGFKFKENPLTIKELVDGIKKNVQGE 282
Cdd:PRK13634 241 EAIGLDLPETVKFKRALeekFGISFPKPCLTLEELAHEVVQLLRKG 286
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-241 |
2.68e-115 |
|
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: 330.83 E-value: 2.68e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKK 82
Cdd:COG1122 1 IELENLSFSYPGGT----PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT----KKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:COG1122 73 LRRKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-276 |
7.44e-114 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 329.40 E-value: 7.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNL 80
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLK 240
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 323465851 241 KHYLDEPTPSLFASSLT--GFKFKENPLTIKELVDGIK 276
Cdd:PRK13649 241 EKQLGVPKITKFAQRLAdrGISFSSLPITIEEFREVLK 278
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-270 |
7.35e-110 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 319.30 E-value: 7.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgNKNL 80
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK--KVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVIS-KSPFELSGGQMRRVAIAGV 159
Cdd:PRK13637 79 SDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMM-QIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEW 238
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILnKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET 238
|
250 260 270
....*....|....*....|....*....|....
gi 323465851 239 LKKHYLDEPTPSLFASSL--TGFKFKENPLTIKE 270
Cdd:PRK13637 239 LESIGLAVPQVTYLVRKLrkKGFNIPDDIFTIEE 272
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-273 |
1.35e-97 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 288.56 E-value: 1.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKK 82
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKKH 242
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
250 260 270
....*....|....*....|....*....|....
gi 323465851 243 YLDEPTPSLFASSL--TG-FKFKENPLTIKELVD 273
Cdd:PRK13643 242 ELGVPKATHFADQLqkTGaVTFEKLPITRAELVT 275
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-273 |
2.29e-93 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 277.43 E-value: 2.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNL 80
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:PRK13646 81 RPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWL 239
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 323465851 240 KKHYLDEPTPSLFASSLT---GFKFKENPLTIKELVD 273
Cdd:PRK13646 241 ADWHIGLPEIVQLQYDFEqkyQTKLKDIALTEEEFVS 277
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-275 |
1.30e-90 |
|
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: 269.69 E-value: 1.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYhitpQTGN-KNLK 81
Cdd:TIGR04520 1 IEVENVSFSYPES---EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL----DTLDeENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:TIGR04520 74 EIRKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWLK 240
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKlNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLK 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 323465851 241 KHYLDEPTPSLFASSLT--GFKFKENPLTIKELVDGI 275
Cdd:TIGR04520 232 EIGLDVPFITELAKALKkrGIPLPPDILTEEELVDEL 268
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-222 |
6.72e-90 |
|
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: 265.87 E-value: 6.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 4 KFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKL 83
Cdd:cd03225 1 ELKNLSFSYPDG---ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT----KLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 RKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNE 163
Cdd:cd03225 74 RRKVGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 164 PQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGK 222
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-282 |
4.93e-88 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 264.64 E-value: 4.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGN--- 77
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 -----------------KNLKKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVIS 140
Cdd:PRK13651 81 ekvleklviqktrfkkiKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 141 KSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEH 220
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 221 GKLIKHDKPRKIFENKEWLKKHYLDEPTPSLFASSLTGFKFKENPLT-IKELVDGIKKNVQGE 282
Cdd:PRK13651 241 GKIIKDGDTYDILSDNKFLIENNMEPPKLLNFVNKLEKKGIDVPKVTsIEELASEINMYLEKK 303
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-282 |
5.93e-82 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 249.77 E-value: 5.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGN---- 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 --------KNLKKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGG 149
Cdd:PRK13631 101 tnpyskkiKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 150 QMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 230 RKIFENKEWLKKHYLDEPTPSLFASSLT--GFKFKE----NPLTIKELVDGIKKNVQGE 282
Cdd:PRK13631 261 YEIFTDQHIINSTSIQVPRVIQVINDLIkkDPKYKKlyqkQPRTIEQLADAINEFIKGG 319
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-247 |
1.43e-73 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 227.20 E-value: 1.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGN-KNLK 81
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLK 240
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
....*..
gi 323465851 241 KHYLDEP 247
Cdd:PRK13645 247 KIEIDPP 253
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-235 |
5.63e-71 |
|
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: 227.09 E-value: 5.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnKNLKK 82
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR-RSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFEN-TVLEDVKFGPKNFGV-SDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-277 |
7.39e-68 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 211.90 E-value: 7.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtgnKNLKK 82
Cdd:PRK13647 5 IEVEDLHFRYKDGT----KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA----ENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13647 77 VRSKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRkIFENKEWLKKH 242
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDIVEQA 234
|
250 260 270
....*....|....*....|....*....|....*
gi 323465851 243 YLDEPTPSLFASSLTGFKFKENPLTIKELVDGIKK 277
Cdd:PRK13647 235 GLRLPLVAQIFEDLPELGQSKLPLTVKEAVQIIRK 269
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-247 |
1.11e-65 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 206.47 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 7 NINYIYSPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpQTGNKNLKKLRKE 86
Cdd:PRK13639 6 DLKYSYPDGT----EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI--KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 87 VGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQI 166
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 167 LCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKKHYLDE 246
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRL 238
|
.
gi 323465851 247 P 247
Cdd:PRK13639 239 P 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-277 |
1.41e-64 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 203.30 E-value: 1.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPgttMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKK 82
Cdd:PRK13632 8 IKVENVSFSYPN---SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGH-TVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEK 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 323465851 242 HYLDEPTPSLFASSLTGFKFKENpltIKELVDGIKK 277
Cdd:PRK13632 239 AKIDSPFIYKLSKKLKGIDPTYN---EEELIEQICK 271
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-275 |
3.41e-63 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 200.31 E-value: 3.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGT-TMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnKNLK 81
Cdd:PRK13633 5 IKCKNVSYKYESNEeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE---ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:PRK13633 82 DIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIF--VNyQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWL 239
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIkeLN-KKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 323465851 240 KKHYLDEPTPSLFASSL--TGFKFKENPLTIKELVDGI 275
Cdd:PRK13633 239 KKIGLDVPQVTELAYELkkEGVDIPSDILTIDEMVNEL 276
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-273 |
5.73e-63 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 199.47 E-value: 5.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKK 82
Cdd:PRK13635 6 IRVEHISFRY-PDA--ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET----VWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13635 79 VRRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
250 260 270
....*....|....*....|....*....|....
gi 323465851 242 HYLDEPTPSLFASSLT--GFKFKENPLTIKELVD 273
Cdd:PRK13635 237 IGLDVPFSVKLKELLKrnGILLPNTYLTMESLVD 270
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-246 |
9.81e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 194.90 E-value: 9.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnKNLKK 82
Cdd:COG1131 1 IEVRGLTKRYG-----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-----RDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG1131 71 VRRRIGYVPQ--EPALYPDlTVRENLRFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKifenkewLKK 241
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE-------LKA 220
|
....*
gi 323465851 242 HYLDE 246
Cdd:COG1131 221 RLLED 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-283 |
6.51e-61 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 194.68 E-value: 6.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpQTGNKNLKK 82
Cdd:PRK13636 6 LKVEELNYNYSDGT----HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI--DYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 323465851 242 HYLDEPTPSLFASSLT---GFKFKENPLTIKELVDGIKKNVQGEF 283
Cdd:PRK13636 239 VNLRLPRIGHLMEILKekdGFVFDELDLTISQARKTLNSWKNKIF 283
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-254 |
1.68e-60 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 193.10 E-value: 1.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYspgtTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKK 82
Cdd:PRK13652 4 IETRDLCYSY----SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT----KENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13652 76 VRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQiFVN--YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLK 240
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELID-FLNdlPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
250
....*....|....*
gi 323465851 241 KHYLDEPT-PSLFAS 254
Cdd:PRK13652 234 RVHLDLPSlPKLIRS 248
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-223 |
9.31e-60 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 189.24 E-value: 9.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LR-KEVGLVFQFPetQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:cd03255 79 FRrRHIGFVFQSF--NLLPDlTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQK-AGHTVILVTHNMdDVAKYADDVLVMEHGKL 223
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
8.08e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 187.17 E-value: 8.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MS--IKFENINYIYSPGTTmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNK 78
Cdd:COG1136 1 MSplLELRNLTKSYGTGEG-EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS-SLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLR-KEVGLVFQFPetQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAI 156
Cdd:COG1136 79 ELARLRrRHIGFVFQFF--NLLPElTALENVALPLLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMdDVAKYADDVLVMEHGKLIK 225
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-224 |
1.03e-58 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 186.80 E-value: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:COG2884 2 IRFENVSKRYPGG----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG2884 77 LRRRIGVVFQ--DFRLLPDrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-239 |
2.48e-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: 191.66 E-value: 2.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPS---SGTIDIAGYHITPQTgnkn 79
Cdd:COG1123 5 LEVRDLSVRYPGG---DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 LKKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGV 159
Cdd:COG1123 78 EALRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEW 238
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
.
gi 323465851 239 L 239
Cdd:COG1123 237 L 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-218 |
1.49e-54 |
|
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: 176.12 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhiTPQTGnknlkk 82
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFE-NTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:cd03293 71 PGPDRGYVFQ--QDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVM 218
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDiWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-224 |
2.24e-53 |
|
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: 173.46 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqTGNKNLKK 82
Cdd:cd03257 2 LEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK-LSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLfeN---TVLEDVKFGPKNFGVSDKEAEIKAKKWLK--QVGLPTDVISKSPFELSGGQMRRVAIA 157
Cdd:cd03257 80 RRKEIQMVFQDPMSSL--NprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLlvGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 158 GVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-273 |
5.39e-53 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 174.15 E-value: 5.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtgnKNLKK 82
Cdd:PRK13650 5 IEVKNLTFKYKEDQ--EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE----ENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13650 79 IRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAkYADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQ 236
|
250 260 270
....*....|....*....|....*....|....
gi 323465851 242 HYLDEPTPSLFASSL--TGFKFKENPLTIKELVD 273
Cdd:PRK13650 237 LGLDIPFTTSLVQSLrqNGYDLPEGYLTEKELEE 270
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-206 |
9.64e-53 |
|
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: 170.30 E-value: 9.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpQTGNKNLKKLRKEVGLVFQFPETQLFENT 102
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL--DYSRKGLLERRQRVGLVFQDPDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRARE 182
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRVREALTAVGA-SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....
gi 323465851 183 EMMQIFVNYQKAGHTVILVTHNMD 206
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTHDVD 188
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-247 |
9.26e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 171.14 E-value: 9.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKP---SSGTIDIAGYHITpqtgNKN 79
Cdd:PRK13640 6 VEFKHVSFTY-PDS--KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT----AKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 LKKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGV 159
Cdd:PRK13640 79 VWDIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDvAKYADDVLVMEHGKLIKHDKPRKIFENKEW 238
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
....*....
gi 323465851 239 LKKHYLDEP 247
Cdd:PRK13640 237 LKEIGLDIP 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
23-227 |
9.37e-52 |
|
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: 168.47 E-value: 9.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQFPetQLFEN- 101
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT------GVPPERRNIGMVFQDY--ALFPHl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR 181
Cdd:cd03259 88 TVAENIAFGLKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 182 EEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHD 227
Cdd:cd03259 167 EELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
23-240 |
1.20e-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: 169.39 E-value: 1.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKKLRKEVGLVFQFPetQLFEN- 101
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT-GLSEKELYELRRRIGMLFQGG--ALFDSl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFGPK-NFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRA 180
Cdd:COG1127 98 TVFENVAFPLReHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPIT 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 181 REEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENK-EWLK 240
Cdd:COG1127 177 SAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDdPWVR 238
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
23-235 |
1.31e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 169.02 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtGNKNLKKLRKEVGLVFQ-FpetQLFEN 101
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD--SKKDINKLRRKVGMVFQqF---NLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 -TVLEDVKFGP-KNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:COG1126 92 lTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 180 AREEMMQIFVNYQKAGHTVILVTHNMD---DVakyADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG1126 171 LVGEVLDVMRDLAKEGMTMVVVTHEMGfarEV---ADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-235 |
3.61e-51 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 167.76 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:cd03258 2 IELKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT-LLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ-FpetQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:cd03258 80 ARRRIGMIFQhF---NLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIF--VNyQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLrdIN-RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-221 |
4.03e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 168.34 E-value: 4.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNA---LLKPSSGTIDIAGyhitpqtgnKN 79
Cdd:COG1116 8 LELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLL---RLiagLEKPTSGEVLVDG---------KP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 LKKLRKEVGLVFQfpETQLFE-NTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAG 158
Cdd:COG1116 75 VTGPGPDRGVVFQ--EPALLPwLTVLDNVALGLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 159 VMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-223 |
4.65e-51 |
|
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: 166.94 E-value: 4.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnKNLKK 82
Cdd:cd03262 1 IEIKNLHKSFG-----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK--KNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ-FpetQLFEN-TVLEDVKFGP-KNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGV 159
Cdd:cd03262 74 LRQKVGMVFQqF---NLFPHlTVLENITLAPiKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-235 |
1.28e-50 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 166.71 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnkNLKK 82
Cdd:cd03295 1 IEFENVTKRYGGG----KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ----DPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGL-PTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:cd03295 73 LRRKIGYVIQ--QIGLFPHmTVEENIALVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-232 |
3.01e-50 |
|
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: 165.43 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLK-----PSSGTIDIAGYHITpqTGN 77
Cdd:cd03260 1 IELRDLNVYYG-----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIY--DLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 KNLKKLRKEVGLVFQFPetQLFENTVLEDVKFGPKNFGVSDKEA-EIKAKKWLKQVGLPTDVISK-SPFELSGGQMRRVA 155
Cdd:cd03260 74 VDVLELRRRVGMVFQKP--NPFPGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAgHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKI 232
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-222 |
6.40e-50 |
|
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: 162.74 E-value: 6.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqTGNKNLKK 82
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--DLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKFGpknfgvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAIAGVMV 161
Cdd:cd03229 74 LRRRIGMVFQ--DFALFPHlTVLENIALG-----------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGK 222
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
23-235 |
3.84e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.04 E-value: 3.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG---YHITPQtgnknlkklRKEVGLVFQ----FPE 95
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvTGLPPE---------KRNVGMVFQdyalFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TqlfenTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:COG3842 92 L-----TVAENVAFGLRMRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 176 LDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG3842 166 LDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-243 |
1.04e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.80 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnKNLKK 82
Cdd:COG1121 7 IELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---------KPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQL-FENTVLEDVKFG-------PKNFGVSDKEAeikAKKWLKQVGLpTDVISKsPF-ELSGGQMRR 153
Cdd:COG1121 73 ARRRIGYVPQRAEVDWdFPITVRDVVLMGrygrrglFRRPSRADREA---VDEALERVGL-EDLADR-PIgELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 154 VAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGkLIKHDKPRKIF 233
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVL 226
|
250
....*....|
gi 323465851 234 eNKEWLKKHY 243
Cdd:COG1121 227 -TPENLSRAY 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-256 |
7.44e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 160.54 E-value: 7.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYhitpQTGN-KNLK 81
Cdd:PRK13644 2 IRLENVSYSYPDGT----PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI----DTGDfSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:PRK13644 74 GIRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVaKYADDVLVMEHGKLIKHDKPRKIF-------- 233
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLsdvslqtl 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 323465851 234 --------ENKEWLKKHYLDEP-----TPSLFASSL 256
Cdd:PRK13644 232 gltppsliELAENLKMHGVVIPwentsSPSSFAEEI 267
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-275 |
8.15e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 160.30 E-value: 8.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEkkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnkNLKK 82
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT---LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD----NFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13648 81 LRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIfVNYQKAGH--TVILVTHNMDDvAKYADDVLVMEHGKLIKHDKPRKIFENKEWLK 240
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHniTIISITHDLSE-AMEADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
250 260 270
....*....|....*....|....*....|....*
gi 323465851 241 KHYLDEPTPSLFASSLtgfKFKENPLTIKELVDGI 275
Cdd:PRK13648 238 RIGLDLPFPIKINQML---GHQTSFLTYEGLVDQL 269
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-224 |
7.49e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.14 E-value: 7.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTmekkGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnKNLKK 82
Cdd:COG3638 3 LELRNLSKRYPGGTP----ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG-RALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ-FPetqLFEN-TVLEDVKFG-----------PKNFGVSDKEAEIKAkkwLKQVGL------PTDvisksp 143
Cdd:COG3638 78 LRRRIGMIFQqFN---LVPRlSVLTNVLAGrlgrtstwrslLGLFPPEDRERALEA---LERVGLadkayqRAD------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 144 fELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGK 222
Cdd:COG3638 146 -QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
..
gi 323465851 223 LI 224
Cdd:COG3638 225 VV 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-237 |
1.26e-46 |
|
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: 156.06 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLmqhFNAL---LKPSSGTIDIAGYHITpqtGNKNLKKLRKEVGLVFQFPetQLF 99
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTL---FNLIsgfLRPTSGSVLFDGEDIT---GLPPHEIARLGIGRTFQIP--RLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 EN-TVLEDV--------KFGPKNFGVSDKEAEI--KAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILC 168
Cdd:cd03219 88 PElTVLENVmvaaqartGSGLLLARARREEREAreRAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 169 LDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKE 237
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-243 |
2.68e-46 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 155.53 E-value: 2.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:TIGR02315 2 LEVENLSKVYPNG----KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDIT-KLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDV---KFGPKN-----FGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRR 153
Cdd:TIGR02315 77 LRRRIGMIFQ--HYNLIERlTVLENVlhgRLGYKPtwrslLGRFSEEDKERALSALERVGL-ADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 154 VAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKI 232
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
250
....*....|.
gi 323465851 233 feNKEWLKKHY 243
Cdd:TIGR02315 234 --DDEVLRHIY 242
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-223 |
3.43e-46 |
|
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: 152.94 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgNKNLKK 82
Cdd:cd03230 1 IEVRNLSKRYG-----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-----KKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKfgpknfgvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAIAGVMV 161
Cdd:cd03230 71 VKRRIGYLPE--EPSLYENlTVRENLK-------------------------------------LSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-233 |
3.46e-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: 154.97 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqTGNKNLKKLRKEVGLVFQFPetQL 98
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISG-LSEAELYRLRRRMGMLFQSG--AL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FEN-TVLEDVKFgP--KNFGVSDKEAEIKAKKWLKQVGLPTDViSKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:cd03261 89 FDSlTVFENVAF-PlrEHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 176 LDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-226 |
6.74e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 6.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYspGTTmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYH--ITPQTGNK 78
Cdd:PRK11124 1 MSIQLNGINCFY--GAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLRKEVGLVFQfpETQLFEN-TVLEDVKFGP-KNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAI 156
Cdd:PRK11124 76 AIRELRRNVGMVFQ--QYNLWPHlTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKH 226
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-226 |
6.82e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 6.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYspGTTmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYH--ITPQTGNK 78
Cdd:COG4161 1 MSIQLKNINCFY--GSH---QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLRKEVGLVFQfpETQLFEN-TVLEDVKFGP-KNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAI 156
Cdd:COG4161 76 AIRLLRQKVGMVFQ--QYNLWPHlTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKH 226
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-224 |
7.95e-46 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 154.26 E-value: 7.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnKNLKK 82
Cdd:cd03256 1 IEVENLSKTYPNG----KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG-KALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDV---KFGPKN-----FGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRR 153
Cdd:cd03256 76 LRRQIGMIFQ--QFNLIERlSVLENVlsgRLGRRStwrslFGLFPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 154 VAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-260 |
9.02e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 157.23 E-value: 9.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG----YHITPQTg 76
Cdd:COG1118 1 MSIEVRNISKRFG-----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlfTNLPPRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 77 nknlkklRKeVGLVFQFPetQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVA 155
Cdd:COG1118 75 -------RR-VGFVFQHY--ALFPHmTVAENIAFGLRVRPPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
250 260
....*....|....*....|....*.
gi 323465851 235 NkewlkkhyldePtPSLFASSLTGFK 260
Cdd:COG1118 224 R-----------P-ATPFVARFLGCV 237
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
1.19e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.66 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTI-----DIAGYHITpqtgn 77
Cdd:COG4619 1 LELEGLSFRVG-----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMPPP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 knlkKLRKEVGLVFQfpETQLFENTVLEDVKFGPKNFGVSDKEAeiKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIA 157
Cdd:COG4619 71 ----EWRRQVAYVPQ--EPALWGGTVRDNLPFPFQLRERKFDRE--RALELLERLGLPPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 158 GVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-245 |
1.55e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 153.47 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnKNLKK 82
Cdd:COG4555 2 IEVENLSKKYG-----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-----KEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPEtqLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG4555 72 ARRQIGVLPDERG--LYDRlTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE--NKEWL 239
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeiGEENL 228
|
....*.
gi 323465851 240 KKHYLD 245
Cdd:COG4555 229 EDAFVA 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-223 |
2.85e-45 |
|
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: 152.18 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTmekkGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnLKK 82
Cdd:cd03292 1 IEFINVTKTYPNGTA----ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-IPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:cd03292 76 LRRKIGVVFQ--DFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-222 |
3.06e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 150.09 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 4 KFENINYIYspgttMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKL 83
Cdd:cd00267 1 EIENLSFRY-----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 RKEVGLVFQfpetqlfentvledvkfgpknfgvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAIAGVMVNE 163
Cdd:cd00267 72 RRRIGYVPQ-----------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 164 PQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGK 222
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-224 |
3.24e-45 |
|
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: 151.89 E-value: 3.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgNKNLKK 82
Cdd:cd03263 1 LQIRNLTKTYKKGT---KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFpeTQLFEN-TVLEDVKFgpknF----GVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIA 157
Cdd:cd03263 73 ARQSLGYCPQF--DALFDElTVREHLRF----YarlkGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 158 GVMVNEPQILCLDEPGAGLDPRAREEMMQIfVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDL-ILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-235 |
6.60e-45 |
|
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: 152.80 E-value: 6.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 22 GLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKKLR-KEVGLVFQ----FPet 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRELRrKKISMVFQsfalLP-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 qlfENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGL 176
Cdd:cd03294 116 ---HRTVLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 177 DPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:cd03294 192 DPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-229 |
6.99e-45 |
|
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: 153.70 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnKNLKKLRKEVGLVFQFPetQLFE 100
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV-----REPRKVRRSIGIVPQYA--SVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 N-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:TIGR01188 80 DlTGRENLEMMGRLYGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 323465851 180 AREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
23-243 |
2.06e-44 |
|
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: 150.96 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnKNLKKLR-----KEVGLVFQFPETQ 97
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG---------RDLASLSrrelaRRIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 lFENTVLEDVKFG--P--KNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:COG1120 88 -FGLTVRELVALGryPhlGLFGRPSAEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 174 AGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFeNKEWLKKHY 243
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-TPELLEEVY 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-222 |
2.26e-44 |
|
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: 148.30 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKK 82
Cdd:cd03228 1 IEFKNVSFSYPGR---PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR----DLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVkfgpknfgvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAIAGVMVN 162
Cdd:cd03228 74 LRKNIAYVPQ--DPFLFSGTIRENI--------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNMDDVaKYADDVLVMEHGK 222
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-223 |
5.20e-44 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 148.84 E-value: 5.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 4 KFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnKNLKKL 83
Cdd:cd03235 1 EVEDLTVSYG-----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---------KPLEKE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 RKEVGLVFQFPET-QLFENTVLEDVKFGP-------KNFGVSDKEAEIKAkkwLKQVGLpTDVISKSPFELSGGQMRRVA 155
Cdd:cd03235 67 RKRIGYVPQRRSIdRDFPISVRDVVLMGLyghkglfRRLSKADKAKVDEA---LERVGL-SELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-235 |
5.59e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.49 E-value: 5.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNAL--LKPS---SGTIDIAGYHI-TPQTg 76
Cdd:COG1117 12 IEVRNLNVYYG-----DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIyDPDV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 77 nkNLKKLRKEVGLVFQ----FPETqLFENtvledVKFGPKNFGVSDKE--AEIkAKKWLKQVGLPTDV---ISKSPFELS 147
Cdd:COG1117 86 --DVVELRRRVGMVFQkpnpFPKS-IYDN-----VAYGLRLHGIKSKSelDEI-VEESLRKAALWDEVkdrLKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR---EEMMQIFvnyqKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTakiEELILEL----KKDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250
....*....|.
gi 323465851 225 KHDKPRKIFEN 235
Cdd:COG1117 233 EFGPTEQIFTN 243
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-224 |
6.79e-43 |
|
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: 146.87 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtgnKNLKK 82
Cdd:COG1124 2 LEVRNLSVSYGQGGR-RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLfeN---TVLEDVKFGPKNFGVSDKEAEIKakKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGV 159
Cdd:COG1124 77 FRRRVQMVFQDPYASL--HprhTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-237 |
9.80e-43 |
|
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: 146.72 E-value: 9.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLmqhFNAL---LKPSSGTIDIAGYHITPQTGNKnlkklRKEVGLV--FQfpETQ 97
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTL---FNLItgfYRPTSGRILFDGRDITGLPPHR-----IARLGIArtFQ--NPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFEN-TVLEDVK---------------FGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG0411 90 LFPElTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGL-ADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKE 237
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-235 |
2.26e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.92 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnKNLKK 82
Cdd:COG1135 2 IELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE-RELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ-FpetQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:COG1135 80 ARRKIGMIFQhF---NLLSSrTVAENVALPLEIAGVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDP-----------RAREEMmqifvnyqkaGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:COG1135 156 ANNPKVLLCDEATSALDPettrsildllkDINREL----------GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
....*.
gi 323465851 230 RKIFEN 235
Cdd:COG1135 226 LDVFAN 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-273 |
5.14e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 145.62 E-value: 5.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnkNLKK 82
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQ--LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE----NVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK13642 79 LRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGH-TVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
250 260 270
....*....|....*....|....*....|....
gi 323465851 242 HYLDEPTPSLFASSL--TGFKFKENPLTIKELVD 273
Cdd:PRK13642 237 IGLDVPFSSNLMKDLrkNGFDLPEKYLSEDELVE 270
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-226 |
1.60e-41 |
|
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: 142.33 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELlDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnKNLKK 82
Cdd:cd03264 1 LQLENLTKRYG-----KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-----KQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:cd03264 70 LRRRIGYLPQ--EFGVYPNfTVREFLDYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNyQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKH 226
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
1.05e-40 |
|
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: 147.98 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNALL---KPSSGTIDIAGYHITpqtgNK 78
Cdd:COG4988 336 SIELEDVSFSYPGG----RPALDGLSLTIPPGERVALVGPSGAGKSTLL---NLLLgflPPYSGSILINGVDLS----DL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLRKEVGLVFQFPetQLFENTVLEDVKFGpkNFGVSDkeAEIKAkkWLKQVGLpTDVISKSP-----------FELS 147
Cdd:COG4988 405 DPASWRRQIAWVPQNP--YLFAGTIRENLRLG--RPDASD--EELEA--ALEAAGL-DEFVAALPdgldtplgeggRGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYqKAGHTVILVTHNMDDVAKyADDVLVMEHGKLI 224
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-172 |
1.31e-40 |
|
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: 137.78 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKKLRKEVGLVFQFPetQLF-EN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDP--QLFpRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 102 TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLP---TDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
3.76e-40 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 148.06 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLK 81
Cdd:COG2274 473 DIELENVSFRYPGD---SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR----QIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAeIKAkkwLKQVGLpTDVISKSP--FE---------LSGGQ 150
Cdd:COG2274 546 SLRRQIGVVLQ--DVFLFSGTIRENITLG--DPDATDEEI-IEA---ARLAGL-HDFIEALPmgYDtvvgeggsnLSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQiFVNYQKAGHTVILVTHNMdDVAKYADDVLVMEHGKLI 224
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILE-NLRRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-229 |
4.72e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 139.46 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTmekkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqTGNKNLKK 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQV-----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ----FPetQLfenTVLEDVKFGPKNF-GVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIA 157
Cdd:PRK09493 75 IRQEAGMVFQqfylFP--HL---TALENVMFGPLRVrGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 158 GVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKlIKHDKP 229
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR-IAEDGD 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-225 |
2.36e-39 |
|
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: 135.64 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 6 ENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKLRK 85
Cdd:cd03214 3 ENLSVGYG-----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----SLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 86 EVGLVFQfpetqlfentvledvkfgpknfgvsdkeaeikakkWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQ 165
Cdd:cd03214 74 KIAYVPQ-----------------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 166 ILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIK 225
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-235 |
1.21e-38 |
|
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: 135.44 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkk 82
Cdd:cd03300 1 IELENVSKFYG-----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 lrKEVGLVFQ----FPETQLFENtvledVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAG 158
Cdd:cd03300 72 --RPVNTVFQnyalFPHLTVFEN-----IAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 159 VMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-235 |
1.45e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 138.28 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNA---LLKPSSGTIDIAGYHIT---PQt 75
Cdd:COG3839 3 SLELENVSKSYG-----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLL---RMiagLEDPTSGEILIGGRDVTdlpPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 76 gnknlkklRKEVGLVFQFPetQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRV 154
Cdd:COG3839 74 --------DRNIAMVFQSY--ALYPHmTVYENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 155 AIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELY 222
|
..
gi 323465851 234 EN 235
Cdd:COG3839 223 DR 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-224 |
2.77e-38 |
|
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: 133.54 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 6 ENINYIYSPGTTMekkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgnkNLKKLRK 85
Cdd:cd03226 3 ENISFSYKKGTEI----LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-------KAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 86 EVGLVFQFPETQLFENTVLEDVKFGPKNFGvsdkEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQ 165
Cdd:cd03226 72 SIGYVMQDVDYQLFTDSVREELLLGLKELD----AGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 166 ILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-247 |
3.11e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 135.52 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLdNISFELldNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpQTGNKNLKKLRKEVGLVFQFPETQLFE 100
Cdd:PRK13638 18 KGL-NLDFSL--SPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKRGLLALRQQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 NTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGlpTDVISKSPFE-LSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD--AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 180 AREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKKHYLDEP 247
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQP 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-235 |
3.57e-38 |
|
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: 134.39 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNL 80
Cdd:cd03296 1 MSIEVRNVSKRFG-----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT------DV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDK--EAEIKAK--KWLKQVGLpTDVISKSPFELSGGQMRRVA 155
Cdd:cd03296 70 PVQERNVGFVFQ--HYALFRHmTVFDNVAFGLRVKPRSERppEAEIRAKvhELLKLVQL-DWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
.
gi 323465851 235 N 235
Cdd:cd03296 227 H 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-246 |
6.31e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 134.35 E-value: 6.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 15 GTTMEKKGL---DNISFELLDNSFIALIGHTGSGKSTLmqhFNAL---LKPSSGTIDIAGYHITPQTGNKNLKKlrkevG 88
Cdd:PRK11300 10 GLMMRFGGLlavNNVNLEVREQEIVSLIGPNGAGKTTV---FNCLtgfYKPTGGTILLRGQHIEGLPGHQIARM-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 89 LVFQFPETQLF-ENTVLED--------VK-------FGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMR 152
Cdd:PRK11300 82 VVRTFQHVRLFrEMTVIENllvaqhqqLKtglfsglLKTPAFRRAESEALDRAATWLERVGL-LEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 153 RVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRK 231
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|....*
gi 323465851 232 IFENKEWLKKhYLDE 246
Cdd:PRK11300 241 IRNNPDVIKA-YLGE 254
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-241 |
1.13e-37 |
|
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: 139.90 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnknlK 81
Cdd:COG4987 333 SLELEDVSFRY-PGA--GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE----D 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAeIKAkkwLKQVGLpTDVISKSP-----------FELSGGQ 150
Cdd:COG4987 406 DLRRRIAVVPQ--RPHLFDTTLRENLRLA--RPDATDEEL-WAA---LERVGL-GDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPR 230
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHE 554
|
250
....*....|.
gi 323465851 231 KIFENKEWLKK 241
Cdd:COG4987 555 ELLAQNGRYRQ 565
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-236 |
9.88e-37 |
|
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: 130.42 E-value: 9.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKK 82
Cdd:cd03254 3 IEFENVNFSYDEK----KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS----RKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGPKNfgvSDKEAEIKAkkwLKQVGLpTDVISKSP-----------FELSGGQM 151
Cdd:cd03254 75 LRSMIGVVLQ--DTFLFSGTIMENIRLGRPN---ATDEEVIEA---AKEAGA-HDFIMKLPngydtvlgengGNLSQGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 152 RRVAIAGVMVNEPQILCLDEPGAGLDPRArEEMMQIFVNYQKAGHTVILVTHNMDDVaKYADDVLVMEHGKLIKHDKPRK 231
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTET-EKLIQEALEKLMKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDE 223
|
....*
gi 323465851 232 IFENK 236
Cdd:cd03254 224 LLAKK 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-229 |
9.90e-37 |
|
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: 130.18 E-value: 9.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnKNLKK 82
Cdd:cd03265 1 IEVENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFP--ETQLfenTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:cd03265 71 VRRRIGIVFQDLsvDDEL---TGWENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-235 |
1.54e-36 |
|
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: 130.15 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQ----FPETQL 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT------NLPPEKRDISYVPQnyalFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FENtvledVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDP 178
Cdd:cd03299 89 YKN-----IAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 179 RAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:cd03299 163 RTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
19-216 |
3.66e-36 |
|
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: 128.12 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQfpETQL 98
Cdd:TIGR03608 10 DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQ--NFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDvISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:TIGR03608 88 IENeTVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLK-LKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 323465851 178 PRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVL 216
Cdd:TIGR03608 167 PKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVI 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-227 |
5.23e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.29 E-value: 5.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnaLL----KPSSGTIDIAGYHITpqtgN 77
Cdd:COG1132 339 EIEFENVSFSYPG----DRPVLKDISLTIPPGETVALVGPSGSGKSTLVN----LLlrfyDPTSGRILIDGVDIR----D 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 KNLKKLRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDkeAEIKAkkWLKQVGLpTDVISKSPF-----------EL 146
Cdd:COG1132 407 LTLESLRRQIGVVPQ--DTFLFSGTIRENIRYG--RPDATD--EEVEE--AAKAAQA-HEFIEALPDgydtvvgergvNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 147 SGGQMRRVAIAGVMVNEPQILCLDEPGAGLDP-------RAREEMMQifvnyqkaGHTVILVTHNMDDVAKyADDVLVME 219
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTetealiqEALERLMK--------GRTTIVIAHRLSTIRN-ADRILVLD 548
|
250
....*....|.
gi 323465851 220 HGKLI---KHD 227
Cdd:COG1132 549 DGRIVeqgTHE 559
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-235 |
1.21e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 128.35 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNAL--LKPS---SGTIDIAGYHI-TPQTgnkNLKKLRKEVGLVFQ 92
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIySPRT---DTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 FPETqlFENTVLEDVKFGPKNFGVSDKEAEIKA-KKWLKQVGLPTDV---ISKSPFELSGGQMRRVAIAGVMVNEPQILC 168
Cdd:PRK14239 94 QPNP--FPMSIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIWDEVkdrLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 169 LDEPGAGLDPRAREEMMQIFVNYqKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-235 |
1.63e-35 |
|
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: 129.79 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTL----MQhfnaLLKP---SSGTIDIAGYHITPQTGnKNLKKLR-KEVGLVFQFP 94
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLaraiLG----LLPPpgiTSGEILFDGEDLLKLSE-KELRKIRgREIQMIFQDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ETQLfeN---TVLEDVKFGPKNF-GVSDKEAEIKAKKWLKQVGL--PTDVISKSPFELSGGQMRRVAIAGVMVNEPQILC 168
Cdd:COG0444 96 MTSL--NpvmTVGDQIAEPLRIHgGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 169 LDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-224 |
3.36e-35 |
|
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: 125.86 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnLKK 82
Cdd:cd03269 1 LEVENVTKRFG-----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-IGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLvfqFPETQLFENTV-LEDVKfgpknfGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:cd03269 75 LPEERGL---YPKMKVIDQLVyLAQLK------GLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-233 |
9.06e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 9.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTTMekkgldNISFELLDNSFIALIGHTGSGKSTLmqhFNAL---LKPSSGTIDIAGYHITPQTGNKn 79
Cdd:COG3840 2 LRLDDLTYRY-GDFPL------RFDLTIAAGERVAILGPSGAGKSTL---LNLIagfLPPDSGRILWNGQDLTALPPAE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 lkklRKeVGLVFQfpETQLFEN-TVLEDVKFG--PK-NFGVSDKEAEIKAkkwLKQVGLpTDVISKSPFELSGGQMRRVA 155
Cdd:COG3840 71 ----RP-VSMLFQ--ENNLFPHlTVAQNIGLGlrPGlKLTAEQRAQVEQA---LERVGL-AGLLDRLPGQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIfVN--YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDL-VDelCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-224 |
9.33e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.99 E-value: 9.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:PRK11153 2 IELKNISKVF-PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT-ALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ-FpeTQLFENTVLEDVKFGPKNFGVSdkEAEIKAK--KWLKQVGLpTDVISKSPFELSGGQMRRVAIAGV 159
Cdd:PRK11153 80 ARRQIGMIFQhF--NLLSSRTVFDNVALPLELAGTP--KAEIKARvtELLELVGL-SDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIF--VNyQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLkdIN-RELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-235 |
7.04e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.71 E-value: 7.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHIT---PQTGNKNL-KKLRKEVGLVFQ----FP 94
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarSLSQQKGLiRQLRQHVGFVFQnfnlFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 EtqlfeNTVLEDVKFGPKNF-GVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:PRK11264 99 H-----RTVLENIIEGPVIVkGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-235 |
1.44e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.16 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHIT---------PQTGNKNLKKLRKEVGL 89
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 90 VFQfpETQLFEN-TVLEDVKFGP-KNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQIL 167
Cdd:PRK10619 97 VFQ--HFNLWSHmTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 168 CLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-225 |
1.61e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 121.63 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLD---NISFELlDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQfpE 95
Cdd:cd03297 7 EKRLPDftlKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQ--Q 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TQLFEN-TVLEDVKFGPKnfGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:cd03297 84 YALFPHlNVRENLAFGLK--RKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 175 GLDPRAREEMM----QIFVNYQKaghTVILVTHNMDDVAKYADDVLVMEHGKLIK 225
Cdd:cd03297 161 ALDRALRLQLLpelkQIKKNLNI---PVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
23-224 |
2.98e-33 |
|
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: 121.39 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtGNKN-LKKLRKE-VGLVFQ-FpetQLF 99
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LDEDaRARLRARhVGFVFQsF---QLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 EN-TVLEDVkfgpknfGV-----SDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:COG4181 103 PTlTALENV-------MLplelaGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 323465851 174 AGLDPRAREEMMQ-IFVNYQKAGHTVILVTHNMDDvAKYADDVLVMEHGKLI 224
Cdd:COG4181 175 GNLDAATGEQIIDlLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRAGRLV 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-234 |
4.16e-33 |
|
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: 123.37 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 38 LIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQ----FPETQLFENtvledVKFGPKN 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQsyalFPHMTVEEN-----VAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 114 FGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQ- 192
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQe 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 323465851 193 KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:TIGR01187 149 QLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-226 |
2.16e-32 |
|
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: 119.26 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKK 82
Cdd:cd03251 1 VEFKNVTFRYPGD---GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT----LAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAEIKAKkwlkqVGLPTDVISKSP-----------FELSGGQM 151
Cdd:cd03251 74 LRRQIGLVSQ--DVFLFNDTVAENIAYG--RPGATREEVEEAAR-----AANAHEFIMELPegydtvigergVKLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 152 RRVAIAGVMVNEPQILCLDEPGAGLDPRArEEMMQIFVNYQKAGHTVILVTHNMDDVaKYADDVLVMEHGKLIKH 226
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTES-ERLVQAALERLMKNRTTFVIAHRLSTI-ENADRIVVLEDGKIVER 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-223 |
3.02e-32 |
|
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: 118.13 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKK 82
Cdd:cd03301 1 VELENVTKRFG-----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT------DLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQ----FPETQLFENtvledVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAG 158
Cdd:cd03301 70 KDRDIAMVFQnyalYPHMTVYDN-----IAFGLKLRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 159 VMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-224 |
3.11e-32 |
|
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: 119.03 E-value: 3.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSG-TIDIAGYhitpQTGNKNLK 81
Cdd:COG1119 4 LELRNVTVRRG-----GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE----RRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLV-----FQFPETQlfenTVLEDV---KFG----PKNFGVSDKEaeiKAKKWLKQVGLpTDVISKSPFELSGG 149
Cdd:COG1119 75 ELRKRIGLVspalqLRFPRDE----TVLDVVlsgFFDsiglYREPTDEQRE---RARELLELLGL-AHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 150 QMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQiFVNY--QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLA-LLDKlaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
3.42e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.58 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MS-IKFENINYIYsPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHIT-PQTgnk 78
Cdd:COG4525 1 MSmLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPGA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 nlkklrkEVGLVFQ----FPETqlfenTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRV 154
Cdd:COG4525 77 -------DRGVVFQkdalLPWL-----NVLDNVAFGLRLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 155 AIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVM 218
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDvWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-223 |
4.29e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.05 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:PRK10908 2 IRFEHVSKAYLGG----RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT-RLKNREVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PRK10908 77 LRRQIGMIFQ-DHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-224 |
5.88e-32 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 118.10 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKK 82
Cdd:cd03253 1 IEFENVTFAYDPG----RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR----EVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAEIKAKKwlKQVGlptDVISKSPF-----------ELSGGQM 151
Cdd:cd03253 73 LRRAIGVVPQ--DTVLFNDTIGYNIRYG--RPDATDEEVIEAAKA--AQIH---DKIMRFPDgydtivgerglKLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 152 RRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFvNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLI 224
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAAL-RDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-224 |
6.65e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.44 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkklrkeVGLVfqfPETQ- 97
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR--------IGYL---PEERg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFEN-TVLEDVKFgpknF----GVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:COG4152 82 LYPKmKVGEQLVY----LarlkGLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 323465851 173 GAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-231 |
9.30e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 123.68 E-value: 9.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKKLRKE-VGLVFQfpETQLFEN 101
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA-TLDADALAQLRREhFGFIFQ--RYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 -TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRA 180
Cdd:PRK10535 101 lTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 323465851 181 REEMMQIFVNYQKAGHTVILVTHNmDDVAKYADDVLVMEHGKLIKHDKPRK 231
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-226 |
1.27e-31 |
|
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: 116.11 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINY-IYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNAL-----LKPSSGTIDIAGYHITPQ 74
Cdd:cd03213 2 VTLSFRNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLL---NALagrrtGLGVSGEVLINGRPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 75 TgnknlkkLRKEVGLVFQfpETQLFEN-TVLEDVKFGpknfgvsdkeAEIKAkkwlkqvglptdviskspfeLSGGQMRR 153
Cdd:cd03213 79 S-------FRKIIGYVPQ--DDILHPTlTVRETLMFA----------AKLRG--------------------LSGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 154 VAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNM-DDVAKYADDVLVMEHGKLIKH 226
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYF 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-237 |
1.79e-31 |
|
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: 116.87 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPgTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnaLLK----PSSGTIDIAGYHITpqtgNK 78
Cdd:cd03249 1 IEFKNVSFRY-P-SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVS----LLErfydPTSGEILLDGVDIR----DL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAEIKAKKwlkqvGLPTDVISKSP-----------FELS 147
Cdd:cd03249 71 NLRWLRSQIGLVSQ--EPVLFDGTIAENIRYG--KPDATDEEVEEAAKK-----ANIHDFIMSLPdgydtlvgergSQLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLDpRAREEMMQIFVNYQKAGHTVILVTHNMDDVaKYADDVLVMEHGKLIKHD 227
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALD-AESEKLVQEALDRAMKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
250
....*....|
gi 323465851 228 KPRKIFENKE 237
Cdd:cd03249 220 THDELMAQKG 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-229 |
3.51e-31 |
|
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: 115.67 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGnknLK 81
Cdd:cd03244 2 DIEFKNVSLRYRPN---LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIG---LH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQfpETQLFENTVLEDVkfGPknFGVSDKEAEIKAkkwLKQVGLpTDVISKSPFEL-----------SGGQ 150
Cdd:cd03244 75 DLRSRISIIPQ--DPVLFSGTIRSNL--DP--FGEYSDEELWQA---LERVGL-KEFVESLPGGLdtvveeggenlSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPrAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYaDDVLVMEHGKLIKHDKP 229
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDP-ETDALIQKTIREAFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-225 |
3.87e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.83 E-value: 3.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKG----LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNK 78
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFGAKQrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY-QLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAK--KWLKQVGLPTDVISKSPFELSGGQMRRVAI 156
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARiaELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTV-ILVTHNMDDVAKYADDVLVMEHGKLIK 225
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
1.46e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.18 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLmqhFNAL---LKPSSGTIDIAGYHITpqtgnkN 79
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTL---LNAIagsLPPDSGSILIDGKDVT------K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 LKKLR--KEVGLVFQ------FPETQLFENTVLEDVKFGPKNF--GVSDKEAEIkAKKWLKQVGL-----PTDVISKspf 144
Cdd:COG1101 73 LPEYKraKYIGRVFQdpmmgtAPSMTIEENLALAYRRGKRRGLrrGLTKKRREL-FRELLATLGLglenrLDTKVGL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 145 eLSGGQmrRVAIAGVM--VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGH-TVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:COG1101 149 -LSGGQ--RQALSLLMatLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEG 225
|
...
gi 323465851 222 KLI 224
Cdd:COG1101 226 RII 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-224 |
1.54e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 112.79 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKK 82
Cdd:cd03247 1 LSINNVSFSYPEQ---EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS------DLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 -LRKEVGLVFQFPetQLFENTVLEDVkfgpknfgvsdkeaeikakkwlkqvGLPtdviskspfeLSGGQMRRVAIAGVMV 161
Cdd:cd03247 72 aLSSLISVLNQRP--YLFDTTLRNNL-------------------------GRR----------FSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNMDDVaKYADDVLVMEHGKLI 224
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGI-EHMDKILFLENGKII 175
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-218 |
1.74e-30 |
|
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: 119.31 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYsPGTTmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnkNLK 81
Cdd:TIGR02857 321 SLEFSGVSVAY-PGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA----DAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPetQLFENTVLEDVKFGPKnfGVSDkeAEIKAKkwLKQVGLPTDV----------ISKSPFELSGGQM 151
Cdd:TIGR02857 393 SWRDQIAWVPQHP--FLFAGTIAENIRLARP--DASD--AEIREA--LERAGLDEFVaalpqgldtpIGEGGAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 152 RRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNmDDVAKYADDVLVM 218
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHR-LALAALADRIVVL 529
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-235 |
2.84e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 114.13 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGldnISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGN---------KNLKKLRKEVGLVF 91
Cdd:COG4598 25 KG---VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadrRQLQRIRTRLGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 92 Q-FpetqlfeN-----TVLEDVKFGPKN-FGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVAIAGVMVNEP 164
Cdd:COG4598 102 QsF-------NlwshmTVLENVIEAPVHvLGRPKAEAIERAEALLAKVGLA-DKRDAYPAHLSGGQQQRAAIARALAMEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 165 QILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMD---DVakyADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG4598 174 EVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGfarDV---SSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-224 |
3.80e-30 |
|
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: 113.20 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYhiTPQtgnKNLKKLRKEVGLVF-QfpETQ 97
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL--VPW---KRRKKFLRRIGVVFgQ--KTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGL 176
Cdd:cd03267 106 LWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 323465851 177 DPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03267 185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-222 |
1.08e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.42 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNknlkkLRKEVGLVFqfPETQLFEN- 101
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----YRRRLAYLG--HADGLKPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFGPKNFGVSDKEAEIKAkkWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR 181
Cdd:COG4133 91 TVRENLRFWAALYGLRADREAIDE--ALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 323465851 182 EEMMQIFVNYQKAGHTVILVTHnmDDVAKYADDVLVMEHGK 222
Cdd:COG4133 168 ALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-224 |
1.87e-29 |
|
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: 109.44 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhiTPQTGNKNLKK 82
Cdd:cd03216 1 LELRGITKRF-GGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpetqlfentvledvkfgpknfgvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAIAGVMVN 162
Cdd:cd03216 73 RRAGIAMVYQ-----------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-223 |
2.60e-29 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 110.58 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 17 TMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQ---- 92
Cdd:NF038007 15 TIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQsfnl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 FPETQLFENTVLedvkfgP-KNFGVSDKEAEIKAKKWLKQVGLPTDVISKsPFELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:NF038007 95 IPHLSIFDNVAL------PlKYRGVAKKERIERVNQVLNLFGIDNRRNHK-PMQLSGGQQQRVAIARAMVSNPALLLADE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 323465851 172 PGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNmDDVAKYADDVLVMEHGKL 223
Cdd:NF038007 168 PTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-234 |
2.71e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.27 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQ----FPE 95
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT------HVPAENRHVNTVFQsyalFPH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TQLFENtvledVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:PRK09452 101 MTVFEN-----VAFGLRMQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 176 LDPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:PRK09452 175 LDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-224 |
2.87e-29 |
|
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: 110.76 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPgttMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHIT---PQTgnk 78
Cdd:cd03245 2 RIEFRNVSFSYPN---QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqldPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 nlkkLRKEVGLVFQfpETQLFENTVLEDVKFGpknFGVSDKEAEIKAkkwLKQVGLpTDVISKSP-----------FELS 147
Cdd:cd03245 76 ----LRRNIGYVPQ--DVTLFYGTLRDNITLG---APLADDERILRA---AELAGV-TDFVNKHPngldlqigergRGLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYqKAGHTVILVTH--NMDDVakyADDVLVMEHGKLI 224
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHrpSLLDL---VDRIIVMDSGRIV 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-235 |
3.61e-29 |
|
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: 115.55 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 16 TTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnALLK--PSSGTIDIAGYHITPQTGnKNLKKLRKEVGLVFQF 93
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGL---ALLRliPSEGEIRFDGQDLDGLSR-RALRPLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 PetqlF---------ENTVLEDVKF-GPknfGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNE 163
Cdd:COG4172 371 P----FgslsprmtvGQIIAEGLRVhGP---GLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 164 PQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
4.92e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.09 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYspGTTMEKKGLDnisFELLDNSFIALIGHTGSGKSTLMQHFNALLKPS-----SGTIDIAGYHITPQtg 76
Cdd:PRK14267 4 AIETVNLRVYY--GSNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 77 NKNLKKLRKEVGLVFQFPETqlFEN-TVLEDVKFGPKNFGVSDKEAEIKAK-KW-LKQVGLPTDV---ISKSPFELSGGQ 150
Cdd:PRK14267 77 DVDPIEVRREVGMVFQYPNP--FPHlTIYDNVAIGVKLNGLVKSKKELDERvEWaLKKAALWDEVkdrLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAgHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPR 230
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
....*..
gi 323465851 231 KIFENKE 237
Cdd:PRK14267 234 KVFENPE 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-229 |
7.61e-29 |
|
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: 109.45 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkKLRKEVGLVfqfPET-QLFEN 101
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE---RARAGIGYV---PEGrRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 -TVLEDVKFGPKNFGVSDKEAEIKA--------KKWLKQVGlptdviskspFELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:cd03224 90 lTVEENLLLGAYARRRAKRKARLERvyelfprlKERRKQLA----------GTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 173 GAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-223 |
1.05e-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: 107.69 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnkNLKK 82
Cdd:cd03246 1 LEVENVSFRY-PGA--EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW----DPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVkfgpknfgvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAIAGVMVN 162
Cdd:cd03246 74 LGDHVGYLPQ--DDELFSGSIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVLVMEHGKL 223
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-235 |
1.22e-28 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 114.40 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKS----TLMQhfnaLLKPS----SGTIDIAGYHITpQTGNKNLKKLR-KEVGLVFQF 93
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILR----LLPDPaahpSGSILFDGQDLL-GLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 P----------ETQLFEntVLEdvkfgpKNFGVSDKEAEIKAKKWLKQVGLPTDV--ISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG4172 101 PmtslnplhtiGKQIAE--VLR------LHRGLSGAAARARALELLERVGIPDPErrLDAYPHQLSGGQRQRVMIAMALA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG4172 173 NEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-224 |
1.34e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 114.56 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 11 IYSP-GTTMekkgLDNISFELLDNSFIALIGHTGSGKSTLMqhfNALLK--PSSGTIDIAGYHITpqtgNKNLKKLRKEV 87
Cdd:PRK11174 357 ILSPdGKTL----AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIELR----ELDPESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 88 GLVFQFPetQLFENTVLEDVKFGPKNfgVSDKE-----AEIKAKKWLKQV--GLPTdVISKSPFELSGGQMRRVAIAGVM 160
Cdd:PRK11174 426 SWVGQNP--QLPHGTLRDNVLLGNPD--ASDEQlqqalENAWVSEFLPLLpqGLDT-PIGDQAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIfVNYQKAGHTVILVTHNMDDVAKYaDDVLVMEHGKLI 224
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQA-LNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-227 |
1.62e-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: 109.11 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtGNKNLKK 82
Cdd:cd03252 1 ITFEHVRFRYKPD---GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL----ALADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAEIKAK-----KWLKQVGLPTD-VISKSPFELSGGQMRRVAI 156
Cdd:cd03252 74 LRRQVGVVLQ--ENVLFNRSIRDNIALA--DPGMSMERVIEAAKlagahDFISELPEGYDtIVGEQGAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQifvNYQK--AGHTVILVTHNMDDVaKYADDVLVMEHGKLI---KHD 227
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMR---NMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVeqgSHD 221
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-230 |
1.66e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 114.58 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYsPGttMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGY---HITPQTgnk 78
Cdd:TIGR03375 463 EIEFRNVSFAY-PG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVdirQIDPAD--- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 nlkkLRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDkEAEIKAkkwLKQVGLpTDVISKSP--FE---------LS 147
Cdd:TIGR03375 537 ----LRRNIGYVPQ--DPRLFYGTLRDNIALG--APYADD-EEILRA---AELAGV-TEFVRRHPdgLDmqigergrsLS 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIfVNYQKAGHTVILVTHNMdDVAKYADDVLVMEHGKLIKhD 227
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDR-LKRWLAGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVA-D 680
|
...
gi 323465851 228 KPR 230
Cdd:TIGR03375 681 GPK 683
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
36-224 |
1.99e-28 |
|
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: 108.35 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQfpETQLFEN-TVLEDVKFGpKNF 114
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT------AAPPADRPVSMLFQ--ENNLFAHlTVEQNVGLG-LSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 115 GVSDKEAEIKA-KKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVN-YQ 192
Cdd:cd03298 98 GLKLTAEDRQAiEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlHA 176
|
170 180 190
....*....|....*....|....*....|..
gi 323465851 193 KAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
2.38e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.36 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSS-----GTIDIAGYHITPQtg 76
Cdd:PRK14258 7 AIKVNNLSFYYD-----TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYER-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 77 NKNLKKLRKEVGLVFqfPETQLFENTVLEDVKFGPKNFGVSDK-------EAEIKAKKWLKQVglpTDVISKSPFELSGG 149
Cdd:PRK14258 80 RVNLNRLRRQVSMVH--PKPNLFPMSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEI---KHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 150 QMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEH-----GKL 223
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQL 234
|
250
....*....|..
gi 323465851 224 IKHDKPRKIFEN 235
Cdd:PRK14258 235 VEFGLTKKIFNS 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-224 |
4.22e-28 |
|
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: 107.45 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgNKNLKKLRKEVGLVFQfpETQLFE 100
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-----VKEPAEARRRLGFVSD--STGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 N-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:cd03266 92 RlTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 323465851 180 AREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-232 |
4.48e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.56 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYspGTTmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNL 80
Cdd:PRK10851 1 MSIEIANIKKSF--GRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS------RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQfpETQLFEN-TVLEDVKFG----PKNFGVSDKEAEIKAKKWLKQVGLPtDVISKSPFELSGGQMRRVA 155
Cdd:PRK10851 70 HARDRKVGFVFQ--HYALFRHmTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKI 232
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-224 |
5.14e-28 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 106.92 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpQTGNKNLKKLRKeVGLVFQFPEtqL 98
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-----KSYQKNIEALRR-IGALIEAPG--F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FEN-TVLEDVKFGPKNFGVSDKEAEikakKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:cd03268 84 YPNlTARENLRLLARLLGIRKKRID----EVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 178 PRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-235 |
7.18e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.89 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 22 GLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQfPETQLFEN 101
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ-SFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR 181
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 182 EEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK10070 201 TEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-230 |
8.42e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG--YHIT-PQtgnknlKKLRKEVGLVFQ-FpetQL 98
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsPR------DAIALGIGMVHQhF---ML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FEN-TVLEDVKFG--PKNFGVSD-KEAEIKAKKWLKQVGL---PTDVISkspfELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:COG3845 92 VPNlTVAENIVLGlePTKGGRLDrKAARARIRELSERYGLdvdPDAKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 172 PGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPR 230
Cdd:COG3845 168 PTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-221 |
1.90e-27 |
|
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: 106.01 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLkklrkevgLVFQ----FPETQL 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRM--------VVFQnyslLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FENTVLEdVKFGPKNFGVSDKEAEIKAKkwLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDP 178
Cdd:TIGR01184 72 RENIALA-VDRVLPDLSKSERRAIVEEH--IALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 179 RAR----EEMMQIfvnYQKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:TIGR01184 148 LTRgnlqEELMQI---WEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-221 |
2.46e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 106.32 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhiTPQTGNKnlkklrKEVGLVFQfPETQLF 99
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---KPVEGPG------AERGVVFQ-NEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 ENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:PRK11248 84 WRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 323465851 180 AREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:PRK11248 163 TREQMQTLLLKlWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-235 |
3.09e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.90 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTL----MQhfnaLLKPSSGTIDIAGYHITPQTGnKNLKKLRKEVGLVFQFPET 96
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLgrllLR----LEEPTSGEILFDGQDITGLSG-RELRPLRRRMQMVFQDPYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 QLfeN---TVLEDVKFGPKNFGV-SDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:COG4608 107 SL--NprmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 173 GAGLDP--RAreemmQIfVNY-----QKAGHTVILVTHNMdDVAKY-ADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:COG4608 185 VSALDVsiQA-----QV-LNLledlqDELGLTYLFISHDL-SVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-235 |
3.32e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.40 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYspGTTMekkGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNAL--LKPS---SGTI-----DIAGYHIT 72
Cdd:PRK14243 11 LRTENLNVYY--GSFL---AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVtfhgkNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 73 PQtgnknlkKLRKEVGLVFQFPETqlFENTVLEDVKFGPKNFGVSDKEAEIkAKKWLKQVGLPTDVISK---SPFELSGG 149
Cdd:PRK14243 86 PV-------EVRRRIGMVFQKPNP--FPKSIYDNIAYGARINGYKGDMDEL-VERSLRQAALWDEVKDKlkqSGLSLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 150 QMRRVAIAGVMVNEPQILCLDEPGAGLDP---RAREEMMQIFvnyqKAGHTVILVTHNMDDVAKYAD-----DVLVME-- 219
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPistLRIEELMHEL----KEQYTIIIVTHNMQQAARVSDmtaffNVELTEgg 231
|
250
....*....|....*...
gi 323465851 220 --HGKLIKHDKPRKIFEN 235
Cdd:PRK14243 232 grYGYLVEFDRTEKIFNS 249
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
36-223 |
4.13e-27 |
|
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: 104.94 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNF 114
Cdd:TIGR01277 27 VAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT------GLAPYQRPVSMLFQ--ENNLFAHlTVRQNIGLGLHPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 115 GVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QK 193
Cdd:TIGR01277 99 LKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLcSE 177
|
170 180 190
....*....|....*....|....*....|
gi 323465851 194 AGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-223 |
5.52e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.53 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIdiagyhitpQTGNKNLKKLRKEVGLVFQfpETQL 98
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTAPLAEAREDTRLMFQ--DARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FE-NTVLEDVKFGPKNfgvSDKEAEIKAkkwLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK11247 93 LPwKKVIDNVGLGLKG---QWRDAALQA---LAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 178 PRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK11247 166 ALTRIEMQDLIESlWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-236 |
6.02e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.43 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItPQTGnknlKK 82
Cdd:PRK13537 8 IDFRNVEKRYG-----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRA----RH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQF----PETQLFENTVLedvkFGpKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPfELSGGQMRRVAIAG 158
Cdd:PRK13537 78 ARQRVGVVPQFdnldPDFTVRENLLV----FG-RYFGLSAAAARALVPPLLEFAKLENKADAKVG-ELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 159 VMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENK 236
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-224 |
6.32e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.95 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMqhfNAL---LKPSSGTIDIAG--YHI-TPQTGnknlkkLRKEVGLVFQfpET 96
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLM---KILsgvYQPDSGEILLDGepVRFrSPRDA------QAAGIAIIHQ--EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 QLFEN-TVLEDVKFG--PKNFG-VSDKEAEIKAKKWLKQVGL---PTDVISkspfELSGGQMRRVAIAGVMVNEPQILCL 169
Cdd:COG1129 89 NLVPNlSVAENIFLGrePRRGGlIDWRAMRRRARELLARLGLdidPDTPVG----DLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 170 DEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-235 |
9.47e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.59 E-value: 9.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKKLRKEVGLVFQFP------ 94
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL-KADPEAQKLLRQKIQIVFQNPygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ----ETQLFE----NTVLedvkfgpknfgvSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQI 166
Cdd:PRK11308 108 rkkvGQILEEplliNTSL------------SAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 167 LCLDEPGAGLDPRAREEMMQIFVNYQKAGHTV-ILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-244 |
9.72e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 104.29 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMqhfNA---LLKPSSGTIDIAGYHITPQTGNKnlkKLRKEVGLVfqfPET-QL 98
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLL---KAisgLLPPRSGSIRFDGEDITGLPPHR---IARLGIGYV---PEGrRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FEN-TVLEDVKFGPKNFGVSDKEAEIKA---------KKWLKQVGlptdviskspFELSGG--QMrrVAIAGVMVNEPQI 166
Cdd:COG0410 90 FPSlTVEENLLLGAYARRDRAEVRADLErvyelfprlKERRRQRA----------GTLSGGeqQM--LAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 167 LCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEwLKKHYL 244
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE-VREAYL 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-251 |
1.95e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYhiTPQtgnKNLKKLRKEVGLVF-QfpETQ 97
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY--VPF---KRRKEFARRIGVVFgQ--RSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFEN-TVLEDVKFGPKNFGVSDKEAeikaKKWLKQVglpTDVISKSPF------ELSGGQMRRVAIAGVMVNEPQILCLD 170
Cdd:COG4586 107 LWWDlPAIDSFRLLKAIYRIPDAEY----KKRLDEL---VELLDLGELldtpvrQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 171 EPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIkHDKP----RKIFENKEWLKKhYLD 245
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRII-YDGSleelKERFGPYKTIVL-ELA 257
|
....*.
gi 323465851 246 EPTPSL 251
Cdd:COG4586 258 EPVPPL 263
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-236 |
2.63e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknl 80
Cdd:PRK13536 40 VAIDLAGVSKSYG-----DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQLfENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPfELSGGQMRRVAIAGVM 160
Cdd:PRK13536 110 RLARARIGVVPQFDNLDL-EFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENK 236
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-221 |
2.66e-26 |
|
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: 102.90 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 22 GLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTI---------DIAgyHITPQTgnknLKKLRK-EVGLVF 91
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvDLA--QASPRE----ILALRRrTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 92 QF-------PETQLFENTVLEDvkfgpknfGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEP 164
Cdd:COG4778 100 QFlrviprvSALDVVAEPLLER--------GVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 165 QILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
3.19e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.60 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnaLL----KPSSGTIDIAGYHITpqtgN 77
Cdd:PRK11160 338 SLTLNNVSFTYPDQ---PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLtrawDPQQGEILLNGQPIA----D 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 KNLKKLRKEVGLVFQFPetQLFENTVLEDVKFGPKNfgvSDKEAEIKAkkwLKQVGLPTDVISKSPFE---------LSG 148
Cdd:PRK11160 407 YSEAALRQAISVVSQRV--HLFSATLRDNLLLAAPN---ASDEALIEV---LQQVGLEKLLEDDKGLNawlgeggrqLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 149 GQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNMDDVAKYaDDVLVMEHGKLI 224
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-204 |
3.77e-26 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 107.06 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkkLRKEVGLVFQFPetQLFENT 102
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE----VRRRVSVCAQDA--HLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFGPKNfgVSDKEAEIKAKK-----WLKQV--GLPTDVISKSPFeLSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:TIGR02868 425 VRENLRLARPD--ATDEELWAALERvgladWLRALpdGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180
....*....|....*....|....*....
gi 323465851 176 LDPRAREEMMQIfVNYQKAGHTVILVTHN 204
Cdd:TIGR02868 502 LDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-226 |
3.80e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 107.49 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKK 82
Cdd:TIGR02203 331 VEFRNVTFRY-PGR--DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT----LAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGPKNfGVSDKEAEIKAkkwlkQVGLPTDVISKSPF-----------ELSGGQM 151
Cdd:TIGR02203 404 LRRQVALVSQ--DVVLFNDTIANNIAYGRTE-QADRAEIERAL-----AAAYAQDFVDKLPLgldtpigengvLLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 152 RRVAIAGVMVNEPQILCLDEPGAGLDPR-------AREEMMQifvnyqkaGHTVILVTHNMDDVAKyADDVLVMEHGKLI 224
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNEserlvqaALERLMQ--------GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
..
gi 323465851 225 KH 226
Cdd:TIGR02203 547 ER 548
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-229 |
3.81e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.74 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpGTTMEkkgldnISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG--YHITPQTgnknl 80
Cdd:PRK10771 2 LKLTDITWLYH-HLPMR------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPPS----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 kklRKEVGLVFQfpETQLFEN-TVLEDVKFGpKNFGVS-DKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAG 158
Cdd:PRK10771 70 ---RRPVSMLFQ--ENNLFSHlTVAQNIGLG-LNPGLKlNAAQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 159 VMVNEPQILCLDEPGAGLDPRAREEMMQIF--VNYQKaGHTVILVTHNMDDVAKYADDVLVMEHGKlIKHDKP 229
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPALRQEMLTLVsqVCQER-QLTLLMVSHSLEDAARIAPRSLVVADGR-IAWDGP 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-223 |
4.73e-26 |
|
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: 107.79 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 6 ENINYIYSPGTtmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgNKNLKKLRK 85
Cdd:TIGR01257 932 KNLVKIFEPSG---RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 86 EVGLVFQfpETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDViSKSPFELSGGQMRRVAIAGVMVNEP 164
Cdd:TIGR01257 1004 SLGMCPQ--HNILFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 165 QILCLDEPGAGLDPRAREEMMQIFVNYqKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-230 |
4.92e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGY---HITPQTGNKNLKKLRKEVGLVFQFpetqlf 99
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRplaDWSPAELARRRAVLPQHSSLSFPF------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 enTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMV------NEPQILCLDEPG 173
Cdd:PRK13548 92 --TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 174 AGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPR 230
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-233 |
5.30e-26 |
|
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: 104.80 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 25 NISFELLDNSFIALIGHTGSGKSTLmqhFNA---LLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQfpETQLFEN 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTL---LRAiagLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQ--EARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 -TVLEDVKFGPKNFGVSDKEAEIKAkkWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRA 180
Cdd:COG4148 92 lSVRGNLLYGRKRAPRAERRISFDE--VVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 323465851 181 REEMMQIFVNYQKAGHT-VILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:COG4148 169 KAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-234 |
1.73e-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: 105.27 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDI-AGYHITPQT--GNKNLKKLRKEVGLVFQfpETQ 97
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTkpGPDGRGRAKRYIGILHQ--EYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LF-ENTVLEDVKfgpKNFGVS--DKEAEIKAKKWLKQVGLPTD----VISKSPFELSGGQMRRVAIAGVMVNEPQILCLD 170
Cdd:TIGR03269 376 LYpHRTVLDNLT---EAIGLElpDELARMKAVITLKMVGFDEEkaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 171 EPGAGLDP-----------RAREEMMQIFvnyqkaghtvILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:TIGR03269 453 EPTGTMDPitkvdvthsilKAREEMEQTF----------IIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-218 |
2.20e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnknlkklRKEVGLVFQ---FPETqlF 99
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQrseVPDS--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 ENTVLEDVKFG--PKN--FGVSDKEAEIKAKKWLKQVGLptDVISKSPF-ELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:NF040873 71 PLTVRDLVAMGrwARRglWRRLTRDDRAAVDDALERVGL--ADLAGRQLgELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 323465851 175 GLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVM 218
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
23-228 |
2.23e-25 |
|
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: 100.55 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKlrkeVGLVFQFPEtqLFEN- 101
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT----RKDLHK----IGSLIESPP--LYENl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFGPKNFGVSDKEAEikakKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR 181
Cdd:TIGR03740 86 TARENLKVHTTLLGLPDSRID----EVLNIVDL-TNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 182 EEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDK 228
Cdd:TIGR03740 161 QELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-233 |
2.67e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnknl 80
Cdd:PRK11231 1 MTLRTENLTVGYG-----TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 KKLRKEVGLVFQFPETQlfEN-TVLEDVKFG--PKN--FGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVA 155
Cdd:PRK11231 72 RQLARRLALLPQHHLTP--EGiTVRELVAYGrsPWLslWGRLSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-246 |
3.35e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.76 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNAL--LKPS---SGTIDIAGYHITPQtgnkNLKKLRKEVGLVFQFPeTQ 97
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKM----DVIELRRRVQMVFQIP-NP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFENTVLEDVKFGPK--NFGVSDKEAEIKAKKWLKQVGLPTDVISK--SPF-ELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:PRK14247 94 IPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLWDEVKDRldAPAgKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 173 GAGLDPRAREEMMQIFVNYQKAgHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENkewlKKHYLDE 246
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN----PRHELTE 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-244 |
3.65e-25 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 99.92 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkk 82
Cdd:cd03218 1 LRAENLSKRYG-----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 lRKEVGLVFQFPETQLFEN-TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTdvISKSP-FELSGGQMRRVAIAGVM 160
Cdd:cd03218 72 -RARLGIGYLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH--LRKSKaSSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEwLK 240
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL-VR 227
|
....
gi 323465851 241 KHYL 244
Cdd:cd03218 228 KVYL 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-224 |
7.65e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 6 ENINYIYSPGTTMEKKG----LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLK 81
Cdd:PRK10419 7 SGLSHHYAHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA-KLNRAQRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPETQLFENTVLEDVKFGPKN--FGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGV 159
Cdd:PRK10419 86 AFRRDIQMVFQDSISAVNPRKTVREIIREPLRhlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-223 |
9.87e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.12 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKKLR-KEVGLVFQFPETqLFEN 101
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS-KLSSAAKAELRnQKLGFIYQFHHL-LPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKsPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR 181
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 323465851 182 EEMMQIF--VNYQKaGHTVILVTHNMdDVAKYADDVLVMEHGKL 223
Cdd:PRK11629 182 DSIFQLLgeLNRLQ-GTAFLVVTHDL-QLAKRMSRQLEMRDGRL 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-235 |
1.95e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGY---HITPqtgnknlkkLRKEVGLVFQ----FPE 95
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlsHVPP---------YQRPINMMFQsyalFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TqlfenTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:PRK11607 106 M-----TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 176 LDPRAREEMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK11607 180 LDKKLRDRMQLEVVDiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-229 |
2.28e-24 |
|
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: 97.48 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTTmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtGNKNLK 81
Cdd:cd03369 6 EIEVENLSVRYAPDLP---PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPetQLFENTVledvkfgPKNFGVSDKEAEIKAKKWLKqvglptdvISKSPFELSGGQMRRVAIAGVMV 161
Cdd:cd03369 79 DLRSSLTIIPQDP--TLFSGTI-------RSNLDPFDEYSDEEIYGALR--------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 162 NEPQILCLDEPGAGLDpRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYaDDVLVMEHGKLIKHDKP 229
Cdd:cd03369 142 KRPRVLVLDEATASID-YATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-244 |
4.29e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.81 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG--YHITPQTGNKNLKKLRKEVGLVFQ---- 92
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIFQIDAIKLRKEVGMVFQqpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 FPETQLFENtvledVKFGPKNFGVSDKEaEIK--AKKWLKQVGLPTDVISK--SPF-ELSGGQMRRVAIAGVMVNEPQIL 167
Cdd:PRK14246 102 FPHLSIYDN-----IAYPLKSHGIKEKR-EIKkiVEECLRKVGLWKEVYDRlnSPAsQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 168 CLDEPGAGLDPRAREEMMQIFVNYQKAgHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN-KEWLKKHYL 244
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpKNELTEKYV 252
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-224 |
4.78e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.19 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfnALLK----PSSGTIDIAGYHITPQTgnk 78
Cdd:PRK13657 335 VEFDDVSFSY-DNS---RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQrvfdPQSGRILIDGTDIRTVT--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 nLKKLRKEVGLVFQfpETQLFENTVLEDVKFGPKNfgVSDKEAEIKAKKwlkqvGLPTDVISKSP--FE---------LS 147
Cdd:PRK13657 404 -RASLRRNIAVVFQ--DAGLFNRSIEDNIRVGRPD--ATDEEMRAAAER-----AQAHDFIERKPdgYDtvvgergrqLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLD-------PRAREEMMQifvnyqkaGHTVILVTHNMDDVAKyADDVLVMEH 220
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDveteakvKAALDELMK--------GRTTFIIAHRLSTVRN-ADRILVFDN 544
|
....
gi 323465851 221 GKLI 224
Cdd:PRK13657 545 GRVV 548
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-223 |
6.39e-24 |
|
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: 96.77 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItPQTGNKnlkK 82
Cdd:cd03248 12 VKFQNVTFAYP--TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHK---Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGPKnfGVSD---KEAEIKAKK----WLKQVGLPTDVISKSPfELSGGQMRRVA 155
Cdd:cd03248 86 LHSKVSLVGQ--EPVLFARSLQDNIAYGLQ--SCSFecvKEAAQKAHAhsfiSELASGYDTEVGEKGS-QLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAgHTVILVTHNMDDVAKyADDVLVMEHGKL 223
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-232 |
6.54e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKK 82
Cdd:COG4604 2 IEIKNVSKRYG-----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 ----LRKEVGLVFQFpetqlfenTVLEDVKFG--PKNFGVSDKEAEIKAKKWLKQVGLptdviskSPF------ELSGGQ 150
Cdd:COG4604 76 rlaiLRQENHINSRL--------TVRELVAFGrfPYSKGRLTAEDREIIDEAIAYLDL-------EDLadryldELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFvnyQKA----GHTVILVTHNMDDVAKYADDVLVMEHGKLIKH 226
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLL---RRLadelGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
....*.
gi 323465851 227 DKPRKI 232
Cdd:COG4604 218 GTPEEI 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-223 |
1.54e-23 |
|
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: 98.26 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 26 ISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhITPQTGNKN--LKKLRKEVGLVFQfpETQLFEN-T 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--RTLFDSRKGifLPPEKRRIGYVFQ--EARLFPHlS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFGPKNfgVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRARE 182
Cdd:TIGR02142 92 VRGNLRYGMKR--ARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 323465851 183 EMMQIFVN-YQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:TIGR02142 169 EILPYLERlHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-235 |
3.75e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.93 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSG-----TIDIAGYHITpqtGNKNLKKLRKEVGLVFQFP 94
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIF---NYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ETqlFENTVLEDVKFGPKNFG-VSDKEAEIKAKKWLKQVGL---PTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLD 170
Cdd:PRK14271 111 NP--FPMSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 171 EPGAGLDPRAREEMMQiFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK14271 189 EPTSALDPTTTEKIEE-FIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-224 |
4.22e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.55 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKK 82
Cdd:PRK11176 342 IEFRNVTFTY-PGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT----LAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQfpETQLFENTVLEDVKFGPKNFgVSDKEAEIKAK--------KWLKQvGLPTdVISKSPFELSGGQMRRV 154
Cdd:PRK11176 415 LRNQVALVSQ--NVHLFNDTIANNIAYARTEQ-YSREQIEEAARmayamdfiNKMDN-GLDT-VIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 155 AIAGVMVNEPQILCLDEPGAGLDPRArEEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLI 224
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTES-ERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-228 |
8.25e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.89 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgnKNLK 81
Cdd:TIGR01193 473 DIVINDVSYSYGYGS----NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL------KDID 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 K--LRKEVGLVFQFPetQLFENTVLEDVKFGPKNfGVSDKE-------AEIKAKKWLKQVGLPTDvISKSPFELSGGQMR 152
Cdd:TIGR01193 543 RhtLRQFINYLPQEP--YIFSGSILENLLLGAKE-NVSQDEiwaaceiAEIKDDIENMPLGYQTE-LSEEGSSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 153 RVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKagHTVILVTHNMdDVAKYADDVLVMEHGKLIK---HDK 228
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRL-SVAKQSDKIIVLDHGKIIEqgsHDE 694
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-225 |
1.12e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.09 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 25 NISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqTGNKNLKKLRkeVGLVFQFPETQLFENTVL 104
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--FGDYSYRSQR--IRMIFQDPSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 105 EDVKFGPK--NFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRARE 182
Cdd:PRK15112 107 SQILDFPLrlNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 323465851 183 EMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIK 225
Cdd:PRK15112 187 QLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-224 |
1.40e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 97.20 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnaLL----KPSSGTIDIAGYHITPQTgn 77
Cdd:COG5265 357 EVRFENVSFGYDP----ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR----LLfrfyDVTSGRILIDGQDIRDVT-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 78 knLKKLRKEVGLVFQfpETQLFENTVLEDVKFGpkNFGVSDKEAEIKAKkwLKQVGlptDVISKSP-----------FEL 146
Cdd:COG5265 427 --QASLRAAIGIVPQ--DTVLFNDTIAYNIAYG--RPDASEEEVEAAAR--AAQIH---DFIESLPdgydtrvgergLKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 147 SGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAR----EEMMQIfvnyqKAGHTVILVTHNMDDVAkYADDVLVMEHGK 222
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTEraiqAALREV-----ARGRTTLVIAHRLSTIV-DADEILVLEAGR 569
|
..
gi 323465851 223 LI 224
Cdd:COG5265 570 IV 571
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-223 |
2.01e-22 |
|
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: 96.65 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 6 ENINYIYSPGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKLRK 85
Cdd:TIGR01842 320 ENVTIVPPGG---KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 86 EVGLVFQfpETQLFENTVLEDV-KFGpKNFgvsDKEAEIKAKKwLKQV-----GLPT---DVISKSPFELSGGQMRRVAI 156
Cdd:TIGR01842 393 HIGYLPQ--DVELFPGTVAENIaRFG-ENA---DPEKIIEAAK-LAGVhelilRLPDgydTVIGPGGATLSGGQRQRIAL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVLVMEHGKL 223
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGRI 531
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-233 |
2.17e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkklrKEVGLVFQ----FPETQL 98
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ------RDICMVFQsyalFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FENtvledVKFGPKNFGVSDKEAEIKAKKWLKQVGLptdviskSPFE------LSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:PRK11432 96 GEN-----VGYGLKMLGVPKEERKQRVKEALELVDL-------AGFEdryvdqISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 173 GAGLDPRAREEMMQ-IFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK11432 164 LSNLDANLRRSMREkIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-224 |
2.43e-22 |
|
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: 92.21 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyHITPQTgnknlkklrkEVGLVFQfPETql 98
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLL----------GLGGGFN-PEL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 fenTVLEDVKFGPKNFGVSDKE-----AEIKAkkwLKQVGlptDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:cd03220 100 ---TGRENIYLNGRLLGLSRKEidekiDEIIE---FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-218 |
3.52e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.00 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 10 YIYSPGTTMekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtGNKNLKKLRKEVGL 89
Cdd:PRK15079 26 WFWQPPKTL--KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM-KDDEWRAVRSDIQM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 90 VFQFPETQLFENTVLEDV------KFGPKnfgVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNE 163
Cdd:PRK15079 103 IFQDPLASLNPRMTIGEIiaeplrTYHPK---LSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 164 PQILCLDEPGAGLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVM 218
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-234 |
3.59e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtgnknlkkLrkEVGLVFQfPETqlfenT 102
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL---------L--ELGAGFH-PEL-----T 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFGPKNFGVSdkEAEIKAKkwlkqvgLPtDVISKSpfEL------------SGgqMR-RVAIAGVMVNEPQILCL 169
Cdd:COG1134 105 GRENIYLNGRLLGLS--RKEIDEK-------FD-EIVEFA--ELgdfidqpvktysSG--MRaRLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 170 DEP-GAGlDP----RAREEMMQIfvnyQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:COG1134 171 DEVlAVG-DAafqkKCLARIREL----RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-229 |
4.47e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.33 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 25 NISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIagyhitpqtGNKNLKKL---RKEVGLVFQ----FPETQ 97
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI---------GEKRMNDVppaERGVGMVFQsyalYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFENtvledVKFGPKNFGVsdKEAEIKakKWLKQVG--LPTD-VISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:PRK11000 92 VAEN-----MSFGLKLAGA--KKEEIN--QRVNQVAevLQLAhLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 175 GLDPRAREEM-MQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:PRK11000 163 NLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-218 |
7.94e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHIT---PQTgnknlkkLRKEVGLVFQFPe 95
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkPEI-------YRQQVSYCAQTP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 tQLFENTVLEDVKFgPknFGVSDKEAEIKA-KKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:PRK10247 91 -TLFGDTVYDNLIF-P--WQIRNQQPDPAIfLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 323465851 175 GLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVaKYADDVLVM 218
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEI-NHADKVITL 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-232 |
9.24e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 9.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 24 DNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGnknlKKLRKEVGLVFQFPETQlFENTV 103
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQNATTP-GDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 104 LEDVKFG--PKN--FGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:PRK10253 99 QELVARGryPHQplFTRWRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 180 AREEMMQIF--VNYQKaGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKI 232
Cdd:PRK10253 178 HQIDLLELLseLNREK-GYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-235 |
1.06e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 17 TMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnLKKLRKEVGLVFQFPET 96
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDPYA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 QLFENTVLEDVKFGP-KNFGVSDKEAEIKAKKWL-KQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:PRK10261 413 SLDPRQTVGDSIMEPlRVHGLLPGKAAAARVAWLlERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 175 GLDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-233 |
1.67e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.15 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 25 NISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQT---------GNKNLKKLR-KEVGLVFQFP 94
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielseqSAAQMRHVRgADMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ETQLfeNTVL-------EDVKFgpkNFGVSDKEAEIKAKKWLKQVGLP--TDVISKSPFELSGGQMRRVAIAGVMVNEPQ 165
Cdd:PRK10261 114 MTSL--NPVFtvgeqiaESIRL---HQGASREEAMVEAKRMLDQVRIPeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 166 ILCLDEPGAGLDPRAREEMMQ-IFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIF 257
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-222 |
1.09e-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: 87.52 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLmqhFNALL---KPSSGTIDIAGyhitpqtgnkn 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSL---LSALLgelEKLSGSVSVPG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 lkklrkEVGLVFQFPetQLFENTVLEDVKFGpKNFgvsDKEaeikakkWLKQV---------------GLPTDV----IS 140
Cdd:cd03250 67 ------SIAYVSQEP--WIQNGTIRENILFG-KPF---DEE-------RYEKVikacalepdleilpdGDLTEIgekgIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 141 kspfeLSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR-AREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVLVME 219
Cdd:cd03250 128 -----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLD 201
|
...
gi 323465851 220 HGK 222
Cdd:cd03250 202 NGR 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
38-219 |
1.83e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.77 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 38 LIGHTGSGKSTLMQHFNALLKP---SSGTIDIAGYHITPqtgnknLKKLRKEVGLVFQFPetQLFEN-TVLEDVKFG-PK 112
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA------LPAEQRRIGILFQDD--LLFPHlSVGENLAFAlPP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 113 NFGVSDKEAEIKAKkwLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQ-IFVNY 191
Cdd:COG4136 104 TIGRAQRRARVEQA--LEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQI 180
|
170 180
....*....|....*....|....*...
gi 323465851 192 QKAGHTVILVTHNMDDVAKyADDVLVME 219
Cdd:COG4136 181 RQRGIPALLVTHDEEDAPA-AGRVLDLG 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-223 |
2.57e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.14 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpQTGNKNLKKLR-KEVGLVFQ----FPETqlfenTVLEDVKFG 110
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH-QMDEEARAKLRaKHVGFVFQsfmlIPTL-----NALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 111 PKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQ-IFV 189
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADlLFS 191
|
170 180 190
....*....|....*....|....*....|....
gi 323465851 190 NYQKAGHTVILVTHNmDDVAKYADDVLVMEHGKL 223
Cdd:PRK10584 192 LNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-224 |
3.32e-20 |
|
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: 86.81 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnKNLKKLRKEVGLVFQ----FPetQL 98
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL---PPHERARAGIAYVPQgreiFP--RL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 fenTVLEDVKFGPKNFGVSDKE--AEIKA-----KKWLKQVGlptdviskspFELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:TIGR03410 91 ---TVEENLLTGLAALPRRSRKipDEIYElfpvlKEMLGRRG----------GDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 172 PGAGLDPRAREEMMQIfVNY--QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRV-IRRlrAEGGMAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-240 |
4.05e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.17 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgTTMEKKGLDNISFELLDNSFIALIGHTGSGKST---LMQHFnalLKPSSGTIDIAGYHITpqtgNKN 79
Cdd:TIGR00958 479 IEFQDVSFSYP--NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNL---YQPTGGQVLLDGVPLV----QYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 80 LKKLRKEVGLVFQFPetQLFENTVLEDVKFGPKnfgvSDKEAEIKAKKWLKQV---------GLPTDVISKSPFeLSGGQ 150
Cdd:TIGR00958 550 HHYLHRQVALVGQEP--VLFSGSVRENIAYGLT----DTPDEEIMAAAKAANAhdfimefpnGYDTEVGEKGSQ-LSGGQ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQifvNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPR 230
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHK 698
|
250
....*....|
gi 323465851 231 KIFENKEWLK 240
Cdd:TIGR00958 699 QLMEDQGCYK 708
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-234 |
1.18e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 16 TTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnALLK--PSSGTIDIAGYHITpQTGNKNLKKLRKEVGLVFQF 93
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGL---ALLRliNSQGEIWFDGQPLH-NLNRRQLLPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 PETQL-----FENTVLEDVKFGPKNFGVSDKEAEIKAKkwLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILC 168
Cdd:PRK15134 371 PNSSLnprlnVLQIIEEGLRVHQPTLSAAQREQQVIAV--MEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 169 LDEPGAGLDPRAREEMMQIFVNYQKAGH-TVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-227 |
2.40e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAgyhitpqtgnKNLKk 82
Cdd:COG0488 316 LELEGLSKSYG-----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----------ETVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 lrkeVGLVFQFPEtQLFEN-TVLEDVKfgpknfGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG0488 380 ----IGYFDQHQE-ELDPDkTVLDELR------DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQkaGhTVILVTHNMDDVAKYADDVLVMEHGKLIKHD 227
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDFP--G-TVLLVSHDRYFLDRVATRILEFEDGGVREYP 511
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-235 |
2.85e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.75 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 24 DNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKP----SSGTIDIAGYHITPQTgnknlkkLR-KEVGLVFQFPETql 98
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCA-------LRgRKIATIMQNPRS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 fentvledvKFGP------------KNFGVSDKEAEIKAKkwLKQVGLPTD--VISKSPFELSGGQMRRVAIAGVMVNEP 164
Cdd:PRK10418 91 ---------AFNPlhtmhtharetcLALGKPADDATLTAA--LEAVGLENAarVLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 165 QILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFEN 235
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
16-238 |
3.54e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 16 TTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALL---KPSSGTIDIAGyHITPQTGN--KNLKKLRKEVGLV 90
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLG-RTVQREGRlaRDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 91 FQfpETQLFEN-TVLEDVKFGP-----------KNFGVSDKEAEIKAkkwLKQVGLpTDVISKSPFELSGGQMRRVAIAG 158
Cdd:PRK09984 92 FQ--QFNLVNRlSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQA---LTRVGM-VHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 159 VMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIkHDKPRKIFENKE 237
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVF-YDGSSQQFDNER 244
|
.
gi 323465851 238 W 238
Cdd:PRK09984 245 F 245
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-230 |
4.08e-19 |
|
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: 86.73 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYsPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQhfnALL---KPSSGTIDIAG---YHITPQT 75
Cdd:COG4618 330 RLSVENLTVVP-PGS--KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR---LLVgvwPPTAGSVRLDGadlSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 76 gnknlkkLRKEVGLVFQfpETQLFENTVLEdvkfgpkN---FGVSDKEAEIKAkkwLKQVG-------LP----TdVISK 141
Cdd:COG4618 404 -------LGRHIGYLPQ--DVELFDGTIAE-------NiarFGDADPEKVVAA---AKLAGvhemilrLPdgydT-RIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 142 SPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVLVMEHG 221
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDG 542
|
....*....
gi 323465851 222 KlIKHDKPR 230
Cdd:COG4618 543 R-VQAFGPR 550
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-228 |
5.70e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 37 ALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyHITPQTGNK-NLKKLRKEVGLVFQfpETQLFEN-TVLEDVKFGPKNf 114
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLFDAEKGiCLPPEKRRIGYVFQ--DARLFPHyKVRGNLRYGMAK- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 115 gvSDKEaeikakKWLKQVGL--PTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD-PRAREEMmqifvNY 191
Cdd:PRK11144 104 --SMVA------QFDKIVALlgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELL-----PY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 323465851 192 -QKAGHTV---IL-VTHNMDDVAKYADDVLVMEHGKLIKHDK 228
Cdd:PRK11144 171 lERLAREInipILyVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-224 |
6.72e-19 |
|
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: 83.09 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALL---KPSSGTIDIAGYHITPQTgnknlkkLRKEVGLVFQFpE 95
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQ-------FQKCVAYVRQD-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKW----LKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVedvlLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 323465851 172 PGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN-MDDVAKYADDVLVMEHGKLI 224
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-232 |
1.36e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKLRKEVGLVFQfpETQL-FEN 101
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE----ALSARAASRRVASVPQ--DTSLsFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKFG--P--KNFGVSDKEAEIKAKKWLKQVGlpTDVISKSPF-ELSGGQMRRVAIAGVMVNEPQILCLDEPGAGL 176
Cdd:PRK09536 93 DVRQVVEMGrtPhrSRFDTWTETDRAAVERAMERTG--VAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 177 DPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKI 232
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-203 |
2.08e-18 |
|
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: 81.25 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTG--NKNLKKLRKEVGLvfqfpETQLfe 100
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDepHENILYLGHLPGL-----KPEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 nTVLEDVKFGPKNFGVSDKEAEikakKWLKQVGLptDVISKSPF-ELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPR 179
Cdd:TIGR01189 89 -SALENLHFWAAIHGGAQRTIE----DALAAVGL--TGFEDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 323465851 180 AREEMMQIFVNYQKAGHTVILVTH 203
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-223 |
2.38e-18 |
|
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: 80.55 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKL-------RKEVGLVFQ 92
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGiayvpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 FPetqLFENTVLedvkfgpknfgvsdkeaeikakkwlkqvglptdvisksPFELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:cd03215 93 LS---VAENIAL--------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 323465851 173 GAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-224 |
2.38e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIA-GYHIT--PQ---------------TGNKNLKKLR 84
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGylPQeppldddltvldtvlDGDAELRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 85 KE---VGLVFQFPETQLFENTVLEDvKFGPKNfgvsDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:COG0488 94 AEleeLEAKLAEPDEDLERLAELQE-EFEALG----GWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 162 NEPQILCLDEPGAGLDPRAR---EEMMQifvNYQkagHTVILVTHN---MDDVakyADDVLVMEHGKLI 224
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIewlEEFLK---NYP---GTVLVVSHDryfLDRV---ATRILELDRGKLT 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-226 |
3.89e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 5 FENINYIYsPGTtmekKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhiTPQTGNKNLKKLR 84
Cdd:PRK11288 7 FDGIGKTF-PGV----KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 85 KEVGLVFQfpETQLF-ENTVLEDVKFG--PKNFGVSDKEAEIK-AKKWLKQVGLptDVISKSPF-ELSGGQMRRVAIAGV 159
Cdd:PRK11288 79 AGVAIIYQ--ELHLVpEMTVAENLYLGqlPHKGGIVNRRLLNYeAREQLEHLGV--DIDPDTPLkYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKH 226
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-224 |
9.08e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQT----GNKNLKKL-RKEVGLVFQFPE 95
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalSEAERRRLlRTEWGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TQLfENTVLEDVKFGPKNFGVSDKE-AEI--KAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEP 172
Cdd:PRK11701 100 DGL-RMQVSAGGNIGERLMAVGARHyGDIraTAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 173 GAGLD--PRAR-EEMMQIFVNyqKAGHTVILVTHNMdDVAK-YADDVLVMEHGKLI 224
Cdd:PRK11701 179 TGGLDvsVQARlLDLLRGLVR--ELGLAVVIVTHDL-AVARlLAHRLLVMKQGRVV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-245 |
1.02e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.58 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItPQTGNKNLKKLRKEVGLVFQfpETQL 98
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PAMSRSRLYTVRKRMSMLFQ--SGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 F-ENTVLEDVKFgPKNFGVSDKEAEIKAKKWLK--QVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:PRK11831 96 FtDMNVFDNVAY-PLREHTQLPAPLLHSTVMMKleAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 176 LDPRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEWLKKHYLD 245
Cdd:PRK11831 174 QDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFLD 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-223 |
1.13e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkklRKEVG--LVFQfpETQLFE 100
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-----AHQLGiyLVPQ--EPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 N-TVLEDVKFG-PKNfgvsdKEAEIKAKKWLKQVGLPTDV-ISKSPFELSGGQMrrVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK15439 100 NlSVKENILFGlPKR-----QASMQKMKQLLAALGCQLDLdSSAGSLEVADRQI--VEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 323465851 178 PRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-223 |
2.21e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 22 GLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHI---TPQTGNKN----LKKLRKEVGLVFqfp 94
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrSPQDGLANgivyISEDRKRDGLVL--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ETQLFENTVLEDVKFGPKNFGVSDKEAEIKA-KKWLKQVGLPTDVISKSPFELSGGQMRRVAIA-GVMVNePQILCLDEP 172
Cdd:PRK10762 344 GMSVKENMSLTALRYFSRAGGSLKHADEQQAvSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIArGLMTR-PKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 323465851 173 GAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
4.60e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTtmekkGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpQTGNKNLKK 82
Cdd:PRK09700 6 ISMAGIGKSFGPVH-----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-----INYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLF-ENTVLEDVKFG----PKNFGVSD---KEAEIKAKKWLKQVGLPTDVISKSPfELSGGQMRRV 154
Cdd:PRK09700 76 LAAQLGIGIIYQELSVIdELTVLENLYIGrhltKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVA-NLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 155 AIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-233 |
5.02e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTlmqhfnallkpSS----GTIDIAGYHITPQT--GNKNLKKL-----RK---- 85
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSV-----------SSlaimGLIDYPGRVMAEKLefNGQDLQRIsekerRNlvga 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 86 EVGLVFQFPETQL-------FEntVLEDVKFgpkNFGVSDKEAEIKAKKWLKQVGLPtDVISK---SPFELSGGQMRRVA 155
Cdd:PRK11022 90 EVAMIFQDPMTSLnpcytvgFQ--IMEAIKV---HQGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVM 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 156 IAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-233 |
5.24e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 24 DNISFELLDNSFIALIGHTGSGKSTlmqhfNAL----LKPS------SGTIDIAG---YHITPQTgnknLKKLR-KEVGL 89
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSV-----TALsilrLLPSppvvypSGDIRFHGeslLHASEQT----LRGVRgNKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 90 VFQFP----------ETQLFENTVLEDvkfgpknfGVSDKEAEIKAKKWLKQVGL--PTDVISKSPFELSGGQMRRVAIA 157
Cdd:PRK15134 97 IFQEPmvslnplhtlEKQLYEVLSLHR--------GMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 158 GVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-236 |
6.11e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLkPS---SGTIDIAGYHITPqtgnKNLKKlRKEVGLVFQFPETQ 97
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA----SNIRD-TERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFEN-TVLEDVKFG--PKNFGVSDKEA-EIKAKKWLKQVGLPTDVISKSpFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:PRK13549 93 LVKElSVLENIFLGneITPGGIMDYDAmYLRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENK 236
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDD 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-236 |
8.31e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLK 81
Cdd:PRK10790 340 RIDIDNVSFAYRDD----NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS----SLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPetqlfenTVLEDVKFGPKNFGVSDKEAEIkakkW--LKQVGLPTDV----------ISKSPFELSGG 149
Cdd:PRK10790 412 VLRQGVAMVQQDP-------VVLADTFLANVTLGRDISEEQV----WqaLETVQLAELArslpdglytpLGEQGNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 150 QMRRVAIAGVMVNEPQILCLDEPGAGLDpRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKP 229
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANID-SGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTH 558
|
....*..
gi 323465851 230 RKIFENK 236
Cdd:PRK10790 559 QQLLAAQ 565
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-222 |
1.11e-16 |
|
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: 74.79 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIdiagyhitpqtgnknlkk 82
Cdd:cd03221 1 IELENLSKTYG-----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 lrkevglvfqfpetqlfenTVLEDVKFGpknfgvsdkeaeikakkWLKQvglptdviskspfeLSGGQMRRVAIAGVMVN 162
Cdd:cd03221 58 -------------------TWGSTVKIG-----------------YFEQ--------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQkagHTVILVTHNMDDVAKYADDVLVMEHGK 222
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-238 |
3.67e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFEL-----LdnsfiALIGHTGSGKSTLMQhfnAL---LKPSSGTIDIAG--YHI-TPQTGNKNlkKL----- 83
Cdd:COG1129 265 GGVVRDVSFSVrageiL-----GIAGLVGAGRTELAR---ALfgaDPADSGEIRLDGkpVRIrSPRDAIRA--GIayvpe 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 -RKEVGLVFQFPetqLFENTVLEDV-KFGpkNFGVSDKEAEIK-AKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:COG1129 335 dRKGEGLVLDLS---IRENITLASLdRLS--RGGLLDRRRERAlAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIkhdkprKIFENKEW 238
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV------GELDREEA 481
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-233 |
3.80e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 24 DNISFELLDNSFIALIGHTGSGKS----TLMqhfnALLKPS---SGTIDIAGYHIT--PQtgnKNLKKLR-KEVGLVFQF 93
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSqtafALM----GLLAANgriGGSATFNGREILnlPE---KELNKLRaEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 PET----------QLFEntVLEDVKfgpknfGVSDKEAEIKAKKWLKQVGLPT--DVISKSPFELSGGQMRRVAIAGVMV 161
Cdd:PRK09473 106 PMTslnpymrvgeQLME--VLMLHK------GMSKAEAFEESVRMLDAVKMPEarKRMKMYPHEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHT-VILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVF 250
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-223 |
3.85e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSF--------------IALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtgnKNLKKLRKEVG 88
Cdd:PRK10522 325 LRNVTFAYQDNGFsvgpinltikrgelLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA----EQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 89 LVFQfpETQLFENTVledvkfGPKNFGVSDKEAEikakKWLKQVGLPTDVISK----SPFELSGGQMRRVAIAGVMVNEP 164
Cdd:PRK10522 401 AVFT--DFHLFDQLL------GPEGKPANPALVE----KWLERLKMAHKLELEdgriSNLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 165 QILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNmDDVAKYADDVLVMEHGKL 223
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLlQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-224 |
3.91e-16 |
|
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: 77.94 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSS--GTIDIAGYHITPQ----TGNKNLKKLRKEVGLVfqfP 94
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASnirdTERAGIVIIHQELTLV---P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ETQLFENTVLEDvKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:TIGR02633 92 ELSVAENIFLGN-EITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 323465851 175 GLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-268 |
1.02e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTTMEKKGLdniSFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLK 81
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGL---SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA----KFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPetQLFENTvledVKFGPKNFGVSDKEAEIKAkkwLKQVGLpTDVISKSPFEL-----------SGGQ 150
Cdd:PLN03232 1307 DLRRVLSIIPQSP--VLFSGT----VRFNIDPFSEHNDADLWEA---LERAHI-KDVIDRNPFGLdaevseggenfSVGQ 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRArEEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPR 230
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQ 1454
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 323465851 231 KIFENK--EWLKKHYLDEPTPSLFASSLTgFKFKENPLTI 268
Cdd:PLN03232 1455 ELLSRDtsAFFRMVHSTGPANAQYLSNLV-FERRENGMSL 1493
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-204 |
1.33e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.75 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQT--------GNKNLKKlrkevglvfqfP 94
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeachylGHRNAMK-----------P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 ETqlfenTVLEDVKFGPKNFGvsDKEAEIKAKkwLKQVGLP--TDVisksPF-ELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:PRK13539 87 AL-----TVAENLEFWAAFLG--GEELDIAAA--LEAVGLAplAHL----PFgYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 323465851 172 PGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN 204
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-237 |
1.50e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.74 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTTMEKKGldnISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtGNKNLK 81
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRG---VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI----GAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLVFQFPetQLFENTVLEDVK-FgpknfgVSDKEAEIKAKkwLKQVGLPTDVISKspfelSGGQMRRVAIAGV- 159
Cdd:PTZ00243 1381 ELRRQFSMIPQDP--VLFDGTVRQNVDpF------LEASSAEVWAA--LELVGLRERVASE-----SEGIDSRVLEGGSn 1445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 160 -MVNEPQILCL--------------DEPGAGLDPrAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYaDDVLVMEHGKLI 224
Cdd:PTZ00243 1446 ySVGQRQLMCMarallkkgsgfilmDEATANIDP-ALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVA 1523
|
250
....*....|...
gi 323465851 225 KHDKPRKIFENKE 237
Cdd:PTZ00243 1524 EMGSPRELVMNRQ 1536
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-225 |
1.88e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.95 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLmqhFNALL-----KPSSGTIDIAGyhitpqtgnKNLKKL------RKEV 87
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTL---AKVLMghpkyEVTSGSILLDG---------EDILELspderaRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 88 GLVFQFPE------TQLFENTVLEDVKFGPknfgVSDKEAEIKAKKWLKQVGLPTDVISKSPFE-LSGGQMRRVAIAGVM 160
Cdd:COG0396 80 FLAFQYPVeipgvsVSNFLRTALNARRGEE----LSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN---MDDVAkyADDVLVMEHGKLIK 225
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVK 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-235 |
2.40e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.94 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSsgtidiagYHITPQT---GNKNLKKL---------RKEVG 88
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN--------WHVTADRfrwNGIDLLKLsprerrkiiGREIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 89 LVFQFP----------ETQLFENTVLEDVKfGP--KNFGVSDKEAeikaKKWLKQVGL--PTDVISKSPFELSGGQMRRV 154
Cdd:COG4170 93 MIFQEPsscldpsakiGDQLIEAIPSWTFK-GKwwQRFKWRKKRA----IELLHRVGIkdHKDIMNSYPHELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 155 AIAGVMVNEPQILCLDEPGAGLDPRAReemMQIF-----VNyQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQ---AQIFrllarLN-QLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
....*.
gi 323465851 230 RKIFEN 235
Cdd:COG4170 244 EQILKS 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-243 |
3.47e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 7 NINYIYSPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLM----QHFNAllkpSSGTIDiagYHITPQTGNKnLKK 82
Cdd:PRK10789 317 NIRQFTYPQT--DHPALENVNFTLKPGQMLGICGPTGSGKSTLLsliqRHFDV----SEGDIR---FHDIPLTKLQ-LDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPetQLFENTVLEDVKFGPKNfgvsDKEAEIKAKKWLKQV---------GLPTDVISKSPFeLSGGQMRR 153
Cdd:PRK10789 387 WRSRLAVVSQTP--FLFSDTVANNIALGRPD----ATQQEIEHVARLASVhddilrlpqGYDTEVGERGVM-LSGGQKQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 154 VAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIF 233
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLA 537
|
250
....*....|
gi 323465851 234 ENKEWLKKHY 243
Cdd:PRK10789 538 QQSGWYRDMY 547
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-221 |
4.38e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 71.89 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYiYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNALLKPS-----SGTIDIAGYhitpqtg 76
Cdd:cd03232 3 VLTWKNLNY-TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL---DVLAGRKtagviTGEILINGR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 77 nKNLKKLRKEVGLVFQFPeTQLFENTVLEDVKFGPKNFGvsdkeaeikakkwlkqvglptdviskspfeLSGGQMRRVAI 156
Cdd:cd03232 72 -PLDKNFQRSTGYVEQQD-VHSPNLTVREALRFSALLRG------------------------------LSVEQRKRLTI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN-MDDVAKYADDVLVMEHG 221
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-246 |
4.39e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLmqhFNA---LLKPSSGTIDIAGYHITpqtgnkNL---KKLRKEVGLVFQfpET 96
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTT---FYMivgLVKPDSGRIFLDGEDIT------HLpmhKRARLGIGYLPQ--EA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 QLF------EN--TVLEdvkfgpkNFGVSDKEAEIKAKKWLKQVGLptDVISKSP-FELSGGQMRRVAIAGVMVNEPQIL 167
Cdd:COG1137 88 SIFrkltveDNilAVLE-------LRKLSKKEREERLEELLEEFGI--THLRKSKaYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 168 CLDEPGAGLDPRAREEMMQIFVNYQKAGhTVILVT-HNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENKEwLKKHYLDE 246
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERG-IGVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL-VRKVYLGE 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-232 |
7.43e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 9 NYIYSPGTTMEkkgLDNISFELLDNSFI-------------ALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqt 75
Cdd:PRK10575 3 EYTNHSDTTFA---LRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 76 GNKNLKKLRKEVG-LVFQFPETQLFenTVLEDVKFG--P-----KNFGVSDKEaeiKAKKWLKQVGLptdviskSPF--- 144
Cdd:PRK10575 76 ESWSSKAFARKVAyLPQQLPAAEGM--TVRELVAIGryPwhgalGRFGAADRE---KVEEAISLVGL-------KPLahr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 145 ---ELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEH 220
Cdd:PRK10575 144 lvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
250
....*....|..
gi 323465851 221 GKLIKHDKPRKI 232
Cdd:PRK10575 224 GEMIAQGTPAEL 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-246 |
9.34e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKnlkKLRKEVGLVFQ----FPE 95
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA---RARRGIGYLPQeasiFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TQLFEN--TVLEDVKfgpknfGVSDKEAEIKAKKWLKQVGLP--TDVISKSpfeLSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:PRK10895 93 LSVYDNlmAVLQIRD------DLSAEQREDRANELMEEFHIEhlRDSMGQS---LSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 172 PGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENkEWLKKHYLDE 246
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD-EHVKRVYLGE 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-228 |
1.17e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.23 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 112 KNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY 191
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110
....*....|....*....|....*....|....*..
gi 323465851 192 QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDK 228
Cdd:NF000106 191 VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
26-221 |
1.90e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 26 ISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKKLRKEVGLVFQ----FPETQLFEN 101
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN------ELEPADRDIAMVFQnyalYPHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 tvledVKFGPKNFGVSdkEAEI-----KAKKWLKQVGLptdvISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGL 176
Cdd:PRK11650 97 -----MAYGLKIRGMP--KAEIeervaEAARILELEPL----LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 323465851 177 DPRAREEM-MQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:PRK11650 166 DAKLRVQMrLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-234 |
2.81e-14 |
|
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: 72.53 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNAL--LKPSSGTIDiagYHIT------------------PQTGNK- 78
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRII---YHVAlcekcgyverpskvgepcPVCGGTl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 --------NL-----KKLRKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFE 145
Cdd:TIGR03269 90 epeevdfwNLsdklrRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL-SHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 146 LSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRARE---EMMQIFVnyQKAGHTVILVTHNMDDVAKYADDVLVMEHGK 222
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlvhNALEEAV--KASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
250
....*....|..
gi 323465851 223 LIKHDKPRKIFE 234
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-223 |
4.80e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.20 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEKkgldNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnknlkK 82
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFK----NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA-------------K 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPETQLFENTVLEDVKFGPknfGVsdkeAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:PLN03073 572 VRMAVFSQHHVDGLDLSSNPLLYMMRCFP---GV----PEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAghtVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-244 |
5.53e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITP-QTGnknlKKLRKEVGLVfqfPE-TQL 98
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTA----KIMREAVAIV---PEgRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FEN-TVLEDVKFGpkNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK11614 92 FSRmTVEENLAMG--GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 178 PRAreeMMQIFVNYQK---AGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFENkEWLKKHYL 244
Cdd:PRK11614 170 PII---IQQIFDTIEQlreQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN-EAVRSAYL 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-213 |
5.83e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpQTGNKNLKKlrKEVGLVFQFPETQLFENT 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-----QPTRQALQK--NLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDV----KFGPKNF----GVSDKEAEIKAkkwLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:PRK15056 96 LVEDVvmmgRYGHMGWlrraKKRDRQIVTAA---LARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 323465851 175 GLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYAD 213
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-222 |
2.58e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 16 TTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNALlkpsSGTIDIAGYHITPQTGNKNL-KKLRKEVGLVFQ-- 92
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLL---NAL----AGRIQGNNFTGTILANNRKPtKQILKRTGFVTQdd 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 --FPETQLFENTVLEDVKFGPKNfgVSDKEAEIKAKKWLKQVGLP---TDVISKSPFE-LSGGQMRRVAIAGVMVNEPQI 166
Cdd:PLN03211 150 ilYPHLTVRETLVFCSLLRLPKS--LTKQEKILVAESVISELGLTkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 167 LCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDD-VAKYADDVLVMEHGK 222
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGR 284
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-223 |
5.64e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.70 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQH-FNALLKPSSGTIDIAGYHITPQTGNKNLK-------KLRKEVGLVf 91
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAlFGAYPGKFEGNVFINGKPVDIRNPAQAIRagiamvpEDRKRHGIV- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 92 qfPETQLFENTVLEDV-KFGPKnfGVSDKEAEIKA-KKWLKQVGLPTdvisKSPF----ELSGGQMRRVAIAGVMVNEPQ 165
Cdd:TIGR02633 352 --PILGVGKNITLSVLkSFCFK--MRIDAAAELQIiGSAIQRLKVKT----ASPFlpigRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 166 ILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-241 |
6.03e-13 |
|
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: 67.19 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKpSSGTIDIAGYHITPQTgnknLKKLRKEVGLVFQfpETQLFENT 102
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVP----LQKWRKAFGVIPQ--KVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VledvkfgPKNFGVSDKEAEIKAKKWLKQVGLPTdVISKSP-----------FELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:cd03289 93 F-------RKNLDPYGKWSDEEIWKVAEEVGLKS-VIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 172 PGAGLDPRA----REEMMQIFvnyqkAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:cd03289 165 PSAHLDPITyqviRKTLKQAF-----ADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-217 |
7.62e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKkgldNISFELLDNSFIALIGHTGSGKSTLM------------------------------ 50
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYK----DLTFSCDSKKTTAIVGETGSGKSTVMsllmrfydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 51 ----QHFNALLK--------------------PSSGTIDIAGYHITpqtgNKNLKKLRKEVGLVFQFPetQLFENTVLED 106
Cdd:PTZ00265 1242 yqgdEEQNVGMKnvnefsltkeggsgedstvfKNSGKILLDGVDIC----DYNLKDLRNLFSIVSQEP--MLFNMSIYEN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 107 VKFGPKN-----------FGVSDKEAEIKAKKWLKQVGlptdvisksPF--ELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:PTZ00265 1316 IKFGKEDatredvkrackFAAIDEFIESLPNKYDTNVG---------PYgkSLSGGQKQRIAIARALLREPKILLLDEAT 1386
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 323465851 174 AGLDPRAREEMMQIFVNYQ-KAGHTVILVTHNMDDVaKYADDVLV 217
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVV 1430
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-229 |
9.37e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNALLKPSSGTIDIAGyHITPQTGNKNLKKLRKEVGLVFQFpetQL 98
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSG-SVLLNGMPIDAKEMRAISAYVQQD---DL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 F--ENTVLEDVKFG-----PKNFGVSDKEAEIKAkkWLKQVGLPT--DVISKSPFE---LSGGQMRRVAIAGVMVNEPQI 166
Cdd:TIGR00955 110 FipTLTVREHLMFQahlrmPRRVTKKEKRERVDE--VLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 167 LCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN-MDDVAKYADDVLVMEHGKLIKHDKP 229
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-223 |
1.03e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 16 TTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKK-------LRKEVG 88
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayiteSRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 89 LvfqFPETQLFENTV----LEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEP 164
Cdd:PRK09700 352 F---FPNFSIAQNMAisrsLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 165 QILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-237 |
1.09e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTtmeKKGLDNISFELLDNSFIALIGHTGSGKSTLmqhFNALLK---PSSGTIDIAGYHItpqtGNK 78
Cdd:PLN03130 1237 SIKFEDVVLRYRPEL---PPVLHGLSFEISPSEKVGIVGRTGAGKSSM---LNALFRiveLERGRILIDGCDI----SKF 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 79 NLKKLRKEVGLVFQFPetQLFENTvledVKFGPKNFGvSDKEAEIkakkW--LKQVGLpTDVISKSPFEL---------- 146
Cdd:PLN03130 1307 GLMDLRKVLGIIPQAP--VLFSGT----VRFNLDPFN-EHNDADL----WesLERAHL-KDVIRRNSLGLdaevseagen 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 147 -SGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRA--------REEMMQIfvnyqkaghTVILVTHNMDDVAKyADDVLV 217
Cdd:PLN03130 1375 fSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTdaliqktiREEFKSC---------TMLIIAHRLNTIID-CDRILV 1444
|
250 260
....*....|....*....|
gi 323465851 218 MEHGKLIKHDKPRKIFENKE 237
Cdd:PLN03130 1445 LDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-211 |
1.17e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgNKNLKKLRKEVGLVFQF----PETQL 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQKQLCFVGHRsginPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FENtVLEDVKFGPKNFGVSDKEAEIKAKKWLK-QVGLptdviskspfeLSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK13540 92 REN-CLYDIHFSPGAVGITELCRLFSLEHLIDyPCGL-----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 323465851 178 PRAREEMMQIFVNYQKAGHTVILVTH-----NMDDVAKY 211
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHqdlplNKADYEEY 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-220 |
1.57e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLK--PSSGTIDIagyhitpqtgnknlkklrkevgLVFQFPEt 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV----------------------PDNQFGR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 qlfENTVLEDVkfgPKNFGVSDkeaeikAKKWLKQVGLPTDVISKSPF-ELSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:COG2401 99 ---EASLIDAI---GRKGDFKD------AVELLNAVGLSDAVLWLRRFkELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 323465851 176 LDPR-ARE--EMMQIFVnyQKAGHTVILVTHNmDDVAKY-ADDVLVMEH 220
Cdd:COG2401 167 LDRQtAKRvaRNLQKLA--RRAGITLVVATHH-YDVIDDlQPDLLIFVG 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-223 |
1.94e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQH-FNALLKPSSGTIDIAGYHITPQTGNKNLK-------KLRKEVGLVf 91
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQClFGAYPGRWEGEIFIDGKPVKIRNPQQAIAqgiamvpEDRKRDGIV- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 92 qfPETQLFEN---TVLEDVKFGpknfGVSDKEAEIK-AKKWLKQVGLPTdvisKSPF----ELSGGQMRRVAIAGVMVNE 163
Cdd:PRK13549 354 --PVMGVGKNitlAALDRFTGG----SRIDDAAELKtILESIQRLKVKT----ASPElaiaRLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 164 PQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-220 |
5.46e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.36 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIdiagyhitpqtgnKNLKKLRkeVGLVfqfPETQL 98
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLR--IGYV---PQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FENTVLEDVK-FGPKNFGVsdKEAEIKAKkwLKQVGlPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK09544 78 LDTTLPLTVNrFLRLRPGT--KKEDILPA--LKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 323465851 178 PRAREEMMQIFVNYQKA-GHTVILVTHNMDDVAKYADDVLVMEH 220
Cdd:PRK09544 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-220 |
5.77e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSpgTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHitpQTGNKNLKK 82
Cdd:PTZ00265 383 IQFKNVRFHYD--TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH---NLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPetQLFENTVLEDVKF------------------GPKNFGVSDKEAEIKAKKWL--------------- 129
Cdd:PTZ00265 458 WRSKIGVVSQDP--LLFSNSIKNNIKYslyslkdlealsnyynedGNDSQENKNKRNSCRAKCAGdlndmsnttdsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 130 ------------------KQVgLPTDVISKSP-----------FELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRA 180
Cdd:PTZ00265 536 emrknyqtikdsevvdvsKKV-LIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 323465851 181 rEEMMQIFVNYQKAGHT--VILVTHNMDDVaKYADDVLVMEH 220
Cdd:PTZ00265 615 -EYLVQKTINNLKGNENriTIIIAHRLSTI-RYANTIFVLSN 654
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-223 |
8.85e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 22 GLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtgNKNLKKLRKEVGLVFqFPETQ---- 97
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI-----NALSTAQRLARGLVY-LPEDRqssg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LFENTVLE----DVKFGPKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:PRK15439 352 LYLDAPLAwnvcALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-223 |
1.19e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIA-----GYHITPQtgnknLKKLRKEvglvfqf 93
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQ-----LEFLRAD------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 petqlfENTVLEDVKFGPknfgvsdKEAEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:PRK10636 392 ------ESPLQHLARLAP-------QELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAghtVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-221 |
1.31e-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: 65.03 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYsPGTTmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnKNLKK 82
Cdd:TIGR01257 1938 LRLNELTKVY-SGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-----TNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFpetqlfenTVLEDVKFGPKNF-------GVSDKEAEIKAKKWLKQVGLP--TDVISKSpfeLSGGQMRR 153
Cdd:TIGR01257 2010 VHQNMGYCPQF--------DAIDDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSlyADRLAGT---YSGGNKRK 2078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 154 VAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHG 221
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-203 |
1.47e-11 |
|
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: 62.13 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGN--KNLKKLRKEVGLvfqfpETQLfe 100
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLGHAPGI-----KTTL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 nTVLEDVKFGPKnfgVSDKEAEIKAkkwLKQVGLP--TDVISKSpfeLSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDP 178
Cdd:cd03231 89 -SVLENLRFWHA---DHSDEQVEEA---LARVGLNgfEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*
gi 323465851 179 RAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-224 |
3.26e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKlrkEVGLVFQfPETQLFE 100
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN---GISMVHQ-ELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 NTVLEDVKFG---PKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSPfELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK10982 88 RSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 178 PRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-244 |
5.45e-11 |
|
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: 62.72 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 122 EIKAK-KWLKQVGLPTDVISKSPFELSGGQMRRVAIA--------GVMvnepqiLCLDEPGAGLDPRAREEMMQIFVNYQ 192
Cdd:TIGR00630 464 EIRERlGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLAtqigsgltGVL------YVLDEPSIGLHQRDNRRLINTLKRLR 537
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 193 KAGHTVILVTHNmDDVAKYADDVLVM-----EH-GKLIKHDKPRKIFENKEWLKKHYL 244
Cdd:TIGR00630 538 DLGNTLIVVEHD-EDTIRAADYVIDIgpgagEHgGEVVASGTPEEILANPDSLTGQYL 594
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-241 |
6.99e-11 |
|
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: 62.62 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKpSSGTIDIAGYHITPQTgnknLKKLRKEVGLVFQfpETQLFENT 102
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT----LQTWRKAFGVIPQ--KVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VledvkfgPKNFGVSDKEAEIKAKKWLKQVGLPTdVISKSP-----------FELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:TIGR01271 1308 F-------RKNLDPYEQWSDEEIWKVAEEVGLKS-VIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 172 PGAGLDPRA----REEMMQIFVNYqkaghTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKEWLKK 241
Cdd:TIGR01271 1380 PSAHLDPVTlqiiRKTLKQSFSNC-----TVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-225 |
8.73e-11 |
|
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: 59.85 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMqhfNALL-----KPSSGTIDIAGYHITPQTGNKnlkKLRKEVGLVFQF 93
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLA---KTIMghpkyEVTEGEILFKGEDITDLPPEE---RARLGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 PETqlfentvLEDVKFgpKNFgvsdkeaeikakkwLKQVGLptdviskspfELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:cd03217 86 PPE-------IPGVKN--ADF--------------LRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTHNmDDVAKY--ADDVLVMEHGKLIK 225
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDYikPDRVHVLYDGRIVK 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-220 |
8.75e-11 |
|
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: 59.47 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMekkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIagyhitPQTGNknlkk 82
Cdd:cd03223 1 IELENLSLATPDGRVL----LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------PEGED----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 lrkevglVFQFPETQLFENTVLEDVKFGPknfgvsdkeaeikakkWLKqvglptdviskspfELSGGQMRRVAIAGVMVN 162
Cdd:cd03223 66 -------LLFLPQRPYLPLGTLREQLIYP----------------WDD--------------VLSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFvnyQKAGHTVILVTHNmDDVAKYADDVLVMEH 220
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLL---KELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-224 |
1.23e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 26 ISFELLDNSFIALIGHTGSGKSTLMQHFNALLkPSSGTIDIAGYHITPQTGNKnLKKLRKEVGL---------VFQFPET 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAE-LARHRAYLSQqqtppfampVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 97 QLFENTVLEDVKfgpknfGVSDKEAEikakkwlkQVGLpTDVISKSPFELSGGQMRRVAIAGVM------VN-EPQILCL 169
Cdd:PRK03695 93 HQPDKTRTEAVA------SALNEVAE--------ALGL-DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpdINpAGQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 170 DEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-225 |
1.68e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.59 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTI-------DIAGYHITPQtgnKNLKKLRKEVGLVFQF 93
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTadrmrfdDIDLLRLSPR---ERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 94 PETQL--FENTVLEDVKFGP---------KNFGVSDKeaeiKAKKWLKQVGL--PTDVISKSPFELSGGQMRRVAIAGVM 160
Cdd:PRK15093 98 PQSCLdpSERVGRQLMQNIPgwtykgrwwQRFGWRKR----RAIELLHRVGIkdHKDAMRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 161 VNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIK 225
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-221 |
2.82e-10 |
|
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: 58.81 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLM---------------------QHFNALLKPSSGTID-----IAgyhITPQTG 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEglspaIA---IDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 77 NKNLkklRKEVGLVfqfpeTQLFENTVLEDVKFGpknfgvsdkeaeIKAK-KWLKQVGLPTDVISKSPFELSGGQMRRVA 155
Cdd:cd03270 88 SRNP---RSTVGTV-----TEIYDYLRLLFARVG------------IRERlGFLVDVGLGYLTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 156 IA--------GVmvnepqILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNmDDVAKYADDVLVM-----EHG 221
Cdd:cd03270 148 LAtqigsgltGV------LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIgpgagVHG 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
116-207 |
4.27e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 116 VSDKEaEIKAKKWLKQVGLPTDViSKSPFE-LSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAReEMMQIFVNYQKA 194
Cdd:PRK10938 373 VSDRQ-QKLAQQWLDILGIDKRT-ADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLIS 449
|
90
....*....|....*
gi 323465851 195 -GHTVIL-VTHNMDD 207
Cdd:PRK10938 450 eGETQLLfVSHHAED 464
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-203 |
6.03e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 24 DNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnKNLKKLRKEvglvfqFPETQLF---- 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG---------EPIRRQRDE------YHQDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 -----ENTVLEDVKFGPKNFGVSDKEAEIKAkkwLKQVGLptdviskSPFE------LSGGQMRRVAIAGVMVNEPQILC 168
Cdd:PRK13538 83 pgiktELTALENLRFYQRLHGPGDDEALWEA---LAQVGL-------AGFEdvpvrqLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 323465851 169 LDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
35-224 |
7.58e-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: 59.04 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 35 FIalIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQtgnkNLKKLRkevglvfqfpetQLFeNTVLEDVKFGPKNF 114
Cdd:COG4615 362 FI--VGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD----NREAYR------------QLF-SAVFSDFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 115 GVSDKEAEIKAKKWLKQ------VGLPTDVISKSpfELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREemmqIF 188
Cdd:COG4615 423 GLDGEADPARARELLERleldhkVSVEDGRFSTT--DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR----VF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 323465851 189 vnYQ------KA-GHTVILVTHnmDDvaKY---ADDVLVMEHGKLI 224
Cdd:COG4615 497 --YTellpelKArGKTVIAISH--DD--RYfdlADRVLKMDYGKLV 536
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
36-237 |
7.95e-10 |
|
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: 58.00 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTgnknLKKLRKEVGLVFQFPetQLFENTVleDVKFGPKNFG 115
Cdd:cd03288 50 VGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDP--ILFSGSI--RFNLDPECKC 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 116 VSDKEAEIKAKKWLKQV--GLP---TDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDpRAREEMMQIFVN 190
Cdd:cd03288 122 TDDRLWEALEIAQLKNMvkSLPgglDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVM 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323465851 191 YQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPRKIFENKE 237
Cdd:cd03288 201 TAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQED 246
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-221 |
7.98e-10 |
|
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: 57.73 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQFPetQLFENT 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP--WLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFGPKnFGVSDKEAEIKAKKWLKQVGL----PTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDP 178
Cdd:cd03290 95 VEENITFGSP-FNKQRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 323465851 179 RAREEMMQ--IFVNYQKAGHTVILVTHNMDDVAkYADDVLVMEHG 221
Cdd:cd03290 174 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-224 |
8.96e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.88 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKK-------LRKEVGLVFQFPe 95
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipeDRLGRGLVPDMS- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 tqLFENTVLEDVKFGP--KNFGVSDKEAEIKAKKWLKQVglptDVISKSPFE----LSGGQMRRVAIAGVMVNEPQILCL 169
Cdd:COG3845 353 --VAENLILGRYRRPPfsRGGFLDRKAIRAFAEELIEEF----DVRTPGPDTparsLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 170 DEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-221 |
1.46e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKFENINYIYSPGTTMEKKGLDNISFELLDNS--------FIALIGHTGSGKSTLMQHFNAllKPSSGTID------- 65
Cdd:PLN03140 866 LAMSFDDVNYFVDMPAEMKEQGVTEDRLQLLREVtgafrpgvLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdirisg 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 66 ----------IAGY------HiTPQTGNKN------LKKLRKEVGLvfqfPETQLFENTVLEDVKFgpknfgVSDKEAei 123
Cdd:PLN03140 944 fpkkqetfarISGYceqndiH-SPQVTVREsliysaFLRLPKEVSK----EEKMMFVDEVMELVEL------DNLKDA-- 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 124 kakkwlkQVGLPtDVISkspfeLSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:PLN03140 1011 -------IVGLP-GVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
250
....*....|....*....
gi 323465851 204 NMD-DVAKYADDVLVMEHG 221
Cdd:PLN03140 1078 QPSiDIFEAFDELLLMKRG 1096
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-221 |
1.65e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINyIYSP-GTTMekkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDI-AGYHIT--PQ--- 74
Cdd:COG4178 362 ALALEDLT-LRTPdGRPL----LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflPQrpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 75 --TGNknlkkLRkEVgLVFQFPETQlfentvledvkfgpknfgVSDkeAEIKAkkWLKQVGLPT-----DVISKSPFELS 147
Cdd:COG4178 437 lpLGT-----LR-EA-LLYPATAEA------------------FSD--AELRE--ALEAVGLGHlaerlDEEADWDQVLS 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 148 GGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNyQKAGHTVILVTHNmDDVAKYADDVLVMEHG 221
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-221 |
2.12e-09 |
|
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: 57.17 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG-YHITPQTGnknlkklrkevglvFQFPETqLFEN 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFS--------------WIMPGT-IKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVledvkfgpknFGVSdkEAEIKAKKWLKQVGLPTDvISKSP-----------FELSGGQMRRVAIAGVMVNEPQILCLD 170
Cdd:cd03291 118 II----------FGVS--YDEYRYKSVVKACQLEED-ITKFPekdntvlgeggITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 323465851 171 EPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHG 221
Cdd:cd03291 185 SPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-224 |
3.95e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.87 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 11 IYSPGttmeKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGtidiagyHITPQTGNKnlkklrkeVGLV 90
Cdd:TIGR03719 13 VVPPK----KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQPGIK--------VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 91 FQfpETQLFEN-TVLEDVKFG-PKNFGVSDKEAEIKAK---------KWLKQVGLPTDVIS-------KSPFE------- 145
Cdd:TIGR03719 74 PQ--EPQLDPTkTVRENVEEGvAEIKDALDRFNEISAKyaepdadfdKLAAEQAELQEIIDaadawdlDSQLEiamdalr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 146 ----------LSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaghTVILVTHN---MDDVAKYa 212
Cdd:TIGR03719 152 cppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDryfLDNVAGW- 227
|
250
....*....|..
gi 323465851 213 ddVLVMEHGKLI 224
Cdd:TIGR03719 228 --ILELDRGRGI 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-223 |
4.10e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 16 TTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLK-------KLRKEVG 88
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvtEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 89 LvfqFPETQLFENTVLEDVKFGPKNFGVSDKEAEIKAKKWL------KQVGLPTDVISkspfeLSGGQMRRVAIAGVMVN 162
Cdd:PRK10982 337 I---YAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVidsmrvKTPGHRTQIGS-----LSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-221 |
4.86e-09 |
|
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: 57.23 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG-YHITPQTgnknlkklrkevglvfqfpeTQLFEN 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQT--------------------SWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 102 TVLEDVKfgpknFGVSDKE----AEIKAKKWLKQVGLPTD----VISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:TIGR01271 502 TIKDNII-----FGLSYDEyrytSVIKACQLEEDIALFPEkdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHG 221
Cdd:TIGR01271 577 THLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-236 |
5.99e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 24 DNISFElldnsfIA------LIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPqtgnKNLKkLRKEVGLVfqfpeTQ 97
Cdd:NF033858 283 DHVSFR------IRrgeifgFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA----GDIA-TRRRVGYM-----SQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 98 LF----ENTVLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPG 173
Cdd:NF033858 347 AFslygELTVRQNLELHARLFHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 174 AGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDvAKYADDVLVMEHGKLIKHDKPRKIFENK 236
Cdd:NF033858 426 SGVDPVARDMFWRLLIELsREDGVTIFISTHFMNE-AERCDRISLMHAGRVLASDTPAALVAAR 488
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-241 |
7.25e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTtmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGT-IDIAGyhitpqtgnknl 80
Cdd:PLN03232 614 AISIKNGYFSWDSKT--SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRG------------ 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 kklrkEVGLVFQFPetQLFENTVLEDVKFGpknfgvSDKEAEiKAKKWLKQVGLPTDV----------ISKSPFELSGGQ 150
Cdd:PLN03232 680 -----SVAYVPQVS--WIFNATVRENILFG------SDFESE-RYWRAIDVTALQHDLdllpgrdlteIGERGVNISGGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKLIKHDKPR 230
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFA 824
|
250
....*....|.
gi 323465851 231 KIFENKEWLKK 241
Cdd:PLN03232 825 ELSKSGSLFKK 835
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-232 |
9.43e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 27 SFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgNKNLKKLRKEVGLVFQFPETQLfentvled 106
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHIT----RLSFEQLQKLVSDEWQRNNTDM-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 107 VKFGPKNFGVSDKEA---EIKA----KKWLKQVGLpTDVISKsPFE-LSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDP 178
Cdd:PRK10938 91 LSPGEDDTGRTTAEIiqdEVKDparcEQLAQQFGI-TALLDR-RFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 323465851 179 RAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLIKHDKPRKI 232
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-219 |
1.03e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.72 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFE-----LLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHIT--PQTgnknLKKlrKEVGLVFQ 92
Cdd:cd03237 7 KKTLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykPQY----IKA--DYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 FpetqLFENTvledvkfgpKNFGVSDK-EAEIkakkwLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:cd03237 81 L----LSSIT---------KDFYTHPYfKTEI-----AKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 323465851 172 PGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVME 219
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-224 |
4.52e-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: 52.26 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 7 NINYIYSPGTTmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPS---SGTIDIAGYhitpqTGNKNLKKL 83
Cdd:cd03233 8 NISFTTGKGRS-KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI-----PYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 RKEVGLVFQ----FPETqlfenTVLEDVKFGpknfgvsdkeAEIKAKKWLKQVglptdviskspfelSGGQMRRVAIAGV 159
Cdd:cd03233 82 PGEIIYVSEedvhFPTL-----TVRETLDFA----------LRCKGNEFVRGI--------------SGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVT--HNMDDVAKYADDVLVMEHGKLI 224
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-223 |
5.05e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 20 KKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTI----DIAgyhITPQTG---NKNLKklrkevGLVFQ 92
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIA---YVPQQAwimNATVR------GNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 93 FPEtqlfENTV-LEDVkfgpknFGVSDKEAEikakkwLKQV--GLPTDVISKSpFELSGGQMRRVAIAGVMVNEPQILCL 169
Cdd:PTZ00243 744 FDE----EDAArLADA------VRVSQLEAD------LAQLggGLETEIGEKG-VNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 323465851 170 DEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKyADDVLVMEHGKL 223
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-224 |
6.19e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpQTGNKNLKKLRKEVGLVFQFPETQLFE 100
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG-----KEVTFNGPKSSQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 101 N-TVLEDVKFG--PKN-FGVSD-KEAEIKAKKWLKQVGLPTDviSKSPF-ELSGGQMRRVAIAGVMVNEPQILCLDEPGA 174
Cdd:PRK10762 93 QlTIAENIFLGreFVNrFGRIDwKKMYAEADKLLARLNLRFS--SDKLVgELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 323465851 175 GLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-234 |
7.16e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMqhfnALL----KPSSGTI-----DIA--------GYHIT--PQTGNKNLkkl 83
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLIagarKIQQGRVevlggDMAdarhrravCPRIAymPQGLGKNL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 rkevglvfqFPETQLFENtvledVKFGPKNFGVSDKEAEIKAKKWLKQVGLptdviskSPF------ELSGGQMRRVAIA 157
Cdd:NF033858 90 ---------YPTLSVFEN-----LDFFGRLFGQDAAERRRRIDELLRATGL-------APFadrpagKLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 158 GVMVNEPQILCLDEPGAGLDPRAR-------EEMMQifvnyQKAGHTVILVTHNMDDVAKYadDVLV-MEHGKLIKHDKP 229
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRrqfweliDRIRA-----ERPGMSVLVATAYMEEAERF--DWLVaMDAGRVLATGTP 221
|
....*
gi 323465851 230 RKIFE 234
Cdd:NF033858 222 AELLA 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-224 |
1.01e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNSFIALIGHTGSGKSTLMqhfnallKPSSGTIDIAGYH--ITPQTGNKNLKKLR-----------KEV 87
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLM-------KVLSGVYPHGSYEgeILFDGEVCRFKDIRdsealgiviihQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 88 GLVfqfPETQLFENTVL--EdvkfgPKNFGVSD-KEAEIKAKKWLKQVGL---PTDVISKspfeLSGGQMRRVAIAGVMV 161
Cdd:NF040905 88 ALI---PYLSIAENIFLgnE-----RAKRGVIDwNETNRRARELLAKVGLdesPDTLVTD----IGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 162 NEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-224 |
1.25e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAgyhitpqtgnKNLK--KL-----RKEVGLVFQFPE 95
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----------QDLIvaRLqqdppRNVEGTVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 96 TQLFE--------NTVLEDVKFGPknfgvSDKE----AEIKAK-----KW---------LKQVGLPTDvisKSPFELSGG 149
Cdd:PRK11147 89 EGIEEqaeylkryHDISHLVETDP-----SEKNlnelAKLQEQldhhnLWqlenrinevLAQLGLDPD---AALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 150 QMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAghtVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-203 |
1.57e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 17 TMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITpqtgnkNLKK-----LRKEVGLVf 91
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN------NIAKpyctyIGHNLGLK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 92 qfpetqlFENTVLEDVKFGPKNFGVSdkEAEIKAKKWLKQvglpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:PRK13541 83 -------LEMTVFENLKFWSEIYNSA--ETLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
170 180 190
....*....|....*....|....*....|..
gi 323465851 172 PGAGLDPRAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:PRK13541 150 VETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
146-221 |
2.41e-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: 49.63 E-value: 2.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 146 LSGGQMRRVAIAGVMVNEPQ--ILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNmDDVAKYADDVLVMEHG 221
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDFGPG 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-223 |
2.97e-07 |
|
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: 51.48 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMqhfNALLkpssGTIDIAGYHITPQtgnknlkklrkevGLVFQFPETQLFENT 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL---SALL----AEMDKVEGHVHMK-------------GSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VL-EDVKFG----PKNFGVSDKEAEIKAKKWLKQVGLPTDVISKSpFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:TIGR00957 714 SLrENILFGkalnEKYYQQVLEACALLPDLEILPSGDRTEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 323465851 178 PRAREEMMQIFVNYQK--AGHTVILVTHNMDDVAKyADDVLVMEHGKL 223
Cdd:TIGR00957 793 AHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQ-VDVIIVMSGGKI 839
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-203 |
3.60e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 6 ENINYIYSpgttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIdiagyhitpQTGNKnlkklrK 85
Cdd:PRK11147 323 ENVNYQID-----GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------HCGTK------L 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 86 EVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAEIkakkwlkqVGLPTDVI-----SKSPFE-LSGGQMRRVAIAGV 159
Cdd:PRK11147 383 EVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGRPRHV--------LGYLQDFLfhpkrAMTPVKaLSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 323465851 160 MVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaghTVILVTH 203
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSH 495
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-203 |
3.95e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 50.77 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 21 KGLDNISFELLDNsFIALIGHTGSGKSTLMQHFNALLKPSSG-TIDIAGYHItpqtgNKNLKKLRKEVGLVFQFPETQLF 99
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYL-----GDDPDLPEIEIELTFGSLLSRLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 100 ENTVLEDV---------------------------KFGPKNFGVSD---KEAEIKAKKWLKQVGLPTDVISKSPFELSG- 148
Cdd:COG3593 86 RLLLKEEDkeeleealeelneelkealkalnellsEYLKELLDGLDlelELSLDELEDLLKSLSLRIEDGKELPLDRLGs 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 149 GQMRRVAIA-------GVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:COG3593 166 GFQRLILLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2-204 |
4.29e-07 |
|
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: 50.47 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENINYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLK 81
Cdd:pfam13304 107 REPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KL---RKEVGLVFQFPETQLFENTVLEDVKFGPKNFGVSDKEAeikakKWLkqvglptdviskSPFELSGGQMRRVAIAG 158
Cdd:pfam13304 187 RLvrgLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGG-----GEL------------PAFELSDGTKRLLALLA 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 323465851 159 VM---VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN 204
Cdd:pfam13304 250 ALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-209 |
4.36e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 10 YIYS--------PGttmEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIdiagyhiTPQTGNKnlk 81
Cdd:PRK11819 5 YIYTmnrvskvvPP---KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA-------RPAPGIK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 klrkeVGLVFQfpETQLFEN-TVLEDVK--FGPK------------NFGVSDK------------EAEIKAKK-W----- 128
Cdd:PRK11819 72 -----VGYLPQ--EPQLDPEkTVRENVEegVAEVkaaldrfneiyaAYAEPDAdfdalaaeqgelQEIIDAADaWdldsq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 129 LKQ----VGLP---TDVISkspfeLSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYqkAGhTVILV 201
Cdd:PRK11819 145 LEIamdaLRCPpwdAKVTK-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PG-TVVAV 216
|
250
....*....|.
gi 323465851 202 THN---MDDVA 209
Cdd:PRK11819 217 THDryfLDNVA 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-203 |
4.45e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 37 ALI--GHTGSGKSTLMQHFNALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLVFQFpetqlfenTVLEDVKFgpkNF 114
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADL--------STLENLHF---LC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 115 GVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKA 194
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRG 186
|
....*....
gi 323465851 195 GHTVILVTH 203
Cdd:PRK13543 187 GGAALVTTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-236 |
4.61e-07 |
|
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: 51.10 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMEkkgLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGYHItpqtGNKNLKK 82
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV---LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----AKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 83 LRKEVGLVFQFPetQLFENTVLEDVK-FGpknfGVSDKEAEikakkWLKQVGLPTDVISKSP----FE-------LSGGQ 150
Cdd:TIGR00957 1358 LRFKITIIPQDP--VLFSGSLRMNLDpFS----QYSDEEVW-----WALELAHLKTFVSALPdkldHEcaeggenLSVGQ 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRArEEMMQIFVNYQKAGHTVILVTHNMDDVAKYAdDVLVMEHGKLIKHDKPR 230
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPS 1504
|
....*.
gi 323465851 231 KIFENK 236
Cdd:TIGR00957 1505 NLLQQR 1510
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-216 |
2.00e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQH--FNALLKPSSGTIDIAGYHiTPQTGNKNLKKLRkevgLVFQFP------ 94
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDtlYPALARRLHLKKEQPGNH-DRIEGLEHIDKVI----VIDQSPigrtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 95 -----ETQLFE---------------NTVLEDVKFGPKNfgVSD------KEAE--------IKAK-KWLKQVGLPTDVI 139
Cdd:cd03271 86 snpatYTGVFDeirelfcevckgkryNRETLEVRYKGKS--IADvldmtvEEALeffenipkIARKlQTLCDVGLGYIKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 140 SKSPFELSGGQMRRVAIAGVMVNE---PQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVL 216
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-216 |
3.77e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 3.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 146 LSGGQMRRVAIAGVMVN---EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVL 216
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-244 |
3.84e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 129 LKQVGLPTDVISKSPFELSGGQMRRVAIA--------GVMvnepqiLCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVIL 200
Cdd:PRK00635 460 LIDLGLPYLTPERALATLSGGEQERTALAkhlgaeliGIT------YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLL 533
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 323465851 201 VTHNmDDVAKYADDVLVME------HGKLIKHDKPRKIFENKEWLKKHYL 244
Cdd:PRK00635 534 VEHD-EQMISLADRIIDIGpgagifGGEVLFNGSPREFLAKSDSLTAKYL 582
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-205 |
5.34e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 1 MSIKfeniNYIYSPGTTMEKKGLDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIagyhitpqtgnknl 80
Cdd:PLN03130 615 ISIK----NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-------------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 81 kkLRKEVGLVFQFpeTQLFENTVLEDVKFGpknfgvSDKEAEiKAKKWLKQVGLPTDV----------ISKSPFELSGGQ 150
Cdd:PLN03130 677 --IRGTVAYVPQV--SWIFNATVRDNILFG------SPFDPE-RYERAIDVTALQHDLdllpggdlteIGERGVNISGGQ 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323465851 151 MRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNM 205
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQL 800
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-203 |
1.92e-05 |
|
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: 45.90 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 3 IKFENINYIYSPGTTMekkgLDNISFELLDNSFIALIGHTGSGKSTLMQ-------HFNALL-KPSSGTIdiagYHItPQ 74
Cdd:TIGR00954 452 IKFENIPLVTPNGDVL----IESLSFEVPSGNNLLICGPNGCGKSSLFRilgelwpVYGGRLtKPAKGKL----FYV-PQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 75 TGNKNLKKLRKEVglvfqfpetqlfentVLEDVKFGPKNFGVSDKEAEikakKWLKQVGLPT--------DVISKSPFEL 146
Cdd:TIGR00954 523 RPYMTLGTLRDQI---------------IYPDSSEDMKRRGLSDKDLE----QILDNVQLTHilereggwSAVQDWMDVL 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323465851 147 SGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPrareEMMQ-IFVNYQKAGHTVILVTH 203
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGyMYRLCREFGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-177 |
2.11e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 25 NISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIdiagyHITPqtgNKNLKKLRKEvglvfQFPetqlFEN-TV 103
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLDP---NERLGKLRQD-----QFA----FEEfTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 104 LEDVKFGPKN----------------------FGVSDKE----------AEIKAKKWLKQVGLPTDVISKSPFELSGGQM 151
Cdd:PRK15064 82 LDTVIMGHTElwevkqerdriyalpemseedgMKVADLEvkfaemdgytAEARAGELLLGVGIPEEQHYGLMSEVAPGWK 161
|
170 180
....*....|....*....|....*.
gi 323465851 152 RRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-204 |
2.14e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 2.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 146 LSGGQMRRVAIAGVM----VNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHN 204
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
146-223 |
2.17e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 2.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323465851 146 LSGGQMRRvAIAGVMVNEP-QILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK11288 397 LSGGNQQK-AILGRWLSEDmKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-203 |
2.66e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMqhfNALLKPSSGTIDIAGYHITpqTGNKNLKKLRKEVGLVFQfPETQLFENT 102
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLV--NGRPLDSSFQRSIGYVQQ-QDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFG-----PKNfgVSDKEAEIKAKKWLKQVGLPT--DVISKSPFE-LSGGQMRRVAIAGVMVNEPQ-ILCLDEPG 173
Cdd:TIGR00956 853 VRESLRFSaylrqPKS--VSKSEKMEYVEEVIKLLEMESyaDAVVGVPGEgLNVEQRKRLTIGVELVAKPKlLLFLDEPT 930
|
170 180 190
....*....|....*....|....*....|
gi 323465851 174 AGLDPRAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-223 |
2.93e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAGyhitpqtgnkNLKKLRKEVGLVFQFpetqlfenT 102
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------EVSVIAISAGLSGQL--------T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 103 VLEDVKFGPKNFGVSDKEAEIKAKKWLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRARE 182
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 323465851 183 EMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKL 223
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-205 |
3.16e-05 |
|
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: 44.28 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 38 LIGHTGSGKSTLMQHFNALLKPSSGTIDiagyhiTPQTGNKNLKKLRkevGLVFQFPETQLFENTVLEDVKfgPKNFGVS 117
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFD------DPPDWDEILDEFR---GSELQNYFTKLLEGDVKVIVK--PQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 118 DKEAEIKAKKWLKQV---GLPTDVISKSPFE---------LSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMM 185
Cdd:cd03236 100 PKAVKGKVGELLKKKderGKLDELVDQLELRhvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180
....*....|....*....|
gi 323465851 186 QIFVNYQKAGHTVILVTHNM 205
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-219 |
3.92e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 3.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323465851 145 ELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNY-QKAGHTVILVTHNMDDVAKYADDVLVME 219
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLsEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
145-205 |
4.63e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 4.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 145 ELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNM 205
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
37-225 |
6.13e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 37 ALIGHTGSGKSTLmqhfNALL------KPSSGTIDIAGyhitpqtgnKNLKKLRKE------VGLVFQFP------ETQL 98
Cdd:PRK09580 31 AIMGPNGSGKSTL----SATLagredyEVTGGTVEFKG---------KDLLELSPEdragegIFMAFQYPveipgvSNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 99 FENTVLEDVK--FGPKNFGVSDKEAEIKAKkwLKQVGLPTDVISKSPFE-LSGGQMRRVAIAGVMVNEPQILCLDEPGAG 175
Cdd:PRK09580 98 FLQTALNAVRsyRGQEPLDRFDFQDLMEEK--IALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 323465851 176 LDPRAREEMMQIFVNYQKAGHTVILVTH--NMDDVAKyADDVLVMEHGKLIK 225
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFIIVTHyqRILDYIK-PDYVHVLYQGRIVK 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-216 |
7.65e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 129 LKQVGLPTDVISKSPFELSGGQMRRVAIA---GVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNM 205
Cdd:TIGR00630 813 LCDVGLGYIRLGQPATTLSGGEAQRIKLAkelSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
90
....*....|.
gi 323465851 206 dDVAKYADDVL 216
Cdd:TIGR00630 893 -DVIKTADYII 902
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-68 |
8.28e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 8.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 323465851 23 LDNISFELLDNSFIALIGHTGSGKSTLMQHFNALLKPSSGTIDIAG 68
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-207 |
8.36e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 33 NSFIALIGHTGSGKSTLMQHF-NALLKPSSGTIDIAGYHITPQTGNKNLKKLRKEVGLvfqfpetqlfentvledvkfgp 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 112 knfgvsdkeaeikakkwlkqvglptdviskspfELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQI---- 187
Cdd:smart00382 60 ---------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelr 106
|
170 180
....*....|....*....|..
gi 323465851 188 --FVNYQKAGHTVILVTHNMDD 207
Cdd:smart00382 107 llLLLKSEKNLTVILTTNDEKD 128
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-225 |
1.30e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 19 EKKGLDNISFELLDNSFIALIGHTGSGKSTLMQ----HfnallkPS----SGTIDIAGYHITPQTGNKnlkklRKEVG-- 88
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKviagH------PAykilEGDILFKGESILDLEPEE-----RAHLGif 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 89 LVFQFPetqlFENTVLEDVKF-------GPKNFGVSDKEA----EIKAKKwLKQVGLPTDVISKSPFE-LSGGQMRRVAI 156
Cdd:CHL00131 88 LAFQYP----IEIPGVSNADFlrlaynsKRKFQGLPELDPleflEIINEK-LKLVGMDPSFLSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 157 AGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTH--NMDDVAKyADDVLVMEHGKLIK 225
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYIK-PDYVHVMQNGKIIK 232
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
2-203 |
1.68e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.26 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 2 SIKFENInyiyspgttmekKGLDNISFELLDnsFIALIGHTGSGKSTLMQHFNALLkpSSGTIDIAGYHITPQTGNKNLK 81
Cdd:COG4938 3 SISIKNF------------GPFKEAELELKP--LTLLIGPNGSGKSTLIQALLLLL--QSNFIYLPAERSGPARLYPSLV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 82 KLRKEVGLvFQFPETQLFENTVLEDVKFGPKNFGVSDKEAeikakkWLKQVGLPTDVISKSPFELS-------GGQMRRV 154
Cdd:COG4938 67 RELSDLGS-RGEYTADFLAELENLEILDDKSKELLEQVEE------WLEKIFPGKVEVDASSDLVRlvfrpsgNGKRIPL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323465851 155 AIAGVMVNE--------------PQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTH 203
Cdd:COG4938 140 SNVGSGVSEllpillallsaakpGSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
121-234 |
1.89e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 121 AEIKAKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaghTVIL 200
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK---TFIV 396
|
90 100 110
....*....|....*....|....*....|....
gi 323465851 201 VTHNMDDVAKYADDVLVMEHGKLIKHDKPRKIFE 234
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFE 430
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
36-239 |
2.67e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLmqhfnalLKPSSGTIDiaGYHITPQ--------TGNKNLKKLRKEVGLVFQ----FPETqlfenTV 103
Cdd:TIGR00956 90 TVVLGRPGSGCSTL-------LKTIASNTD--GFHIGVEgvitydgiTPEEIKKHYRGDVVYNAEtdvhFPHL-----TV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 104 LEDVKF-----GPKN--FGVSDKE-AEIKAKKWLKQVGLP----TDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDE 171
Cdd:TIGR00956 156 GETLDFaarckTPQNrpDGVSREEyAKHIADVYMATYGLShtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 172 PGAGLDP-------RAREEMMQIFvnyqkagHTVILVT--HNMDDVAKYADDVLVMEHGKLI---KHDKPRKIFENKEWL 239
Cdd:TIGR00956 236 ATRGLDSatalefiRALKTSANIL-------DTTPLVAiyQCSQDAYELFDKVIVLYEGYQIyfgPADKAKQYFEKMGFK 308
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-177 |
3.09e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLMQHFNALLKPSSGTIDiagyhitpqtgnKNLKKLRKEvglvfQFPETQlFENTVLEDVKFGPKNFG 115
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------PELKISYKP-----QYIKPD-YDGTVEDLLRSITDDLG 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 116 VSDKEAEIkakkwLKQVGLPtDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:PRK13409 430 SSYYKSEI-----IKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-177 |
6.30e-04 |
|
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: 40.92 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 36 IALIGHTGSGKSTLMQHFNALLKPSSGTIDiagyhitpqtgnKNLKKLRKEvglvfQFPETQlFENTVlEDV--KFGPKN 113
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVD------------EDLKISYKP-----QYISPD-YDGTV-EEFlrSANTDD 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323465851 114 FGVSDKEAEIkakkwLKQVGLpTDVISKSPFELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLD 177
Cdd:COG1245 430 FGSSYYKTEI-----IKPLGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
145-205 |
7.72e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 7.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323465851 145 ELSGGQMRRVAIAGVMVNEPQILCLDEPGAGLDPRAREEMMQIFVNYQKaGHTVILVTHNM 205
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEHDL 271
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
163-244 |
2.39e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMdDVAKYADDVLVMEHG------KLIKHDKPRKIFENK 236
Cdd:PRK00635 1720 HPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLIEMGPGsgktggKILFSGPPKDISASK 1798
|
....*...
gi 323465851 237 EWLKKHYL 244
Cdd:PRK00635 1799 DSLLKTYM 1806
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
84-224 |
3.31e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 84 RKEVGLVFqfpETQLFENTVLEDVKfGPKNFGVSDKEAEIK-AKKWLKQVGLPTDVISKSPFELSGGQMRRVAIAGVMVN 162
Cdd:NF040905 346 RKGYGLNL---IDDIKRNITLANLG-KVSRRGVIDENEEIKvAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFT 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323465851 163 EPQILCLDEPGAGLDPRAREEMMQIFVNYQKAGHTVILVTHNMDDVAKYADDVLVMEHGKLI 224
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
146-216 |
4.23e-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: 37.59 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323465851 146 LSGGQ------MRRVAIAGVMVNEPQILCLDEPGAGLDPRARE-------EMMQIFVNYQkaghtVILVTHNmDDVAKYA 212
Cdd:cd03240 116 CSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEeslaeiiEERKSQKNFQ-----LIVITHD-EELVDAA 189
|
....
gi 323465851 213 DDVL 216
Cdd:cd03240 190 DHIY 193
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
35-82 |
9.44e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.29 E-value: 9.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 323465851 35 FIALIGHTGSGKSTLmqhFNALLKPSSGTIDIAGYHITPQTGNKNLKK 82
Cdd:pfam01926 1 RVALVGRPNVGKSTL---INALTGAKAIVSDYPGTTRDPNEGRLELKG 45
|
|
| |
