|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
41-244 |
2.69e-80 |
|
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: 240.83 E-value: 2.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPK 107
Cdd:cd03225 1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkelrRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPDHQVVMPTVEADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:cd03225 78 GLVFQNPDDQFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 188 LLDELTTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEELK-YADGAVYMENGR 244
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK---TIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
40-254 |
1.43e-75 |
|
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: 229.53 E-value: 1.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN------- 108
Cdd:COG1122 1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNlrelrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:COG1122 77 vgLVFQNPDDQLFAPTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL---NKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
40-249 |
3.17e-65 |
|
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: 204.59 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVstrQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN------ 108
Cdd:TIGR04520 1 IEVENVSFSY---PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtlDEENlweirk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQNPDHQVVMPTVEADVAFGL---GkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:TIGR04520 78 kvgMVFQNPDNQFVGATVEDDVAFGLenlG----VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKL-NKEEG-ITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
39-254 |
4.85e-56 |
|
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: 180.62 E-value: 4.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN--- 108
Cdd:COG1120 1 MLEAENLSVGYGGR-----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslSRRElar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQnpDHQVVMP-TVEADVAFGLGKYHDMNQ---EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:COG1120 76 riaYVPQ--EPPAPFGlTVRELVALGRYPHLGLFGrpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 182 EACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRL--ARERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-254 |
1.37e-53 |
|
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: 181.25 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPK 107
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltklSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 N---------FVFQNPDHQVV-MPTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAI 176
Cdd:COG1123 336 SlrelrrrvqMVFQDPYSSLNpRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDL--QRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
36-249 |
1.01e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 172.96 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 36 DNVAVECRNLCFS-VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN- 108
Cdd:PRK13633 1 MNEMIKCKNVSYKyESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --------FVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIA 177
Cdd:PRK13633 81 wdirnkagMVFQNPDNQIVATIVEEDVAFGpenLG----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 178 GALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKEL-NKKYG-ITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
36-254 |
1.34e-52 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 172.10 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 36 DNVAVECRNLCFSVSTRqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKNF-- 109
Cdd:PRK13632 4 KSVMIKVENVSFSYPNS---ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitiSKENLke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -------VFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:PRK13632 81 irkkigiIFQNPDNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDL--RKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
35-254 |
7.59e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.80 E-value: 7.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----EKPKN- 108
Cdd:COG1121 2 MMMPAIELENLTVSYGGR-----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkppRRARRr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDHQVVMP-TVEaDVAfGLGKYHDMN-----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGAL 180
Cdd:COG1121 77 igYVPQRAEVDWDFPiTVR-DVV-LMGRYGRRGlfrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 181 AEACKVLLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMeNGRVVRHGDAATI 254
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLREL---RREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
56-249 |
6.37e-49 |
|
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: 160.76 E-value: 6.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPdhqVVMP--T 122
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppeRRNIGMVFQDY---ALFPhlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:cd03259 89 VAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLRE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLInaKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:cd03259 168 ELREELKELQ--RELGITTIYVTHDQEEaLALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
39-254 |
1.68e-48 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 167.77 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLcfSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTVFVE----------- 104
Cdd:COG1123 4 LLEVRDL--SVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 --KPKNFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:COG1123 81 rgRRIGMVFQDPMTQLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLREL--QRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
58-254 |
2.41e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 161.72 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------------EKPKNFVFQNPDHQVVMPTVE 124
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlseetvwdvRRQVGMVFQNPDNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:PRK13635 101 DDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23296450 205 IKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13635 180 LETVRQL--KEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
40-245 |
4.55e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 160.67 E-value: 4.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN------- 108
Cdd:PRK13650 5 IEVKNLTFKYKEDQ--EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllTEENvwdirhk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK13650 83 igMVFQNPDNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
40-254 |
4.92e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 4.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------EKPKN-- 108
Cdd:COG1131 1 IEVRGLTKRYG-----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpAEVRRri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -FVFQNPdhqVVMP--TVEADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACK 185
Cdd:COG1131 76 gYVPQEP---ALYPdlTVRENLRF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 186 VLLLDELTTFLD-ESdqmgvIKAVKDLINA-KKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1131 152 LLILDEPTSGLDpEA-----RRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDEL 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
60-267 |
6.93e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 157.61 E-value: 6.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK----PKNF---------VFQNPDHQVVMPTVEAD 126
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitDDNFeklrkhigiVFQNPDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 127 VAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIK 206
Cdd:PRK13648 105 VAFGL-ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 207 AVKDLINAKkgDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATISDFIKAKQSSYID 267
Cdd:PRK13648 184 LVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLD 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
37-247 |
8.96e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.97 E-value: 8.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 37 NVAVECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN- 108
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---------FVFQnpDHQVVmP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIA 177
Cdd:COG1136 81 arlrrrhigFVFQ--FFNLL-PelTALENVALPL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 178 GALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVR 247
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLREL--NRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-249 |
1.28e-46 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 153.75 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknfvfQNPDHqvvM 120
Cdd:cd03214 1 EVENLSVGYGGR-----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG------KDLAS---L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTVEA--DVAFglgkyhdMNQeevksrvikALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDE 198
Cdd:cd03214 67 SPKELarKIAY-------VPQ---------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23296450 199 SDQMGVIKAVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHG 249
Cdd:cd03214 131 AHQIELLELLRRL--ARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
41-249 |
1.92e-46 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 154.61 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKN------FVFQ 112
Cdd:cd03235 1 EVEDLTVSYGGH-----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgKPLEKerkrigYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 NPDHQVVMP-TVEADVAFGLgkYHDMN-----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:cd03235 76 RRSIDRDFPiSVRDVVLMGL--YGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLEE-LKYADGAVYMeNGRVVRHG 249
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL--RREG-MTILVVTHDLGLvLEYFDRVLLL-NRTVVASG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
35-246 |
1.65e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.71 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN----- 108
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgKPVTgpgpd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhqVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:COG1116 82 rgVVFQEP---ALLPwlTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 185 KVLLLDEltTF--LDE--SDQMGvikavKDLIN-AKKGDVTALWVTHRLEElkyadgAVYMENgRVV 246
Cdd:COG1116 158 EVLLMDE--PFgaLDAltRERLQ-----DELLRlWQETGKTVLFVTHDVDE------AVFLAD-RVV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
39-254 |
4.09e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 4.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------EKPK- 107
Cdd:COG3842 5 ALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtglppEKRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPD---HqvvMpTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:COG3842 80 GMVFQDYAlfpH---L-TVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 185 KVLLLDELTTFLDES--DQMgvIKAVKDLInaKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG3842 155 RVLLLDEPLSALDAKlrEEM--REELRRLQ--RELGITFIYVTHDQEEaLALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
40-245 |
7.18e-44 |
|
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: 148.02 E-value: 7.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---- 108
Cdd:cd03255 1 IELKNLSKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ------FVFQnpDHQVVmP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGAL 180
Cdd:cd03255 80 rrrhigFVFQ--SFNLL-PdlTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 181 AEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLREL--NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
40-246 |
8.92e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 145.31 E-value: 8.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN-------FVF 111
Cdd:cd03293 1 LEVRNVSKTYGGGGG-AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgEPVTgpgpdrgYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 112 QNPdhqVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03293 80 QQD---ALLPwlTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 190 DEltTF--LDE--SDQMGvikavKDLINA-KKGDVTALWVTHRLEElkyadgAVYMENgRVV 246
Cdd:cd03293 156 DE--PFsaLDAltREQLQ-----EELLDIwRETGKTVLLVTHDIDE------AVFLAD-RVV 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
40-249 |
9.03e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 147.15 E-value: 9.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVStrQGISVpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF---------------VE 104
Cdd:PRK13639 2 LETRDLKYSYP--DGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikydkkslleVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 KPKNFVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:PRK13639 78 KTVGIVFQNPDDQLFAPTVEEDVAFGplnLG----LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 182 EACKVLLLDELTTFLDEsdqMGVIKAVKDLINAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDP---MGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
35-254 |
1.20e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 146.87 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNvAVECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSS---------GTVFVEK 105
Cdd:PRK13640 2 KDN-IVEFKHVSF---TYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PK-------NFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAG 178
Cdd:PRK13640 78 TVwdirekvGIVFQNPDNQFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 179 ALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKL--KKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
59-226 |
3.55e-42 |
|
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: 142.95 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF--------------VFQNPDHQVVMPTV 123
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgEPLDYsrkgllerrqrvglVFQDPDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:TIGR01166 87 DQDVAFGplnLG----LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*.
gi 23296450 201 QMGVIKAVKDLINAKKGDVTAlwvTH 226
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVIS---TH 185
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
41-245 |
2.07e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.49 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN----------- 108
Cdd:COG4619 2 ELEGLSFRVGGK-----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgKPLSampppewrrqv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -FVFQNPdhqvVM--PTVEADVAFGLGKYHDMNQEEvksRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:COG4619 77 aYVPQEP----ALwgGTVRDNLPFPFQLRERKFDRE---RALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 185 KVLLLDELTTFLDESDQMGVIKAVKDLINAKkgDVTALWVTHRLEELK-YADGAVYMENGRV 245
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEE--GRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
39-254 |
8.95e-41 |
|
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: 141.09 E-value: 8.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLcfSVSTRQGI-SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNF- 109
Cdd:COG1124 1 MLEVRNL--SVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvtrrRRKAFr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -----VFQ------NPDHqvvmpTVEADVAFGLgkyHDMNQEEVKSRVIKALEAVGM-RDYMQR-PIQtLSGGQKQRIAI 176
Cdd:COG1124 79 rrvqmVFQdpyaslHPRH-----TVDRILAEPL---RIHGLPDREERIAELLEQVGLpPSFLDRyPHQ-LSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKgdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERG--LTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
48-246 |
9.30e-41 |
|
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: 139.70 E-value: 9.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 48 SVSTRQGISvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK----------NFVFQNPDHQ 117
Cdd:cd03226 6 SFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrksiGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VVMPTVEADVAFGLGKYHDMNQeevksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03226 84 LFTDSVREELLLGLKELDAGNE-----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23296450 198 ESDQMGVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVV 246
Cdd:cd03226 159 YKNMERVGELIRELAAQGK---AVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
40-254 |
3.46e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 140.32 E-value: 3.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-------------VEKP 106
Cdd:PRK13652 4 IETRDLCYSYSG----SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitkenireVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 107 KNFVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGpinLG----LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 184 CKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDL--PETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
56-256 |
5.76e-40 |
|
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: 138.84 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------KPKNFVFQNPDhQVVMP---TV 123
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkeprEARRQIGVLPD-ERGLYdrlTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:COG4555 92 RENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 204 VIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATISD 256
Cdd:COG4555 171 LREILRALKKEGK---TVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
60-256 |
2.87e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 137.94 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN---------FVFQNPDHQVVMPTVEAD 126
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevNAENekwvrskvgLVFQDPDDQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 127 VAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK13647 101 VAFGpvnMG----LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 204 VIKAVKDLINAKKgdvTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK13647 177 LMEILDRLHNQGK---TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
56-271 |
7.91e-39 |
|
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: 7.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNpdhQVVMP--T 122
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlpphKRPVNTVFQN---YALFPhlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD----E 198
Cdd:cd03300 89 VFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDlklrK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 199 SDQMgvikAVKDLinAKKGDVTALWVTHRLEElkyadgavymengrvvrhgdAATISDFIKAKQSSYIDQIGS 271
Cdd:cd03300 168 DMQL----ELKRL--QKELGITFVFVTHDQEE--------------------ALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
41-244 |
1.83e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 131.98 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkpknfvfqnpdhqvvm 120
Cdd:cd00267 1 EIENLSFRYGGR-----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ptveadvafglgkyhdmNQEEVKSRVIKALEAVGMRdyMQrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:cd00267 60 -----------------GKDIAKLPLEELRRRIGYV--PQ-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23296450 201 QMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGR 244
Cdd:cd00267 116 RERLLELLREL---AEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
35-254 |
3.24e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 133.95 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------EK 105
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDR-----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqditglsEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PKN-------FVFQNP---DHqvvMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIA 175
Cdd:COG1127 76 ELYelrrrigMLFQGGalfDS---L-TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 176 IAGALAEACKVLLLDELTTFLD-ESdqMGVIkavKDLINA--KKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDA 251
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpIT--SAVI---DELIRElrDELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTP 226
|
...
gi 23296450 252 ATI 254
Cdd:COG1127 227 EEL 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
60-254 |
4.79e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 4.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------KPKN----FVFQNPD---HqvvMpTVE 124
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlPPRErrvgFVFQHYAlfpH---M-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFGLGKyHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALA-EAcKVLLLDE----------- 191
Cdd:COG1118 94 ENIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADRyPSQ-LSGGQRQRVALARALAvEP-EVLLLDEpfgaldakvrk 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 192 -----LTTFLDESdqmgvikavkdlinakkgDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1118 171 elrrwLRRLHDEL------------------GGTTVFVTHDQEEaLELADRVVVMNQGRIEQVGTPDEV 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
35-253 |
5.84e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 139.89 E-value: 5.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNF--- 109
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngVDLSDLdpa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 --------VFQNPdhQVVMPTVEADVAFGLgkyHDMNQEEVKsrviKALEAVGMRDYMQR-------PI----QTLSGGQ 170
Cdd:COG4988 408 swrrqiawVPQNP--YLFAGTIRENLRLGR---PDASDEELE----AALEAAGLDEFVAAlpdgldtPLgeggRGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLD-ESDQmgvikAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDaETEA-----EILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQG 553
|
....
gi 23296450 250 DAAT 253
Cdd:COG4988 554 THEE 557
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
49-252 |
1.27e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---------FVFQ 112
Cdd:COG2884 7 VSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlKRREipylrrrigVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 npDHQVVMP-TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:COG2884 87 --DFRLLPDrTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 192 LTTFLDESDQMGVIKAVKDlINaKKGdVTALWVTHRLEELKYADG-AVYMENGRVVRHGDAA 252
Cdd:COG2884 164 PTGNLDPETSWEIMELLEE-IN-RRG-TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARG 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
40-268 |
1.37e-37 |
|
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: 132.24 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--------------EK 105
Cdd:cd03261 1 IELRGLTKSFGGRT-----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisglseaelyRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PKNF--VFQNP---DHqvvMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYM-QRPIQtLSGGQKQRIAIAGA 179
Cdd:cd03261 76 RRRMgmLFQSGalfDS---L-TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEdLYPAE-LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 180 LAEACKVLLLDELTTFLDESdQMGVIkavKDLIN--AKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGdaaTISD 256
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPI-ASGVI---DDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG---TPEE 223
|
250
....*....|..
gi 23296450 257 fIKAKQSSYIDQ 268
Cdd:cd03261 224 -LRASDDPLVRQ 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
39-254 |
5.69e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.66 E-value: 5.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN--- 108
Cdd:COG3839 3 SLELENVSKSYG-----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvtdlPPKDrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -FVFQNPdhqVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACK 185
Cdd:COG3839 78 aMVFQSY---ALYPhmTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 186 VLLLDELTTFLDES--DQM-GVIKAV-KDLinakkgDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG3839 154 VFLLDEPLSNLDAKlrVEMrAEIKRLhRRL------GTTTIYVTHDQVEaMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
59-254 |
9.40e-37 |
|
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: 129.99 E-value: 9.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVN-----PSSGTVFVEkPKN----------------FVFQNPDhq 117
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLD-GKDiydldvdvlelrrrvgMVFQKPN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 vVMP-TVEADVAFGLgKYHDM-NQEEVKSRVIKALEAVGMRDYMQRPIQ--TLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:cd03260 92 -PFPgSIYDNVAYGL-RLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 194 TFLDESDQMgvikAVKDLINAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:cd03260 170 SALDPISTA----KIEELIAELKKEYTIVIVTHNMQQaARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
60-249 |
1.09e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 131.32 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------------KPKNFVFQNPDHQVVMPTVE 124
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkkvklsdirKKVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFG---LGkyhdMNQEEVKSRVIKALEAVGM--RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK13637 103 KDIAFGpinLG----LSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23296450 200 DQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13637 179 GRDEILNKIKEL--HKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
39-256 |
1.60e-36 |
|
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: 129.77 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNlcfsVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPK 107
Cdd:cd03296 2 SIEVRN----VSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpvqERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQnpdHQVVMP--TVEADVAFGL---GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:cd03296 77 GFVFQ---HYALFRhmTVFDNVAFGLrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 183 ACKVLLLDELTTFLD---ESDQMGVIKAVKDLINakkgdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:cd03296 154 EPKVLLLDEPFGALDakvRKELRRWLRRLHDELH-----VTTVFVTHDQEEaLEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
58-254 |
3.67e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 129.72 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------------KPKNFVFQNPDHQVVMPTV 123
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklqgirKLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK13644 96 EEDLAFGPENLC-LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23296450 204 VIKAVKDLinAKKGDvTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13644 175 VLERIKKL--HEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
39-249 |
5.43e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 135.73 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-------PKN--- 108
Cdd:COG2274 473 DIELENVSFRYPGD---SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidPASlrr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQNPdhQVVMPTVEADVAFGlgkYHDMNQEEVksrvIKALEAVGMRDY-------MQRPI----QTLSGGQKQRI 174
Cdd:COG2274 550 qigVVLQDV--FLFSGTIRENITLG---DPDATDEEI----IEAARLAGLHDFiealpmgYDTVVgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETE----AIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDG 691
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
40-231 |
6.43e-36 |
|
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: 127.21 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNFVFQNPDHQV 118
Cdd:COG4133 3 LEAENLSCRRGER-----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 --------VMP--TVEADVAFgLGKYHDMNQEEvkSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:COG4133 78 aylghadgLKPelTVRENLRF-WAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23296450 189 LDELTTFLDESDqmgvIKAVKDLINAKKGD-VTALWVTHRLEEL 231
Cdd:COG4133 155 LDEPFTALDAAG----VALLAELIAAHLARgGAVLLTTHQPLEL 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
60-249 |
2.11e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.21 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------KPKNF---------VFQNPDHQVVMPT 122
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkKNKKLkplrkkvgiVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGlgkyhDMN----QEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK13634 103 VEKDICFG-----PMNfgvsEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23296450 198 ESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13634 178 PKGRKEMMEMFYKL--HKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
60-194 |
4.39e-35 |
|
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: 123.14 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PKN--FVFQNPdhqVVMP--TVE 124
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslRKEigYVFQDP---QLFPrlTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 125 ADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQ----TLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:pfam00005 78 ENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
40-249 |
4.52e-35 |
|
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: 125.70 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLcfSVS-TRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkPKN---------- 108
Cdd:cd03257 2 LEVKNL--SVSfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-GKDllklsrrlrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -------FVFQNPDHQV--VMpTVEADVAFGL-GKYHDMNQEEVKSRVIKALEAVGM-RDYMQR-PIQtLSGGQKQRIAI 176
Cdd:cd03257 79 irrkeiqMVFQDPMSSLnpRM-TIGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRyPHE-LSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKL--QEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
40-250 |
8.02e-35 |
|
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: 125.14 E-value: 8.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgisvpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---- 108
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlPPEKrdis 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 FVFQNpdhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:cd03299 75 YVPQN---YALFPhmTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLInaKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIR--KEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
53-250 |
9.74e-35 |
|
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: 125.00 E-value: 9.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 53 QGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPD-----HQVVM------- 120
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarRRIGMifqhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ---PTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03258 94 lssRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 198 ESDQMGVIKAVKDlINAKKGdVTALWVTHRLEELK-YADGAVYMENGRVVRHGD 250
Cdd:cd03258 173 PETTQSILALLRD-INRELG-LTIVLITHEMEVVKrICDRVAVMEKGEVVEEGT 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
58-249 |
1.68e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 124.74 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KP----------KNFVFQnPDHQVVmP---TV 123
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPismlssrqlaRRLALL-PQHHLT-PegiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFG----LGKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK11231 94 RELVAYGrspwLSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23296450 200 DQMGVIKAVKDLINAKKGDVTALwvtHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK11231 173 HQVELMRLMRELNTQGKTVVTVL---HDLNQAsRYCDHLVVLANGHVMAQG 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
56-235 |
1.76e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.11 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQVVMP-TVEADVAFGL- 131
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggARVAYVPQRSEVPDSLPlTVRDLVAMGRw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 ---GKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESdqmgVIKAV 208
Cdd:NF040873 84 arrGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE----SRERI 158
|
170 180
....*....|....*....|....*...
gi 23296450 209 KDLINAKKGD-VTALWVTHRLEELKYAD 235
Cdd:NF040873 159 IALLAEEHARgATVVVVTHDLELVRRAD 186
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
40-244 |
2.56e-34 |
|
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: 121.72 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHQvv 119
Cdd:cd03228 1 IEFKNVSFSYPGR---PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-----------DGV-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 mptveaDVAfglgkyhDMNQEEVKSRVIkaleAVGmrdymQRPI---QT-----LSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:cd03228 65 ------DLR-------DLDLESLRKNIA----YVP-----QDPFlfsGTireniLSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 192 LTTFLD-ESDQmgvikAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGR 244
Cdd:cd03228 123 ATSALDpETEA-----LILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
60-249 |
3.85e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.57 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF--------------VFQNPDHQVVMPTVE 124
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgKPIDYsrkglmklresvgmVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFGLgkyhdMN----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsd 200
Cdd:PRK13636 102 QDVSFGA-----VNlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23296450 201 qMGVIKAVKDLINAKKG-DVTALWVTHRLEELK-YADGAVYMENGRVVRHG 249
Cdd:PRK13636 175 -MGVSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
49-256 |
5.67e-34 |
|
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: 123.06 E-value: 5.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---------FVFQ 112
Cdd:cd03256 6 LSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklKGKAlrqlrrqigMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 npDHQVVMP-TVEADVAFGLGKYH-------DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:cd03256 86 --QFNLIERlSVLENVLSGRLGRRstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 185 KVLLLDELTTFLDESDQMGVIKAVKDlINAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKR-INREEG-ITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
40-245 |
6.79e-34 |
|
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: 120.97 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpdhqvv 119
Cdd:cd03230 1 IEVRNLSKRYGKK-----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 mptveadvafgLGKYHDMNQEEVKSRVIKALEAVGMRDYMqRPIQTL--SGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03230 60 -----------LGKDIKKEPEEVKRRIGYLPEEPSLYENL-TVRENLklSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23296450 198 ESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRV 245
Cdd:cd03230 128 PESRREFWELLREL---KKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-249 |
1.40e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 123.28 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 37 NVAVECRNLCFSVSTRQGISVpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK--------- 107
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQ--LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 ----NFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK13642 80 rrkiGMVFQNPDNQFVGATVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 184 CKVLLLDELTTFLD---ESDQMGVIKAVKDlinakKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13642 159 PEIIILDESTSMLDptgRQEIMRVIHEIKE-----KYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-249 |
1.45e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.53 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNfvfQNPDHQV- 118
Cdd:COG4559 3 EAENLSVRLGGRT-----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgRPLA---AWSPWELa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 ----VMP---------TVEADVAFGLgkY-HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA--- 181
Cdd:COG4559 75 rrraVLPqhsslafpfTVEEVVALGR--ApHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 182 EAC----KVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLeEL--KYADGAVYMENGRVVRHG 249
Cdd:COG4559 153 EPVdggpRWLFLDEPTSALDLAHQHAVLRLARQL--ARRG-GGVVAVLHDL-NLaaQYADRILLLHQGRLVAQG 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
39-252 |
3.96e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 120.89 E-value: 3.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV--------FVEKPKN-- 108
Cdd:COG4161 2 SIQLKNINCFYGSHQ-----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdFSQKPSEka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---------FVFQN----PdHQVVMPT-VEADVafglgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRI 174
Cdd:COG4161 77 irllrqkvgMVFQQynlwP-HLTVMENlIEAPC-----KVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAA 252
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL--SQTG-ITQVIVTHEVEfARKVASQVVYMEKGRIIEQGDAS 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
53-254 |
5.43e-33 |
|
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: 120.57 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 53 QGISV-----PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSG---TVFVEKP---------KNFVFQNPD 115
Cdd:COG1119 7 RNVTVrrggkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGERRggedvwelrKRIGLVSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 HQVVMP---TVEaDV----AFG-LGKYHDMNQEEVKsRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:COG1119 87 LQLRFPrdeTVL-DVvlsgFFDsIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 188 LLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELkyADG---AVYMENGRVVRHGDAATI 254
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKL--AAEGAPTLVLVTHHVEEI--PPGithVLLLKDGRVVAAGPKEEV 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
38-246 |
1.50e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.88 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 38 VAVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNfvfQNPDH 116
Cdd:PRK13548 1 AMLEARNLSVRLGGRT-----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgRPLA---DWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 117 QV-----VMP---------TVEADVAFGLGKyHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA- 181
Cdd:PRK13548 73 ELarrraVLPqhsslsfpfTVEEVVAMGRAP-HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 182 -----EACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLeEL--KYADGAVYMENGRVV 246
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQL--AHERGLAVIVVLHDL-NLaaRYADRIVLLHQGRLV 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
58-245 |
2.68e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 121.98 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------KPKNFVFQN----PdHqvvMpT 122
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaenRHVNTVFQSyalfP-H---M-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES--D 200
Cdd:PRK09452 103 VFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKlrK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23296450 201 QMGV-IKAVKdlinaKKGDVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK09452 182 QMQNeLKALQ-----RKLGITFVFVTHDQEEaLTMSDRIVVMRDGRI 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
40-254 |
4.18e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.48 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLcfsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------KPKN 108
Cdd:PRK11607 20 LEIRNL-----TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvppyqRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 FVFQNpdhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK11607 95 MMFQS---YALFPhmTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 187 LLLDELTTFLDES--DQMGVikAVKDLInaKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11607 171 LLLDEPMGALDKKlrDRMQL--EVVDIL--ERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-244 |
1.04e-31 |
|
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: 116.03 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPdhqVV 119
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEP---WI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 MP-TVEADVAFGlgkyHDMNQEEVKsRVIKA------LEAVGMRDYM---QRPIqTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03250 78 QNgTIRENILFG----KPFDEERYE-KVIKAcalepdLEILPDGDLTeigEKGI-NLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 190 DElttfldesdqmgVIKAV---------KDLINAK-KGDVTALWVTHRLEELKYADGAVYMENGR 244
Cdd:cd03250 152 DD------------PLSAVdahvgrhifENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
58-235 |
2.31e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 115.97 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPD--HQVVMPTVEADVAFGLGKYH 135
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG-EDISTLKPEiyRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 DM-------NQEEVKSRVIKALEAVGMRDYM-QRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQmgviKA 207
Cdd:PRK10247 100 NLifpwqirNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK----HN 175
|
170 180 190
....*....|....*....|....*....|
gi 23296450 208 VKDLIN--AKKGDVTALWVTHRLEELKYAD 235
Cdd:PRK10247 176 VNEIIHryVREQNIAVLWVTHDKDEINHAD 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
56-249 |
2.40e-31 |
|
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: 115.43 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN----FVFQNpdhQVVMP--T 122
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlPPKDrdiaMVFQN---YALYPhmT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:cd03301 89 VYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLinAKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03301 168 QMRAELKRL--QQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
40-245 |
3.01e-31 |
|
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: 115.32 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN------ 108
Cdd:cd03262 1 IEIKNLHKSFGDFH-----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltDDKKninelr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ----FVFQNPD---HQvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:cd03262 76 qkvgMVFQQFNlfpHL----TVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 182 EACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRV 245
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDL--AEEG-MTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
64-256 |
3.96e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.24 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQnpDHQVVMP-TVEADVAFGL 131
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalppaERPVSMLFQ--ENNLFPHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKyhDMN-QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES--DQMgvIKAV 208
Cdd:COG3840 97 RP--GLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrQEM--LDLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23296450 209 KDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:COG3840 173 DEL--CRERGLTVLMVTHDPEDaARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
62-249 |
4.58e-31 |
|
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: 114.70 E-value: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 62 DCSFRIPsGQLWMILGPNGCGKSTLLKILAGVVNPSSG------TVFVEKPKN-----------FVFQNpdhQVVMP--T 122
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKinlppqqrkigLVFQQ---YALFPhlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYHDMnqeEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:cd03297 92 VRENLAFGLKRKRNR---EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:cd03297 169 QLLPELKQI--KKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-250 |
9.59e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.49 E-value: 9.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------- 104
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 ----------KPKNF---------VFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRD-YMQR 161
Cdd:PRK13631 97 helitnpyskKIKNFkelrrrvsmVFQFPEYQLFKDTIEKDIMFGpvaLG----VKKSEAKKLAKFYLNKMGLDDsYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 162 PIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD---ESDQMGVIKavkdliNAKKGDVTALWVTHRLEE-LKYADGA 237
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLIL------DAKANNKTVFVITHTMEHvLEVADEV 246
|
250
....*....|...
gi 23296450 238 VYMENGRVVRHGD 250
Cdd:PRK13631 247 IVMDKGKILKTGT 259
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
56-246 |
1.16e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.14 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPDHqvvmptveadvafglgkyh 135
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-KEVSFASPRD------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 dmnqeevksrvikALEA-VGMrdymqrpIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinA 214
Cdd:cd03216 72 -------------ARRAgIAM-------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL--R 129
|
170 180 190
....*....|....*....|....*....|...
gi 23296450 215 KKGdVTALWVTHRLEE-LKYADGAVYMENGRVV 246
Cdd:cd03216 130 AQG-VAVIFISHRLDEvFEIADRVTVLRDGRVV 161
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
56-249 |
1.62e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 113.14 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNFVFQN------------PDHQVVmpt 122
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgKPLDIAARNrigylpeerglyPKMKVI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 veaDVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQm 202
Cdd:cd03269 89 ---DQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23296450 203 gviKAVKDLINAKKGD-VTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:cd03269 165 ---ELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
58-254 |
2.48e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 114.33 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF--------------VFQNPDHQVVMPT 122
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgKPLDYskrgllalrqqvatVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:PRK13638 95 IDSDIAFSL-RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23296450 203 GVIKAVKDLINAKKGDVTAlwvTHRLEELKYADGAVY-MENGRVVRHGDAATI 254
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIIS---SHDIDLIYEISDAVYvLRQGQILTHGAPGEV 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
59-249 |
2.70e-30 |
|
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: 112.67 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGqLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKNFvfqnpdHQVV--MP--------- 121
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlKQPQKL------RRRIgyLPqefgvypnf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:cd03264 88 TVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23296450 202 MGVIKAVKDLinakKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:cd03264 167 IRFRNLLSEL----GEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
35-253 |
2.96e-30 |
|
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: 118.72 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSvstRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPK------ 107
Cdd:COG4987 329 PGGPSLELEDVSFR---YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLrdlded 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 ------NFVFQNPDhqVVMPTVEADVAFGLGkyhDMNQEEVksrvIKALEAVGMRDYMQRPIQ-----------TLSGGQ 170
Cdd:COG4987 406 dlrrriAVVPQRPH--LFDTTLRENLRLARP---DATDEEL----WAALERVGLGDWLAALPDgldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIkavKDLINAKKGDvTALWVTHRLEELKYADGAVYMENGRVVRHGD 250
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALL---ADLLEALAGR-TVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
...
gi 23296450 251 AAT 253
Cdd:COG4987 553 HEE 555
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
53-255 |
4.57e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 53 QGIS-----VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPknFVFQNP----DHQVVM-- 120
Cdd:COG1129 8 RGISksfggVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEP--VRFRSPrdaqAAGIAIih 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ------P--TVEADVAFG--LGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:COG1129 86 qelnlvPnlSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 191 ELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATIS 255
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRL---KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELT 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
40-250 |
5.30e-30 |
|
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: 112.63 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQGisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNF-------- 109
Cdd:cd03249 1 IEFKNVSFRYPSRPD--VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgVDIRDLnlrwlrsq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ---VFQNPdhqVVMP-TVEADVAFGLgkyHDMNQEEVKsRVIKALEA--------------VGmrdymQRPIQtLSGGQK 171
Cdd:cd03249 79 iglVSQEP---VLFDgTIAENIRYGK---PDATDEEVE-EAAKKANIhdfimslpdgydtlVG-----ERGSQ-LSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 172 QRIAIAGALAEACKVLLLDELTTFLD-ESDqmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGD 250
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDaESE-----KLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
59-251 |
9.96e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 112.03 E-value: 9.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV--------FVEKPK-----------NFVFQN----Pd 115
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPSdkairelrrnvGMVFQQynlwP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 HQVVMPT-VEADV-AFGLGKyhdmnqEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK11124 96 HLTVQQNlIEAPCrVLGLSK------DQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 193 TTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDA 251
Cdd:PRK11124 169 TAALDPEITAQIVSIIREL--AETG-ITQVIVTHEVEvARKTASRVVYMENGHIVEQGDA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
41-245 |
1.99e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 109.23 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVStrqGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHqvvm 120
Cdd:cd03246 2 EVENVSFRYP---GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-----------DG---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ptveADV-AFGLGKYHDMnqeevksrvikaleaVGmrdYMQRPIQ---------TLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:cd03246 64 ----ADIsQWDPNELGDH---------------VG---YLPQDDElfsgsiaenILSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 191 ELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL---KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
58-248 |
2.04e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 111.72 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-----VEKP---KNFVFQnpdHQVVMP--TVEADV 127
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpVEGPgaeRGVVFQ---NEGLLPwrNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 128 AFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE----LTTFLDESDQMG 203
Cdd:PRK11248 92 AFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEpfgaLDAFTREQMQTL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 204 VIKAVKDliNAKKgdvtALWVTHRLEElkyadgAVYMEN---------GRVVRH 248
Cdd:PRK11248 171 LLKLWQE--TGKQ----VLLITHDIEE------AVFMATelvllspgpGRVVER 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
39-249 |
3.98e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKN---- 108
Cdd:COG1132 339 EIEFENVSFSYPGDR----PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirDLTLEslrr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQnpDHQVVMPTVEADVAFGLGKYHDmnqEEVksrvIKALEAVGMRDYMQR-------PI----QTLSGGQKQRI 174
Cdd:COG1132 415 qigVVPQ--DTFLFSGTIRENIRYGRPDATD---EEV----EEAAKAAQAHEFIEAlpdgydtVVgergVNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 175 AIAGALAEACKVLLLDELTTFLD-ESDQMgVIKAVKDLInakkGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDtETEAL-IQEALERLM----KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
60-249 |
6.04e-29 |
|
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: 109.38 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKNFVFQN----PDHQVVMP--TVEADVA 128
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvKEPAEARRRlgfvSDSTGLYDrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 129 FgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:cd03266 101 Y-FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23296450 209 KDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:cd03266 180 RQLRALGK---CILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
40-249 |
6.15e-29 |
|
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: 109.63 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-------------- 105
Cdd:cd03253 1 IEFENVTFAYDPGR----PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 ----PKNFVFQNPdhqvvmpTVEADVAFGlgkYHDMNQEEVksrvIKALEA-----------------VGMRDYMqrpiq 164
Cdd:cd03253 77 igvvPQDTVLFND-------TIGYNIRYG---RPDATDEEV----IEAAKAaqihdkimrfpdgydtiVGERGLK----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 165 tLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGR 244
Cdd:cd03253 138 -LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR----TTIVIAHRLSTIVNADKIIVLKDGR 212
|
....*
gi 23296450 245 VVRHG 249
Cdd:cd03253 213 IVERG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
56-246 |
6.64e-29 |
|
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: 109.13 E-value: 6.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKNFVFQN----PDHQVVMP--TVE 124
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirTDRKAARQSlgycPQFDALFDelTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdqmgV 204
Cdd:cd03263 94 EHLRF-YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-----A 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23296450 205 IK-AVKDLINAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVV 246
Cdd:cd03263 168 SRrAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
60-249 |
8.60e-29 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 109.00 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKN------FVFQNPDHQVVMPTVEADV 127
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvREPREvrrrigIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 128 AFglGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKA 207
Cdd:cd03265 96 IH--ARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23296450 208 VKDLInaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:cd03265 174 IEKLK--EEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEG 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
58-252 |
1.75e-28 |
|
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: 109.51 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------VEKPKNFVFQNPdHQVVMP 121
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqldrkqrraFRRDVQLVFQDS-PSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 --TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDE 198
Cdd:TIGR02769 104 rmTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 199 SDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAA 252
Cdd:TIGR02769 184 VLQAVILELLRKL--QQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVA 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
40-250 |
2.67e-28 |
|
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: 108.09 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQ 117
Cdd:cd03251 1 VEFKNVTF---RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 V-VMP--------TVEADVAFGLgkyHDMNQEEVksrvIKALEAVGMRDY-MQRPIQ----------TLSGGQKQRIAIA 177
Cdd:cd03251 78 IgLVSqdvflfndTVAENIAYGR---PGATREEV----EEAARAANAHEFiMELPEGydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 178 GALAEACKVLLLDELTTFLD-ESDqmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGD 250
Cdd:cd03251 151 RALLKDPPILILDEATSALDtESE-----RLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
57-244 |
2.75e-28 |
|
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: 106.50 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------------EKPKNFVFQNPdhqVVMP 121
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpplRRRIGMVFQDF---ALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 --TVEADVAFGLgkyhdmnqeevksrvikaleavgmrdymqrpiqtlSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:cd03229 90 hlTVLENIALGL-----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23296450 200 DQMGVIKAVKDLiNAKKGdVTALWVTHRLEEL-KYADGAVYMENGR 244
Cdd:cd03229 135 TRREVRALLKSL-QAQLG-ITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
40-254 |
3.02e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNlcfsVSTRQGISVPIlRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNFVFQNPDHQ 117
Cdd:PRK11432 7 VVLKN----ITKRFGSNTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgEDVTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VV---------MPTVEaDVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:PRK11432 82 MVfqsyalfphMSLGE-NVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 189 LDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIREL--QQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
58-249 |
5.02e-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: 106.81 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFriPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPDhqvVMP--TVE 124
Cdd:cd03298 14 PMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaappaDRPVSMLFQENN---LFAhlTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFGLGKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:cd03298 89 QNVGLGLSPGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23296450 205 IKAVKDLINAKKgdVTALWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:cd03298 168 LDLVLDLHAETK--MTVLMVTHQPEDaKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
59-245 |
5.02e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.17 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPDHQVVMpTVEADV 127
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlharDRKVGFVFQHYALFRHM-TVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 128 AFGLG---KYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK10851 96 AFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRyPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23296450 204 VIKAVKDLINAKKgdVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK10851 175 LRRWLRQLHEELK--FTSVFVTHDQEEaMEVADRVVVMSQGNI 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
39-249 |
9.59e-28 |
|
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: 106.13 E-value: 9.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkpkNFVFQNPDHQV 118
Cdd:cd03245 2 RIEFRNVSFSYPNQE---IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD---GTDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMP--------------TVEADVAFGLGKYHDmnqeevkSRVIKALEAVGMRDYMQR-------PI----QTLSGGQKQR 173
Cdd:cd03245 76 LRRnigyvpqdvtlfygTLRDNITLGAPLADD-------ERILRAAELAGVTDFVNKhpngldlQIgergRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLInakkGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL----GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
60-254 |
1.15e-27 |
|
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: 106.37 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNFV-------FQNP---DHQVVMPT 122
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglPPHEIArlgigrtFQIPrlfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYHDM-----NQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL- 196
Cdd:cd03219 96 VMVAAQARTGSGLLLararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLn 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 197 -DESDQMG-VIKAVKDlinakkGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:cd03219 176 pEETEELAeLIRELRE------RGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
56-254 |
1.65e-27 |
|
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: 106.96 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------------KPKNFVFQnpdHQV 118
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamsrkelrelrrKKISMVFQ---SFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:cd03294 113 LLPhrTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 197 DEsdqmgVIKavKDL------INAKKGDvTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:cd03294 192 DP-----LIR--REMqdellrLQAELQK-TIVFITHDLDEaLRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
43-254 |
1.95e-27 |
|
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: 107.83 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQGIsVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---SSGTVFVE-------KPKNF--- 109
Cdd:COG0444 5 RNLKVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedllklSEKELrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -------VFQ------NPdhqvVMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGGQKQ 172
Cdd:COG0444 84 rgreiqmIFQdpmtslNP----VM-TVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldryPHE-LSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 173 RIAIAGALaeAC--KVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:COG0444 158 RVMIARAL--ALepKLLIADEPTTALDVTIQAQILNLLKDL--QRELGLAILFITHDLGVVAEiADRVAVMYAGRIVEEG 233
|
....*
gi 23296450 250 DAATI 254
Cdd:COG0444 234 PVEEL 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
58-262 |
4.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.98 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK------PKN-----------FVFQNPDHQVVM 120
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNkdikqirkkvgLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTVEADVAFGLGKYhDMNQEEVKSRVIKALEAVGMRD--YMQRPIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDE 198
Cdd:PRK13649 101 ETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISEslFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 199 SDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI---SDFIKAKQ 262
Cdd:PRK13649 179 KGRKELMTLFKKL---HQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIfqdVDFLEEKQ 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
64-255 |
4.48e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 109.55 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFVE-------------KPKNFVFQNPdhQVVMPTVEADVAfg 130
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgielreldpeswrKHLSWVGQNP--QLPHGTLRDNVL-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 131 LGKyHDMNQEEVKSrvikALEAVGMRDYMQR-------PIQ----TLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK11174 445 LGN-PDASDEQLQQ----ALENAWVSEFLPLlpqgldtPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 200 DQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHGDAATIS 255
Cdd:PRK11174 520 SEQLVMQALNAASRRQ----TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS 571
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
43-250 |
7.33e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 106.70 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN------- 108
Cdd:COG1135 5 ENLSKTFPTKGG-PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalSERElraarrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDhqvVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEA 183
Cdd:COG1135 84 igMIFQHFN---LLSsrTVAENVALPL-EIAGVPKAEIRKRVAELLELVGLSDKADAyPSQ-LSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 184 CKVLLLDELTTFLD-ESdqmgvIKAVKDL---INAKKGdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:COG1135 159 PKVLLCDEATSALDpET-----TRSILDLlkdINRELG-LTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
56-245 |
1.33e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.85 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNFVFQNPDHQVVMPTVEADVAFG--- 130
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAASRRVASVPQDTSLSFEfdv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 131 -----------LGKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK09536 95 rqvvemgrtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23296450 200 DQMGVIKAVKDLINAKKGDVTALwvtHRLE-ELKYADGAVYMENGRV 245
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAI---HDLDlAARYCDELVLLADGRV 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
35-252 |
2.10e-26 |
|
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: 102.90 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------EK 105
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAG-ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfaldED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PK--------NFVFQNpdHQ----------VVMPTVEADVAfglgkyhdmnqeEVKSRVIKALEAVGMRDYMQ-RPIQtL 166
Cdd:COG4181 83 ARarlrarhvGFVFQS--FQllptltalenVMLPLELAGRR------------DARARARALLERVGLGHRLDhYPAQ-L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdQMGviKAVKDLI---NAKKGdVTALWVTHRLEELKYADGAVYMENG 243
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDA--ATG--EQIIDLLfelNRERG-TTLVLVTHDPALAARCDRVLRLRAG 222
|
....*....
gi 23296450 244 RVVRHGDAA 252
Cdd:COG4181 223 RLVEDTAAT 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
57-256 |
2.21e-26 |
|
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: 102.51 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknfVFQN------PDHQVVmptvEADVAF- 129
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI--------RFDGrditglPPHERA----RAGIGYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 130 --GLGKYHDMNQEE---------VKSRVIKALEAV-GM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:cd03224 81 peGRRIFPELTVEEnlllgayarRRAKRKARLERVyELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 194 tfldesdqMG----VIKAVKDLINA-KKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:cd03224 161 --------EGlapkIVEEIFEAIRElRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
60-248 |
2.22e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------------EKPKNFVFQNPDHQVVMPT 122
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgnknlkklRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGlGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:PRK13641 103 VLKDVEFG-PKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 202 MGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRH 248
Cdd:PRK13641 182 KEMMQLFKDY---QKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKH 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
59-249 |
2.72e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.53 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNFVFQNPDHQV-------VMP---TVEAD 126
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgEHIQHYASKEVARRIgllaqnaTTPgdiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 127 VAFGLGKYHDMN---QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK10253 102 VARGRYPHQPLFtrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23296450 204 VIKAVKDLiNAKKGDVTALwVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:PRK10253 182 LLELLSEL-NREKGYTLAA-VLHDLNQaCRYASHLIALREGKIVAQG 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
60-243 |
2.84e-26 |
|
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: 102.54 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPDHQVV------MP--TVEADVAFGL 131
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGPDRMVVfqnyslLPwlTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKY-HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD----ESDQMGVIK 206
Cdd:TIGR01184 80 DRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaltrGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 23296450 207 AVKDlinakkGDVTALWVTHRLEE-LKYADGAVYMENG 243
Cdd:TIGR01184 160 IWEE------HRVTVLMVTHDVDEaLLLSDRVVMLTNG 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
58-246 |
3.02e-26 |
|
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: 101.91 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVeKPKNFVFQNPDHQVVMPTVEADVAFG------- 130
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-DGKSYQKNIEALRRIGALIEAPGFYPnltaren 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 131 ---LGKYHDMNqeevKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDqmgvIKA 207
Cdd:cd03268 93 lrlLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG----IKE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23296450 208 VKDLI-NAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVV 246
Cdd:cd03268 165 LRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLI 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
60-250 |
4.68e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV--------FVEKPKNF---------------------- 109
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEKekvleklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -------VFQNPDHQVVMPTVEADVAFGLGKYhDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:PRK13651 103 irrrvgvVFQFAEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 182 EACKVLLLDELTTFLDESdqmGVIKAVKDLINAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGD 250
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQ---GVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGD 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
56-254 |
5.78e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPknfvFQNPDHQVV--MP---------TV 123
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgEP----LDPEDRRRIgyLPeerglypkmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDeSDQMG 203
Cdd:COG4152 89 GEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 204 VIK-AVKDLinAKKGdVTALWVTHRL---EELkyADGAVYMENGRVVRHGDAATI 254
Cdd:COG4152 167 LLKdVIREL--AAKG-TTVIFSSHQMelvEEL--CDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
48-259 |
9.16e-26 |
|
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: 101.61 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 48 SVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN------------FVFQnp 114
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgEDIReqdpvelrrkigYVIQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 dhQV-VMP--TVEADVAFgLGKYHDMNQEEVKSRVIKALEAVGM--RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03295 83 --QIgLFPhmTVEENIAL-VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 190 DELTTFLD----ESDQMGVIKAVKDLinaKKgdvTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI-----SDFIK 259
Cdd:cd03295 160 DEPFGALDpitrDQLQEEFKRLQQEL---GK---TIVFVTHDIDEaFRLADRIAIMKNGEIVQVGTPDEIlrspaNDFVA 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
60-269 |
1.27e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------------EKPKNFVFQNPDHQVVMPT 122
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYhDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:PRK13643 102 VLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 202 MGVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI---SDFIKA------KQSSYIDQI 269
Cdd:PRK13643 181 IEMMQLFESIHQSGQ---TVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVfqeVDFLKAhelgvpKATHFADQL 255
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
47-254 |
1.37e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 103.34 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 47 FSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPD-----HQVVM- 120
Cdd:PRK11153 11 FPQGGRT---IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQIGMi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ---------PTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:PRK11153 88 fqhfnllssRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 191 ELTTFLDESDQMGVIKAVKDlINAKKGdVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11153 166 EATSALDPATTRSILELLKD-INRELG-LTIVLITHEMDVVKrICDRVAVIDAGRLVEQGTVSEV 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
57-254 |
2.21e-25 |
|
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: 100.88 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNFV-------FQNP-------- 114
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrditglPPHRIArlgiartFQNPrlfpeltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 -DH-----QVVMPTVEADVAFGLGKYHDmNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:COG0411 97 lENvlvaaHARLGRGLLAALLRLPRARR-EEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 189 LDE----LTTflDESDQM-GVIKAVKDlinakKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG0411 176 LDEpaagLNP--EETEELaELIRRLRD-----ERGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
57-249 |
3.09e-25 |
|
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: 99.53 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknfvfqnpdhQVVMP-----------TVEA 125
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----------RVSSLlglgggfnpelTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQmgvI 205
Cdd:cd03220 104 NIYL-NGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ---E 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23296450 206 KAVKDLINAKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHG 249
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
41-254 |
3.12e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.68 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQGI----SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKNF--- 109
Cdd:COG4167 6 EVRNLSKTFKYRTGLfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINghklEYGDYkyr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ------VFQNPD-----HQVVMPTVEADVAFGLgkyhDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIA 177
Cdd:COG4167 86 ckhirmIFQDPNtslnpRLNIGQILEEPLRLNT----DLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 178 GALAEACKVLLLDELTTFLDESdqmgvIKAvkDLIN------AKKGdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:COG4167 162 RALILQPKIIIADEALAALDMS-----VRS--QIINlmlelqEKLG-ISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGK 233
|
....
gi 23296450 251 AATI 254
Cdd:COG4167 234 TAEV 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
40-249 |
3.17e-25 |
|
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: 104.41 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQ 117
Cdd:TIGR02203 331 VEFRNVTF---RYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghDLADYTLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 V------VM---PTVEADVAFGLGKYHDMNQEEVKSRVIKALEAV-GMRDYMQRPI----QTLSGGQKQRIAIAGALAEA 183
Cdd:TIGR02203 408 ValvsqdVVlfnDTIANNIAYGRTEQADRAEIERALAAAYAQDFVdKLPLGLDTPIgengVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 184 CKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGR----TTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
59-246 |
3.21e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------EKPKNF------VFQ------NPDH 116
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgeplaklnrAQRKAFrrdiqmVFQdsisavNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 117 qvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRD-YMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK10419 107 -----TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23296450 196 LDESDQMGVIKAVKDLinAKKGDVTALWVTH--RLEElKYADGAVYMENGRVV 246
Cdd:PRK10419 182 LDLVLQAGVIRLLKKL--QQQFGTACLFITHdlRLVE-RFCQRVMVMDNGQIV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
40-254 |
4.54e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 103.61 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQGI------SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFVE-------KP 106
Cdd:COG4172 276 LEARDLKVWFPIKRGLfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDgqdldglSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 107 KNF---------VFQ------NPDHqvvmpTVEADVAFGLGKYH-DMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGG 169
Cdd:COG4172 355 RALrplrrrmqvVFQdpfgslSPRM-----TVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 170 QKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRH 248
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL--QREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQ 507
|
....*.
gi 23296450 249 GDAATI 254
Cdd:COG4172 508 GPTEQV 513
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
40-249 |
4.62e-25 |
|
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: 99.22 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRqgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKN----- 108
Cdd:cd03254 3 IEFENVNFSYDEK----KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidirDISRKslrsm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhqVVMP-TVEADVAFGlgkyHDMNQEEVksrVIKALEAVGMRDY-MQRPI----------QTLSGGQKQRI 174
Cdd:cd03254 79 igVVLQDT---FLFSgTIMENIRLG----RPNATDEE---VIEAAKEAGAHDFiMKLPNgydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR----TSIIIAHRLSTIKNADKILVLDDGKIIEEG 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-197 |
4.81e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 42 CRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekPKN----FVFQNP--- 114
Cdd:COG0488 1 LENLSKSFGGR-----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--PKGlrigYLPQEPpld 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 DHQVVMPTV-----------------EADVAFG----------LGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTL 166
Cdd:COG0488 74 DDLTVLDTVldgdaelraleaeleelEAKLAEPdedlerlaelQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSEL 153
|
170 180 190
....*....|....*....|....*....|.
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
35-254 |
4.87e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.11 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLK------------------------IL 90
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQ-----ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndlipgarvegeilldgedIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 91 AGVVNPSS-----GTVFvEKPKNF---VFQNpdhqvvmptveadVAFGLgKYHDM-NQEEVKSRVIKALEAVGM----RD 157
Cdd:COG1117 82 DPDVDVVElrrrvGMVF-QKPNPFpksIYDN-------------VAYGL-RLHGIkSKSELDEIVEESLRKAALwdevKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 158 YMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDesdqmgVI--KAVKDLINAKKGDVTALWVTH------RLe 229
Cdd:COG1117 147 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD------PIstAKIEELILELKKDYTIVIVTHnmqqaaRV- 219
|
250 260
....*....|....*....|....*
gi 23296450 230 elkyADGAVYMENGRVVRHGDAATI 254
Cdd:COG1117 220 ----SDYTAFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-249 |
5.39e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.47 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 34 FSDNVAVEcrNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------- 103
Cdd:PRK13645 3 FSKDIILD--NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 104 --------EKPKNFVFQNPDHQVVMPTVEADVAFG---LGKyhdmNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQK 171
Cdd:PRK13645 81 kikevkrlRKEIGLVFQFPEYQLFQETIEKDIAFGpvnLGE----NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 172 QRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVtaLWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRI--IMVTHNMDQvLRIADEVIVMHEGKVISIG 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
40-249 |
8.59e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.94 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQG----------------ISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV 103
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 104 ------EKPKNFVFQnpdHQVVM----------PTVEadvAFGLGKY-HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTL 166
Cdd:cd03267 81 aglvpwKRRKKFLRR---IGVVFgqktqlwwdlPVID---SFYLLAAiYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEEL-KYADGAVYMENGRV 245
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY-NRERG-TTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
....
gi 23296450 246 VRHG 249
Cdd:cd03267 233 LYDG 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
40-245 |
1.09e-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: 98.31 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKN---------- 108
Cdd:cd03248 12 VKFQNVTFAYPTRP--DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPISqyehkylhsk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhQVVMPTVEADVAFGLGkyhDMNQEEVKSRVIKAlEAVGMRDYMQRPIQT--------LSGGQKQRIAIAG 178
Cdd:cd03248 90 vsLVGQEP--VLFARSLQDNIAYGLQ---SCSFECVKEAAQKA-HAHSFISELASGYDTevgekgsqLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 179 ALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03248 164 ALIRNPQVLILDEATSALDaESEQQ-----VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
60-246 |
1.37e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE------KPKN-----------FVFQNPDHQVVMPT 122
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithKTKDkyirpvrkrigMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGlGKYHDMNQEEVKSRVIKALEAVGM-RDYM-QRPIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:PRK13646 103 VEREIIFG-PKNFKMNLDEVKNYAHRLLMDLGFsRDVMsQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23296450 201 QMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVV 246
Cdd:PRK13646 181 KRQVMRLLKSL--QTDENKTIILVSHDMNEVaRYADEVIVMKEGSIV 225
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
57-249 |
2.39e-24 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 101.70 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNF------VFQNPdhQVVMPTV 123
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDgvdlrqlDPAELrarmalVPQDP--VLFAASV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFGlgkYHDMNQEEVKSRVIKA-----LEAV--GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:TIGR02204 431 MENIRYG---RPDATDEEVEAAARAAhahefISALpeGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 197 D-ESDQMgVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR02204 508 DaESEQL-VQQALETLMKGR----TTLIIAHRLATVLKADRIVVMDQGRIVAQG 556
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
59-245 |
3.20e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.83 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF--------VEKPKNFVFQNPDhqvVMP--TVEADVA 128
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplaeAREDTRLMFQDAR---LLPwkKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 129 FGL-GKYHDmnqeevksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMgvikA 207
Cdd:PRK11247 104 LGLkGQWRD--------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI----E 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23296450 208 VKDLINA--KKGDVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK11247 172 MQDLIESlwQQHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
57-254 |
3.64e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.46 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQ-----NPDHqvvmpTVEADVAFGl 131
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLElgagfHPEL-----TGRENIYLN- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDL 211
Cdd:COG1134 113 GRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23296450 212 inaKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATI 254
Cdd:COG1134 193 ---RESGRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
49-240 |
4.18e-24 |
|
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: 100.82 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN------FVFQNPd 115
Cdd:TIGR02857 327 VSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvpladaDADSwrdqiaWVPQHP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 hQVVMPTVEADVAFGLGkyhDMNQEEVKsrviKALEAVGMRDYMQ-RP--IQT--------LSGGQKQRIAIAGALAEAC 184
Cdd:TIGR02857 406 -FLFAGTIAENIRLARP---DASDAEIR----EALERAGLDEFVAaLPqgLDTpigeggagLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 185 KVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYM 240
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGR----TVLLVTHRLALAALADRIVVL 529
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
62-254 |
5.73e-24 |
|
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: 99.02 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 62 DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--------EKPKN---------FVFQNP---DHQvvmp 121
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsARGIFlpphrrrigYVFQEArlfPHL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADVAFGlgkYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:COG4148 93 SVRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23296450 202 MGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG4148 170 AEILPYLERL--RDELDIPILYVSHSLDEvARLADHVVLLEQGRVVASGPLAEV 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
58-251 |
7.00e-24 |
|
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: 100.50 E-value: 7.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------EKPKNFVFQNP-DHQVVMPTVEAD 126
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdrETFGKHIGYLPqDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 127 VA-FGlgkyhdmnqEEVKSR-VIKALEAVGMRDYMQRPIQ-----------TLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:TIGR01842 412 IArFG---------ENADPEkIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 194 TFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDA 251
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL---KARGITVVVITHRPSLLGCVDKILVLQDGRIARFGER 537
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
40-256 |
8.87e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 96.32 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNlcfsVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLK-------------ILAG--VVNPSSGTVFVE 104
Cdd:PRK09493 2 IEFKN----VSKHFG-PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGlkVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 KPKNFVFQNPDhqvVMPTVEA--DVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:PRK09493 77 QEAGMVFQQFY---LFPHLTAleNVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDL--AEEG-MTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
57-256 |
2.96e-23 |
|
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: 94.66 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknfVFQN------PDHQVV------MP--- 121
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI--------RFDGeditglPPHRIArlgigyVPegr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 ------TVEADVAfgLGKYHDMNQEEVKSRvikaLEAVG-----MRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:COG0410 88 rifpslTVEENLL--LGAYARRDRAEVRAD----LERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 191 ELTtfldesdqMG----VIKAVKDLINA-KKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:COG0410 162 EPS--------LGlaplIVEEIFEIIRRlNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
54-252 |
3.82e-23 |
|
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: 98.28 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF---VEkpknfVFQ-NPDH--QVV--MP---- 121
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgAD-----LSQwDREElgRHIgyLPqdve 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 ----TVEADVA-FGlgkyhDMNQEEVksrvIKALEAVGMRDYMQR-------PI----QTLSGGQKQRIAIAGALAEACK 185
Cdd:COG4618 417 lfdgTIAENIArFG-----DADPEKV----VAAAKLAGVHEMILRlpdgydtRIgeggARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 186 VLLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAA 252
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRAL---KARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
48-253 |
7.23e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.56 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 48 SVSTRQGISVpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKP------KNFVFQNPDHQVV- 119
Cdd:PRK15056 13 TVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPtrqalqKNLVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 --MPTVEADVAFgLGKYHDMN-----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK15056 91 wsFPVLVEDVVM-MGRYGHMGwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 193 TTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVyMENGRVVRHGDAAT 253
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGK---TMLVSTHNLGSVtEFCDYTV-MVKGTVLASGPTET 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
58-249 |
1.11e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 91.61 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNFVFQNPDHQVVMptveadvafglgkyhd 136
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItLDGVPVSDLEKALSSLISV---------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 MNQEevksrviKALEAVGMRDYMQRPiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKk 216
Cdd:cd03247 80 LNQR-------PYLFDTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK- 148
|
170 180 190
....*....|....*....|....*....|...
gi 23296450 217 gdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03247 149 ---TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
40-254 |
1.22e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.80 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLC--FSVST----RQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------- 104
Cdd:COG4608 8 LEVRDLKkhFPVRGglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqditglsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 ---KPKN----FVFQNPdHQVVMP--TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQR-PIQtLSGGQKQR 173
Cdd:COG4608 88 relRPLRrrmqMVFQDP-YASLNPrmTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRyPHE-FSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAA 252
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL--QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRD 243
|
..
gi 23296450 253 TI 254
Cdd:COG4608 244 EL 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-254 |
2.23e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------------KPKNFVFQNPDHqvv 119
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgkdifqidaiklrKEVGMVFQQPNP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 MP--TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK14246 102 FPhlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 194 TFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK14246 182 SMIDIVNS----QAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
40-254 |
3.10e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQGI----SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF----- 109
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdHPLHFgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -------VFQNPD-----HQVVMPTVEadvaFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAI 176
Cdd:PRK15112 85 rsqrirmIFQDPStslnpRQRISQILD----FPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQG-ISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
49-228 |
6.19e-22 |
|
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: 94.73 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPDHQ 117
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdEVRRRVSVCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VVMPTVEADVAFGLGkyhDMNQEEvksrVIKALEAVGMRDYMQRPI-----------QTLSGGQKQRIAIAGALAEACKV 186
Cdd:TIGR02868 420 LFDTTVRENLRLARP---DATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23296450 187 LLLDELTTFLD--ESDQMgvikaVKDLINAKKGDVTaLWVTHRL 228
Cdd:TIGR02868 493 LLLDEPTEHLDaeTADEL-----LEDLLAALSGRTV-VLITHHL 530
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
58-254 |
6.74e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.30 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNfVFQNPD--------------HQVVMPTV 123
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG-LD-VATTPSrelakrlailrqenHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFGLGKYHD--MNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD--ES 199
Cdd:COG4604 93 RELVAFGRFPYSKgrLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkHS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 200 DQMgvIKAVKDLinAKKGDVTALWVTHrleEL----KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG4604 172 VQM--MKLLRRL--ADELGKTVVIVLH---DInfasCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
35-245 |
7.30e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQgISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKN----- 108
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGS-VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDViFNGQPMSklssa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -----------FVFQN----PD----HQVVMPTVeadvafgLGKyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGG 169
Cdd:PRK11629 80 akaelrnqklgFIYQFhhllPDftalENVAMPLL-------IGK---KKPAEINSRALEMLAAVGLEHRANHRPSELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 170 QKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdvTA-LWVTHRLEELKYADGAVYMENGRV 245
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL-NRLQG--TAfLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
59-256 |
8.52e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.66 E-value: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN-------FVfqnPDHQVVMP--T 122
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgeditklPPHEraragiaYV---PQGREIFPrlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYHDMNQEEVKSrvIKALEAVgMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTtfldESDQM 202
Cdd:TIGR03410 92 VEENLLTGLAALPRRSRKIPDE--IYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT----EGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 203 GVIK----AVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:TIGR03410 165 SIIKdigrVIRRL--RAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDE 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
57-245 |
9.04e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------EKPKN----FVFQN----PdHqvvMp 121
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvneLEPADrdiaMVFQNyalyP-H---M- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES-- 199
Cdd:PRK11650 92 SVRENMAYGL-KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlr 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 200 DQMGV-IKAVKDLINakkgdVTALWVTH-RLEELKYADGAVYMENGRV 245
Cdd:PRK11650 171 VQMRLeIQRLHRRLK-----TTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-249 |
9.37e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 9.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KP-KNF-------- 109
Cdd:TIGR00958 479 IEFQDVSFSYPNRP--DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgVPlVQYdhhylhrq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ---VFQNPdhqVVM-PTVEADVAFGLGKYHDmnqEEVKSrvikALEAVGMRDYMQRPIQT-----------LSGGQKQRI 174
Cdd:TIGR00958 557 valVGQEP---VLFsGSVRENIAYGLTDTPD---EEIMA----AAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 175 AIAGALAEACKVLLLDELTTFLD-ESDQmgvikAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDaECEQ-----LLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-269 |
1.43e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.98 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------V 103
Cdd:PRK11831 8 VDMRGVSFTRGNR-----CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipamsrsrlytV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 104 EKPKNFVFQNPDHQVVMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK11831 83 RKRMSMLFQSGALFTDM-NVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 184 CKVLLLDEltTFLDESD-QMGVIKAVKDLINAKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISDFIKAK 261
Cdd:PRK11831 162 PDLIMFDE--PFVGQDPiTMGVLVKLISELNSALG-VTCVVVSHDVPEvLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
....*...
gi 23296450 262 QSSYIDQI 269
Cdd:PRK11831 239 VRQFLDGI 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
54-251 |
1.66e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.44 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 54 GIS-----VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKNFvfqnpdhQVVMPTVEADV 127
Cdd:PRK11288 9 GIGktfpgVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRF-------ASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 128 A--------------------------FGLgkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:PRK11288 82 AiiyqelhlvpemtvaenlylgqlphkGGI-----VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 182 EACKVLLLDELTTFLD--ESDQ-MGVIKAVKDlinakKGDVTaLWVTHRLEELkYA--DGAVYMENGRVVRHGDA 251
Cdd:PRK11288 157 RNARVIAFDEPTSSLSarEIEQlFRVIRELRA-----EGRVI-LYVSHRMEEI-FAlcDAITVFKDGRYVATFDD 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-246 |
1.88e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 31 RIKFSD-----NVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvek 105
Cdd:COG0488 302 EIRFPPperlgKKVLELEGLSKSYGDK-----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 pknfvfqnpdhqvvmpTVEADVAFGlgkYHDMNQEEVKS--RVIKALEAVG-------MRDYMQR----------PIQTL 166
Cdd:COG0488 373 ----------------KLGETVKIG---YFDQHQEELDPdkTVLDELRDGApggteqeVRGYLGRflfsgddafkPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLD-ESdqmgvIKAVKDLINAKKGdvTALWVTH-R--LEELkyADGAVYMEN 242
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDiET-----LEALEEALDDFPG--TVLLVSHdRyfLDRV--ATRILEFED 504
|
....
gi 23296450 243 GRVV 246
Cdd:COG0488 505 GGVR 508
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
56-191 |
1.99e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.08 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---SSGTVF----------VEKPK-NFVFQNP---DHqv 118
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLlngrrltalpAEQRRiGILFQDDllfPH-- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 119 vMpTVEADVAFGLGkyHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:COG4136 91 -L-SVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
59-249 |
1.99e-21 |
|
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: 89.85 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPKNFVFQnpDHQVVMPTVEA 125
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlaladpawlrRQVGVVLQ--ENVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAFGlgkyhdmNQEEVKSRVIKALEAVGMRDY-MQRPI----------QTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:cd03252 95 NIALA-------DPGMSMERVIEAAKLAGAHDFiSELPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 195 FLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGR----TVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
75-226 |
2.03e-21 |
|
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: 93.31 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPknfvfqnpdhQVVMPTVEADVAFGLGKYH--DMNQEEVKSRVI 147
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisyKP----------QYISPDYDGTVEEFLRSANtdDFGSSYYKTEII 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 148 KALeavGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTH 226
Cdd:COG1245 441 KPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF--AENRGKTAMVVDH 514
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
60-255 |
2.39e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF-------------VFQnpdHQVVMP--TV 123
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPVRIrsprdaialgigmVHQ---HFMLVPnlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFGL--GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL--DES 199
Cdd:COG3845 98 AENIVLGLepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpQEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 200 DQmgVIKAVKDLinAKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATIS 255
Cdd:COG3845 178 DE--LFEILRRL--AAEG-KSIIFITHKLREvMAIADRVTVLRRGKVVGTVDTAETS 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
58-197 |
3.99e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 88.18 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNFVFQNPDHQVV----MPTVEAD--VAFG 130
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAEQRDEPHENILylghLPGLKPElsALEN 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 131 LGKYHDMNQEEVKSrVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:TIGR01189 94 LHFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
75-226 |
4.51e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.18 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPknfvfqnpdhQVVMPTVEADVAFGLGKYHDM-NQEEVKSRVIK 148
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisyKP----------QYIKPDYDGTVEDLLRSITDDlGSSYYKSEIIK 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 149 ALeavGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgDVTALWVTH 226
Cdd:PRK13409 440 PL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER--EATALVVDH 512
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
57-246 |
6.09e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----------KPKNF---VFQNPdhqvVM--- 120
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklpeyKRAKYigrVFQDP----MMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 P--TVEADVA--------FGLGKYHDMNQ-EEVKSRvIKALEaVGMRDYMQRPIQTLSGGQKQriaiAGALAEAC----K 185
Cdd:COG1101 95 PsmTIEENLAlayrrgkrRGLRRGLTKKRrELFREL-LATLG-LGLENRLDTKVGLLSGGQRQ----ALSLLMATltkpK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 186 VLLLDELTTFLDESDQMGVIKAVKDLINAKKgdVTALWVTHRLEE-LKYADGAVYMENGRVV 246
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENN--LTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
62-226 |
1.04e-20 |
|
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: 88.23 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 62 DCSFR-------IPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKnfVFQNPdhQVVMPTVEADV-AFGLGK 133
Cdd:cd03237 10 LGEFTleveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--VSYKP--QYIKADYEGTVrDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 134 YHDM-NQEEVKSRVIKALeavGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLI 212
Cdd:cd03237 86 TKDFyTHPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170
....*....|....*
gi 23296450 213 -NAKKgdvTALWVTH 226
Cdd:cd03237 163 eNNEK---TAFVVEH 174
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-254 |
1.07e-20 |
|
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: 89.79 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 45 LCFSVSTRQGisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------------EKPK- 107
Cdd:TIGR02142 1 LSARFSKRLG---DFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrkgiflppEKRRi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPD---HQVVMPTVEADVAFGLGKYHDMNQEEVksrvikaLEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:TIGR02142 78 GYVFQEARlfpHLSVRGNLRYGMKRARPSERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 185 KVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERL--HAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
43-254 |
1.24e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.31 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKP------KNFVFQNPD 115
Cdd:PRK10575 15 RNVSFRVPGRT-----LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdAQPleswssKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 HQVVMP-----TVEADVAFG-------LGKYHDMNQEevksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK10575 90 LPQQLPaaegmTVRELVAIGrypwhgaLGRFGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 184 CKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRL--SQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
49-249 |
1.39e-20 |
|
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: 90.95 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------------EKPKNFVFQNPd 115
Cdd:TIGR01193 479 VSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdidrhtlRQFINYLPQEP- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 hqvVMPTVEADVAFGLGKYHDMNQEEVKsrviKALEAVGMRD---YMQRPIQT--------LSGGQKQRIAIAGALAEAC 184
Cdd:TIGR01193 558 ---YIFSGSILENLLLGAKENVSQDEIW----AACEIAEIKDdieNMPLGYQTelseegssISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 185 KVLLLDELTTFLDESDQMgviKAVKDLINAKkgDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR01193 631 KVLILDESTSNLDTITEK---KIVNNLLNLQ--DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
49-226 |
1.61e-20 |
|
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: 87.08 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PK-----NFVFQ 112
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraiPYlrrkiGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 N----PDHqvvmpTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:cd03292 86 DfrllPDR-----NVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 23296450 189 LDELTTFLDESDQMGVIKAVKDlINakKGDVTALWVTH 226
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKK-IN--KAGTTVVVATH 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
40-249 |
1.97e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.32 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTrqgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKN---------- 108
Cdd:PRK11000 4 VTLRNVTKAYGD-----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgEKRMNdvppaergvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 FVFQNpdhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK11000 79 MVFQS---YALYPhlSVAENMSFGL-KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 187 LLLDELTTFLDES--DQMGV-IKAVKdlinaKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK11000 155 FLLDEPLSNLDAAlrVQMRIeISRLH-----KRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
64-254 |
2.11e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------KPKNFVFQNPD---HQvvmpTVEADVAF 129
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttppsrRPVSMLFQENNlfsHL----TVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 130 GLGKYHDMNQEEvKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:PRK10771 95 GLNPGLKLNAAQ-REKLHAIARQMGIEDLLARlPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23296450 209 KDLINAKkgDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK10771 173 SQVCQER--QLTLLMVSHSLEDaARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
40-249 |
2.23e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.08 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQ 117
Cdd:PRK11176 342 IEFRNVTF---TYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VVM---------PTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVgmrDYMQRPIQT--------LSGGQKQRIAIAGAL 180
Cdd:PRK11176 419 VALvsqnvhlfnDTIANNIAYARTEQYSREQIEEAARMAYAMDFI---NKMDNGLDTvigengvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 181 AEACKVLLLDELTTFLD-ESDqmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK11176 496 LRDSPILILDEATSALDtESE-----RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
31-235 |
3.17e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 31 RIKFSDNVAVECRNLcfSVSTRQGisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFV 110
Cdd:COG4178 354 RIETSEDGALALEDL--TLRTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 F--QNP-------DHQVVMPTVEadvafglgkyHDMNQEEVKsrviKALEAVGMRDYMQRP------IQTLSGGQKQRIA 175
Cdd:COG4178 430 FlpQRPylplgtlREALLYPATA----------EAFSDAELR----EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 176 IAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYAD 235
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENE----AALYQLLREELPGTTVISVGHRSTLAAFHD 551
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
43-254 |
3.68e-20 |
|
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: 89.36 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLcfSVSTRQG-ISVPILRDCSFRIPSGQLWMILGPNGCGKS----TLLKILAGVVNPSSGTVFVE------KPKN--- 108
Cdd:COG4172 10 EDL--SVAFGQGgGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgqdllgLSERelr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --------FVFQ------NPDHqvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGGQ 170
Cdd:COG4172 88 rirgnriaMIFQepmtslNPLH-----TIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldayPHQ-LSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdvTALW-VTH-----RleelKYADGAVYMENGR 244
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL-QRELG--MALLlITHdlgvvR----RFADRVAVMRQGE 234
|
250
....*....|
gi 23296450 245 VVRHGDAATI 254
Cdd:COG4172 235 IVEQGPTAEL 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
40-226 |
3.79e-20 |
|
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: 84.04 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTvfVEKPKNFVFQnpdhqvv 119
Cdd:cd03221 1 IELENLSKTYGGK-----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVKIG------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 mptveadvafglgkyhdmnqeevksrvikaleavgmrdYMQRpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLD-E 198
Cdd:cd03221 67 --------------------------------------YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDlE 104
|
170 180
....*....|....*....|....*...
gi 23296450 199 SdqmgvIKAVKDLINAKKGDVtaLWVTH 226
Cdd:cd03221 105 S-----IEALEEALKEYPGTV--ILVSH 125
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
47-254 |
4.97e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 47 FSVSTRQGisvPIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFV-EKP------------KNFVFQN 113
Cdd:COG4138 6 VAVAGRLG---PI----SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLnGRPlsdwsaaelarhRAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 114 PDHQVVMPtveadvAF---GLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGAL--------AE 182
Cdd:COG4138 78 QSPPFAMP------VFqylALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 183 AcKVLLLDELTTFLDESDQmgviKAVKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG4138 152 G-QLLLLDEPMNSLDVAQQ----AALDRLLRelCQQG-ITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAEV 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-229 |
1.68e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 33 KFSDNVAVECRNLC--FSVSTRQgISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFV 110
Cdd:COG2401 18 SSVLDLSERVAIVLeaFGVELRV-VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 FQNpdhqvvMPTVEAdvafgLGKYHDMNQeevksrVIKALEAVGMRD--YMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:COG2401 97 GRE------ASLIDA-----IGRKGDFKD------AVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23296450 189 LDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLE 229
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKL--ARRAGITLVVATHHYD 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
40-254 |
1.78e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQGI-----SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF------VEKPK- 107
Cdd:PRK11308 6 LQAIDLKKHYPVKRGLfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdlLKADPe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 ---------NFVFQNPdHQVVMP--TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIA 175
Cdd:PRK11308 86 aqkllrqkiQIVFQNP-YGSLNPrkKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 176 IAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL--QQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
60-226 |
2.56e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.52 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKNFVfqnpdHQ--VVM----------P 121
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyvpfKRRKEFA-----RRigVVFgqrsqlwwdlP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEadvAFGL-GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:COG4586 113 AID---SFRLlKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180
....*....|....*....|....*.
gi 23296450 201 QMGVIKAVKDlINAKKGdVTALWVTH 226
Cdd:COG4586 190 KEAIREFLKE-YNRERG-TTILLTSH 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
39-254 |
2.97e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLcfsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------EKPKN--- 108
Cdd:PRK11264 3 AIEVKNL-----VKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtARSLSqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -----------FVFQN----PDHQVVMPTVEADVAFglgkyHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQR 173
Cdd:PRK11264 78 glirqlrqhvgFVFQNfnlfPHRTVLENIIEGPVIV-----KGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEELK-YADGAVYMENGRVVRHGDAA 252
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR---TMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAK 229
|
..
gi 23296450 253 TI 254
Cdd:PRK11264 230 AL 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
43-251 |
3.04e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG--VVNPSSGTVFVEKpKN------------ 108
Cdd:COG0396 4 KNLHVSVEGK-----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDG-EDilelspderara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FV-FQNPdhqVVMPTV-------EADVAFGLGKyhdMNQEEVKSRVIKALEAVGM-RDYMQRPI-QTLSGGQKQRIAI 176
Cdd:COG0396 78 giFLaFQYP---VEIPGVsvsnflrTALNARRGEE---LSAREFLKLLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 177 AGALAEACKVLLLDELTTFLDeSDqmgVIKAVKDLINA-KKGDVTALWVTH--RLeeLKY--ADGAVYMENGRVVRHGDA 251
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLD-ID---ALRIVAEGVNKlRSPDRGILIITHyqRI--LDYikPDFVHVLVDGRIVKSGGK 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
64-197 |
3.07e-19 |
|
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: 83.31 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkPKNFVFQNPD---------HQVVMPT---VEADVAFgl 131
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN-GGPLDFQRDSiargllylgHAPGIKTtlsVLENLRF-- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 132 gkYHDMNQEEvksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03231 97 --WHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
54-243 |
4.59e-19 |
|
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: 83.15 E-value: 4.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF--VEKPKNFVFQNPDHQ-------------V 118
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsNKNESEPSFEATRSRnrysvayaaqkpwL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMPTVEADVAFGlgkyHDMNQEEVKSrVIKALEAVGMRDYMQRPIQT--------LSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:cd03290 91 LNATVEENITFG----SPFNKQRYKA-VTDACSLQPDIDLLPFGDQTeigerginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 191 ELTTFLD--ESD---QMGVIKAVKDlinAKKgdvTALWVTHRLEELKYADGAVYMENG 243
Cdd:cd03290 166 DPFSALDihLSDhlmQEGILKFLQD---DKR---TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
60-226 |
5.38e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-----VEKPKN-----------FVFQnpDHQVVMP-T 122
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghdITRLKNrevpflrrqigMIFQ--DHHLLMDrT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:PRK10908 96 VYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLDKAKNfPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|....*
gi 23296450 202 MGVIKAVKDLinaKKGDVTALWVTH 226
Cdd:PRK10908 174 EGILRLFEEF---NRVGVTVLMATH 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-250 |
2.02e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.49 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKN----- 108
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQP---QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIAdysea 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -------FVFQNPDhqVVMPTVEADVAFGLGKYHDmnqeevkSRVIKALEAVGMRDYMQ-------------RPiqtLSG 168
Cdd:PRK11160 411 alrqaisVVSQRVH--LFSATLRDNLLLAAPNASD-------EALIEVLQQVGLEKLLEddkglnawlgeggRQ---LSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 169 GQKQRIAIAGALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVR 247
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDaETERQ-----ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
...
gi 23296450 248 HGD 250
Cdd:PRK11160 554 QGT 556
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
51-246 |
5.82e-18 |
|
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: 80.39 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 51 TRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTVFV--EKPKNFVFQN-----PDHQVVM 120
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFngQPRKPDQFQKcvayvRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 P--TVEADVAFGLgkyHDMNQEEVKSRVIKALEA-VGMRDYMQRPI-----QTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:cd03234 94 PglTVRETLTYTA---ILRLPRKSSDAIRKKRVEdVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 193 TTFLDESDQMGVIKAVKDLinAKKGDvTALWVTH--RLEELKYADGAVYMENGRVV 246
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQL--ARRNR-IVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-249 |
6.78e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.09 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSV-STRQGISvpilrDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE------------- 104
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVE-----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtvtraslr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 KPKNFVFQNPdhQVVMPTVEADVAfgLGKyHDMNQEEVKsrviKALEAVGMRDYMQRPIQ-----------TLSGGQKQR 173
Cdd:PRK13657 409 RNIAVVFQDA--GLFNRSIEDNIR--VGR-PDATDEEMR----AAAERAQAHDFIERKPDgydtvvgergrQLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETE----AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
38-249 |
8.13e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 38 VAVECRNLCFSVSTRQGISV-PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS--SGTVFV----EKPKN-- 108
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLIngrpLDKRSfr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ----FVFQnpdHQVVMP--TVEadvafglgkyhdmnqeevksrvikalEAVgmrdYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:cd03213 82 kiigYVPQ---DDILHPtlTVR--------------------------ETL----MFAAKLRGLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRL--EELKYADGAVYMENGRVVRHG 249
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRL--ADTG-RTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
58-249 |
1.13e-17 |
|
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: 82.18 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHQ---------------VVmP- 121
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-----------DGQdirdvtqaslraaigIV-Pq 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 -------TVEADVAFGLgkyHDMNQEEVksrvIKALEAVGMRDYMQR-P--IQT--------LSGGQKQRIAIAGALAEA 183
Cdd:COG5265 440 dtvlfndTIAYNIAYGR---PDASEEEV----EAAARAAQIHDFIESlPdgYDTrvgerglkLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 184 CKVLLLDELTTFLD---ESDQMGVIKAVkdlinAKkgDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG5265 513 PPILIFDEATSALDsrtERAIQAALREV-----AR--GRTTLVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
41-197 |
1.54e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCfsvSTRQGisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfVEKPKNFVFQNPD----- 115
Cdd:PRK13539 4 EGEDLA---CVRGG--RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-KLDGGDIDDPDVAeachy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 --HQVVMP---TVEADVAFGLGKYhdmNQEEvkSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:PRK13539 78 lgHRNAMKpalTVAENLEFWAAFL---GGEE--LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
....*..
gi 23296450 191 ELTTFLD 197
Cdd:PRK13539 153 EPTAALD 159
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-249 |
2.06e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKP---------------KNFVFQNPDHQVVmpt 122
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPvpsrarharqrvgvvPQFDNLDPDFTVR--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 vEADVAFGlgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:PRK13537 99 -ENLLVFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13537 176 LMWERLRSLLARGK---TILLTTHFMEEAeRLCDRLCVIEEGRKIAEG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
56-249 |
2.57e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVN--PS---SGTVFVEKPKNF-------------VFQNPDHq 117
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFkmdvielrrrvqmVFQIPNP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 vvMPTVE--ADVAFGLgKYHDM--NQEEVKSRVIKALEAVGM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:PRK14247 94 --IPNLSifENVALGL-KLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 190 DELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK14247 171 DEPTANLDPENT----AKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
61-211 |
2.90e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 61 RDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-----VEKpknfvfQNPD---------HQV-VMP--TV 123
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepIRR------QRDEyhqdllylgHQPgIKTelTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFglgkYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdqmg 203
Cdd:PRK13538 92 LENLRF----YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK----- 162
|
....*...
gi 23296450 204 viKAVKDL 211
Cdd:PRK13538 163 --QGVARL 168
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
65-233 |
3.73e-17 |
|
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: 78.56 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 65 FRIP---SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTvFVEKP------KNF---VFQNPDHQVVMPTVEADVAfglG 132
Cdd:cd03236 18 HRLPvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPdwdeilDEFrgsELQNYFTKLLEGDVKVIVK---P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 133 KYHDMNQEEVKSRVIKALEAV---GMRDY----------MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:cd03236 94 QYVDLIPKAVKGKVGELLKKKderGKLDElvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190
....*....|....*....|....*....|....
gi 23296450 200 DQMGVIKAVKDLINAKKgdvTALWVTHRLEELKY 233
Cdd:cd03236 174 QRLNAARLIRELAEDDN---YVLVVEHDLAVLDY 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
52-249 |
3.89e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 52 RQGISVPIlRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------------KPKNFVFQNp 114
Cdd:PRK10070 37 KTGLSLGV-KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevrrKKIAMVFQS- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 dhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK10070 115 --FALMPhmTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 193 TTFLDE------SDQMGVIKAvkdlinakKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:PRK10070 192 FSALDPlirtemQDELVKLQA--------KHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-226 |
3.98e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 37 NVAVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKIL--------------------AGVVNP 96
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH-----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrllelneearvegevrlfgRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 97 SSGTVFVEKPKNFVFQNPDHQVVMpTVEADVAFGLgKYHDM--NQEEVKSRVIKALEAVGMRDYMQRPIQ----TLSGGQ 170
Cdd:PRK14267 77 DVDPIEVRREVGMVFQYPNPFPHL-TIYDNVAIGV-KLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDEsdqMGVIKaVKDLINAKKGDVTALWVTH 226
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDP---VGTAK-IEELLFELKKEYTIVLVTH 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
58-249 |
4.13e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---EKPKNFVFQNPDHQVVMPTVEADVAFGL--- 131
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvPVPARARLARARIGVVPQFDNLDLEFTVren 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 ----GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKA 207
Cdd:PRK13536 135 llvfGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23296450 208 VKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13536 215 LRSLLARGK---TILLTTHFMEEAeRLCDRLCVLEAGRKIAEG 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-269 |
6.35e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLcfSVSTRQGISV-PILRDCSFRIPSGQLWMILGPNGCGKS-TLLKIL-----AGVVNPSSGTVF-------VEKPK- 107
Cdd:PRK15134 9 ENL--SVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsPPVVYPSGDIRFhgesllhASEQTl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 --------NFVFQ------NPDHqvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGG 169
Cdd:PRK15134 87 rgvrgnkiAMIFQepmvslNPLH-----TLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdyPHQ-LSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 170 QKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRH 248
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL--QQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQ 238
|
250 260
....*....|....*....|.
gi 23296450 249 GDAATIsdfIKAKQSSYIDQI 269
Cdd:PRK15134 239 NRAATL---FSAPTHPYTQKL 256
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
56-249 |
7.04e-17 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 80.17 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPKNFVFQnpDHQVVMPT 122
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDgvdlaiadpawlrRQMGVVLQ--ENVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGlgkyhdmNQEEVKSRVIKALEAVGMRDYMQRPIQ-----------TLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:TIGR01846 547 IRDNIALC-------NPGAPFEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDE 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 192 LTTFLD-ESDQmgVIKAVKDLINAKKgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR01846 620 ATSALDyESEA--LIMRNMREICRGR---TVIIIAHRLSTVRACDRIIVLEKGQIAESG 673
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
37-222 |
7.92e-17 |
|
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: 77.09 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 37 NVAVECRNLC--FSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFV--FQ 112
Cdd:COG4778 2 TTLLEVENLSktFTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdlAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 NPDHQV----------------VMPTVEA-DVafglgkyhdmnqeevksrVIKALEAVGM---------RDYMQR----- 161
Cdd:COG4778 82 ASPREIlalrrrtigyvsqflrVIPRVSAlDV------------------VAEPLLERGVdreeararaRELLARlnlpe 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 162 -----PIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMgvikAVKDLINAKKGDVTAL 222
Cdd:COG4778 144 rlwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEAKARGTAI 205
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-231 |
8.89e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.77 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILaGVVNPSSGTVFVEKPKNFVFQN----- 113
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNiyerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 114 --------------PDHQVVMPTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQT----LSGGQKQRIA 175
Cdd:PRK14258 81 vnlnrlrrqvsmvhPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 176 IAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL 231
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSL--RLRSELTMVIVSHNLHQV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-261 |
9.87e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.41 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGvvnpssgtvfvekpknfvfqNPDHQVvm 120
Cdd:cd03217 2 EIKDLHVSVGGKE-----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--------------------HPKYEV-- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ptVEADVAFglgKYHDMNQEEVKSRvikALEAVGMRdyMQRPIQ---------------TLSGGQKQRIAIAGALAEACK 185
Cdd:cd03217 55 --TEGEILF---KGEDITDLPPEER---ARLGIFLA--FQYPPEipgvknadflryvneGFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 186 VLLLDELTTFLDesdqMGVIKAVKDLINA-KKGDVTALWVTHRLEELKY--ADGAVYMENGRVVRHGDaATISDFIKAK 261
Cdd:cd03217 125 LAILDEPDSGLD----IDALRLVAEVINKlREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSGD-KELALEIEKK 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
59-228 |
1.77e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfVEKPKNFVFQNPDHQVVMPTVEADVafglGKYHDMN 138
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLRIGYVPQKLYLDTTLPLTV----NRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 139 QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMgvikAVKDLINA--KK 216
Cdd:PRK09544 94 PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV----ALYDLIDQlrRE 169
|
170
....*....|..
gi 23296450 217 GDVTALWVTHRL 228
Cdd:PRK09544 170 LDCAVLMVSHDL 181
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
67-249 |
3.16e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 67 IPSGQLWMILGPNGCGKSTLLKILAGVVN----PSSGTVF--------------VEKPK---NFVFQNPDhQVVMPTVEA 125
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELlgrtvqregrlardIRKSRantGYIFQQFN-LVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAFG-LG---------KYHDMNQeevKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK09984 106 NVLIGaLGstpfwrtcfSWFTREQ---KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 196 LDESDQMGVIKAVKDlINAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHG 249
Cdd:PRK09984 183 LDPESARIVMDTLRD-INQNDG-ITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
58-243 |
5.64e-16 |
|
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: 75.66 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfveKPKNFVFQNPDHQVVMP-TVEADVAFGLgkyhD 136
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWIMPgTIKENIIFGV----S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 MNQEEVKSrVIKA------LEAVGMRDY--MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:cd03291 124 YDEYRYKS-VVKAcqleedITKFPEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
170 180 190
....*....|....*....|....*....|....*
gi 23296450 209 KDLINAKKgdvTALWVTHRLEELKYADGAVYMENG 243
Cdd:cd03291 203 VCKLMANK---TRILVTSKMEHLKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
59-259 |
1.33e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.36 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPdhQVVMPTVEADVAFglgkyhdmN 138
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQA--WIMNATVRGNILF--------F 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 139 QEEVKSRVIKA-----LEAvgmrDYMQRP--IQT--------LSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdQMG 203
Cdd:PTZ00243 745 DEEDAARLADAvrvsqLEA----DLAQLGggLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA--HVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 204 ViKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAAtisDFIK 259
Cdd:PTZ00243 819 E-RVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA---DFMR 870
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
39-249 |
2.42e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPknfvFQNPDHQ 117
Cdd:PRK10790 340 RIDIDNVSFAYRDDN----LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgRP----LSSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VV-----M----PTVEADVAFG---LGKyhDMNQEevksRVIKALEAV-------GMRDYMQRPI----QTLSGGQKQRI 174
Cdd:PRK10790 412 VLrqgvaMvqqdPVVLADTFLAnvtLGR--DISEE----QVWQALETVqlaelarSLPDGLYTPLgeqgNNLSVGQKQLL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDEsdqmGVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDS----GTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
57-255 |
2.44e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPS---SGTVFVE-KPKnfVFQN-PD---------HQVVMPT 122
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEgEEL--QASNiRDteragiaiiHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVA---FgLG----KYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK13549 95 KELSVLeniF-LGneitPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 196 LDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATIS 255
Cdd:PRK13549 174 LTESETAVLLDIIRDL---KAHGIACIYISHKLNEVKaISDTICVIRDGRHIGTRPAAGMT 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
56-247 |
2.46e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK-----------------NFVFQ------ 112
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadalaqlrrehfGFIFQryhlls 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 --NPDHQVVMPTVEAdvafGLGKyhdmnqEEVKSRVIKALEAVGMRDYMQ-RPIQtLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:PRK10535 100 hlTAAQNVEVPAVYA----GLER------KQRLLRAQELLQRLGLEDRVEyQPSQ-LSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 190 DELTTFLDESDQMGVIKAVKDLinAKKGDvTALWVTHRLEELKYADGAVYMENGRVVR 247
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQL--RDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
40-235 |
3.01e-15 |
|
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: 71.42 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLcfSVSTRQGIsvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTvfVEKPKN----FVFQNPd 115
Cdd:cd03223 1 IELENL--SLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR--IGMPEGedllFLPQRP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 hqvvmptveadvafglgkYhdMNQEEVKSRVIKALEavgmrdymqrpiQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:cd03223 74 ------------------Y--LPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23296450 196 LDESDQMGVIKAVKDLInakkgdVTALWVTHRLEELKYAD 235
Cdd:cd03223 122 LDEESEDRLYQLLKELG------ITVISVGHRPSLWKFHD 155
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
40-246 |
3.85e-15 |
|
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: 72.53 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLcfSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK------PKN----- 108
Cdd:cd03244 3 IEFKNV--SLRYRPN-LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiGLHdlrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhqVVMP-TVEADVAFgLGKYHDmnqeevkSRVIKALEAVGMRDY-MQRPIQ----------TLSGGQKQRI 174
Cdd:cd03244 80 isIIPQDP---VLFSgTIRSNLDP-FGEYSD-------EELWQALERVGLKEFvESLPGGldtvveeggeNLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 175 AIAGALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVV 246
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDpETDAL-----IQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-242 |
3.91e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 33 KFSDNVAVECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNF--- 109
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYDTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLkdi 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -----------VFQNP---------------------------------DHQVVMPTVEADVAFGLGKYHDMNQE----- 140
Cdd:PTZ00265 454 nlkwwrskigvVSQDPllfsnsiknnikyslyslkdlealsnyynedgnDSQENKNKRNSCRAKCAGDLNDMSNTtdsne 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 141 --EVK--------SRVIKALEAVGMRDYMQ-----------RPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PTZ00265 534 liEMRknyqtikdSEVVDVSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 23296450 200 DQMGVIKAVKDLiNAKKGDVTALwVTHRLEELKYADGAVYMEN 242
Cdd:PTZ00265 614 SEYLVQKTINNL-KGNENRITII-IAHRLSTIRYANTIFVLSN 654
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
59-254 |
4.23e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG----VVNPSSGTVFVEKPKNfvfQNPDHQV----------VMPTvE 124
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGARVTGDVTLN---GEPLAAIdaprlarlraVLPQ-A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFG--------LGKY-HDMNQEEVKSR----VIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE--------- 182
Cdd:PRK13547 92 AQPAFAfsareivlLGRYpHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRL--ARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADV 242
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
58-243 |
4.59e-15 |
|
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: 74.95 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfveKPKNFVFQNPDHQVVMP-TVEADVAFGLgkyhd 136
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGRISFSPQTSWIMPgTIKDNIIFGL----- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 mNQEEVKSR-VIKA--LEavgmRDYMQRPIQ----------TLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:TIGR01271 512 -SYDEYRYTsVIKAcqLE----EDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23296450 204 VIKA-VKDLINAKkgdvTALWVTHRLEELKYADGAVYMENG 243
Cdd:TIGR01271 587 IFEScLCKLMSNK----TRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
59-254 |
4.77e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK--------------------------NFVFQ 112
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadknqlrllrtrlTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 NPD---HQVVMPTV-EADV-AFGLGKyhdmnqEEVKSRVIKALEAVGMRDYMQR--PIQtLSGGQKQRIAIAGALAEACK 185
Cdd:PRK10619 100 HFNlwsHMTVLENVmEAPIqVLGLSK------QEARERAVKYLAKVGIDERAQGkyPVH-LSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 186 VLLLDELTTFLDESDQMGVIKAVKDLinAKKGDvTALWVTHRLEELKYADGAV-YMENGRVVRHGDAATI 254
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQL--AEEGK-TMVVVTHEMGFARHVSSHViFLHQGKIEEEGAPEQL 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
65-216 |
9.01e-15 |
|
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: 73.67 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 65 FRIP---SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQ---------------NPDHQVVM-Ptvea 125
Cdd:COG1245 91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKrfrgtelqdyfkklaNGEIKVAHkP---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 dvafglgKYHDMNQEEVKSRVIKALEAV-------------GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:COG1245 167 -------QYVDLIPKVFKGTVRELLEKVdergkldelaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180
....*....|....*....|....
gi 23296450 193 TTFLDESDQMGVIKAVKDLINAKK 216
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGK 263
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-197 |
9.38e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 37 NVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPK-NFVFQNP 114
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKlAYVDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 DHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIkaleaVGMRDYM----QRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:TIGR03719 395 DALDPNKTVWEEISGGL-DIIKLGKREIPSRAY-----VGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
....*..
gi 23296450 191 ELTTFLD 197
Cdd:TIGR03719 469 EPTNDLD 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
41-269 |
9.74e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQGISVPI------LRDCSFRIPSGQLWMILGPNGCGKST----LLKILAgvvnpSSGTV-FVEKP-KN 108
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKRTvdhnvvVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIwFDGQPlHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 F--------------VFQNPdHQVVMP--TVEADVAFGLGKYH-DMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQ 170
Cdd:PRK15134 352 LnrrqllpvrhriqvVFQDP-NSSLNPrlNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHG 249
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL--QQKHQLAYLFISHDLHVVRaLCHQVIVLRQGEVVEQG 508
|
250 260
....*....|....*....|
gi 23296450 250 DAATIsdfIKAKQSSYIDQI 269
Cdd:PRK15134 509 DCERV---FAAPQQEYTRQL 525
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
57-255 |
1.08e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpKNFVFQNPDHQVVMP--------------- 121
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNINYNKLDHKLAAQlgigiiyqelsvide 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 -TVEADVAFG---LGKYHDMN---QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:PRK09700 95 lTVLENLYIGrhlTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 195 FL--DESDQMGVIkavkdlINAKKGDVTAL-WVTHRLEELK-YADGAVYMENGRVVRHGDAATIS 255
Cdd:PRK09700 175 SLtnKEVDYLFLI------MNQLRKEGTAIvYISHKLAEIRrICDRYTVMKDGSSVCSGMVSDVS 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
75-261 |
1.19e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKIL--------------------AGVVNPSSGTVFVEKPKNFVFQNPDHqvvMP-TVEADVAFGLGK 133
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrmndlnpevtitgsivyngHNIYSPRTDTVDLRKEIGMVFQQPNP---FPmSIYENVVYGLRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 134 YHDMNQEEVKSRVIKALEAVGM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdqmgvIKA-- 207
Cdd:PRK14239 113 KGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP------ISAgk 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 208 VKDLINAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI---------SDFIKAK 261
Cdd:PRK14239 187 IEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMfmnpkhketEDYISGK 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
40-256 |
2.11e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNFVFQNPDHQV 118
Cdd:PRK15439 12 LCARSISKQYS-----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 ---VMP---------TVEADVAFGLGKyhdmnQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK15439 87 giyLVPqepllfpnlSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLINakKGdVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLA--QG-VGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
65-235 |
2.25e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 65 FRIPS---GQLWMILGPNGCGKSTLLKILAGVVNPSSGTvFVEKP------KNF---VFQNPDHQVVMPTVEADVafglg 132
Cdd:PRK13409 91 YGLPIpkeGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPswdevlKRFrgtELQNYFKKLYNGEIKVVH----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 133 K--YHDMNQEEVKSRVIKALEAV-------------GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK13409 165 KpqYVDLIPKVFKGKVRELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190
....*....|....*....|....*....|....*....
gi 23296450 198 ESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKY-AD 235
Cdd:PRK13409 245 IRQRLNVARLIRELAEGK----YVLVVEHDLAVLDYlAD 279
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
43-252 |
2.38e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 70.75 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGvvNPS----SGTVFV-----------EKPK 107
Cdd:TIGR01978 4 KDLHVSVEDK-----EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFkgqdllelepdERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPDHQVVMPTVEADV-----------AFGLGKYHDMN-QEEVKsrviKALEAVGM-RDYMQRPIQT-LSGGQKQR 173
Cdd:TIGR01978 77 AGLFLAFQYPEEIPGVSNLEflrsalnarrsARGEEPLDLLDfEKLLK----EKLALLDMdEEFLNRSVNEgFSGGEKKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDesdqMGVIKAVKDLINAKKGDVTA-LWVTHRLEELKY--ADGAVYMENGRVVRHGD 250
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLD----IDALKIVAEGINRLREPDRSfLIITHYQRLLNYikPDYVHVLLDGRIVKSGD 228
|
..
gi 23296450 251 AA 252
Cdd:TIGR01978 229 VE 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
62-241 |
2.60e-14 |
|
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: 72.47 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 62 DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKN--FVFQNPdhqvvmptveadvAFGLGKYHD--- 136
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKlfYVPQRP-------------YMTLGTLRDqii 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 --MNQEEVKSR------VIKALEAVGMRDYMQRPI---------QTLSGGQKQRIAIAGALAEACKVLLLDELTTfldes 199
Cdd:TIGR00954 537 ypDSSEDMKRRglsdkdLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTS----- 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23296450 200 dqmGVIKAVKDLI--NAKKGDVTALWVTHRLEELKYADGAVYME 241
Cdd:TIGR00954 612 ---AVSVDVEGYMyrLCREFGITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
48-254 |
3.41e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 48 SVSTRQGisvPIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFV-EKPknfVFQNPDH---------- 116
Cdd:PRK03695 7 AVSTRLG---PL----SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFaGQP---LEAWSAAelarhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 117 QVVMPTVEADVAFGLGKY-HDMNQEEVKSRVIKAL-EAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE-------ACKVL 187
Cdd:PRK03695 76 QQQTPPFAMPVFQYLTLHqPDKTRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 188 LLDELTTFLDESDQmgviKAVKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK03695 156 LLDEPMNSLDVAQQ----AALDRLLSelCQQG-IAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
64-250 |
4.49e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------VEKPKNFVFQNPDHQV--VMpTVEA 125
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmkddewraVRSDIQMIFQDPLASLnpRM-TIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAFGLGKYH-DMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK15079 120 IIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23296450 204 VIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:PRK15079 200 VVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
40-254 |
1.41e-13 |
|
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: 68.34 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkpKNFVFQNPDHQ-- 117
Cdd:cd03218 1 LRAENLSKRYGKRK-----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD--GQDITKLPMHKra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 ----VVMP---------TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:cd03218 74 rlgiGYLPqeasifrklTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 185 KVLLLDELTTFLDE---SDQMGVIKAVKD-----LI---NAKkgdvtalwvthrlEELKYADGAVYMENGRVVRHGDAAT 253
Cdd:cd03218 153 KFLLLDEPFAGVDPiavQDIQKIIKILKDrgigvLItdhNVR-------------ETLSITDRAYIIYEGKVLAEGTPEE 219
|
.
gi 23296450 254 I 254
Cdd:cd03218 220 I 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
58-239 |
1.52e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknfvfQNPDHQvvMPTVEADVAF-----GLG 132
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER------QSIKKD--LCTYQKQLCFvghrsGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 133 K--------YHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:PRK13540 87 PyltlrencLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 23296450 205 IKAVKDliNAKKGDVTALwVTHRLEELKYADGAVY 239
Cdd:PRK13540 167 ITKIQE--HRAKGGAVLL-TSHQDLPLNKADYEEY 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
60-230 |
1.78e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.66 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLK------------------------ILAGVVNPssgtVFVEKPKNFVFQNPD 115
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvtfhgknLYAPDVDP----VEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 hqvvmP---TVEADVAFG---LGKYHDMNqEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:PRK14243 102 -----PfpkSIYDNIAYGariNGYKGDMD-ELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23296450 190 DELTTFLDESDQMgvikAVKDLINAKKGDVTALWVTHRLEE 230
Cdd:PRK14243 176 DEPCSALDPISTL----RIEELMHELKEQYTIIIVTHNMQQ 212
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
54-235 |
2.28e-13 |
|
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: 66.58 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLK-ILAgvvnPSSGTVFVEKPKNFvfqnPDHQVVMptveadvafgLG 132
Cdd:cd03238 5 GANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY----ASGKARLISFLPKF----SRNKLIF----------ID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 133 KyhdmnqeevksrvIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK--VLLLDELTTFLDESDQMGVIKAV 208
Cdd:cd03238 67 Q-------------LQFLIDVGL-GYLTlgQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180
....*....|....*....|....*..
gi 23296450 209 KDLINAKkgdVTALWVTHRLEELKYAD 235
Cdd:cd03238 133 KGLIDLG---NTVILIEHNLDVLSSAD 156
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
58-197 |
2.47e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVV---MPTVEADVAfGLGKY 134
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYlghLPGLKADLS-TLENL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 135 HDMNQ---EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK13543 104 HFLCGlhgRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
58-217 |
2.58e-13 |
|
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: 66.90 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTV---------FVEKPKNFVFQNPDHQVVMP--TV 123
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIhyngipykeFAEKYPGEIIYVSEEDVHFPtlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFglgkyhdmnqeevksrvikALEAVGmrDYMQRPIqtlSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:cd03233 101 RETLDF-------------------ALRCKG--NEFVRGI---SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170
....*....|....
gi 23296450 204 VIKAVKDLINAKKG 217
Cdd:cd03233 157 ILKCIRTMADVLKT 170
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
64-254 |
3.32e-13 |
|
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: 69.06 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------KPK-----------NFVFQNPD---HQVVM 120
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtKPGpdgrgrakryiGILHQEYDlypHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTVEAdvAFGLgkyhDMNQEEVKSRVIKALEAVGMRDYMQRPI-----QTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:TIGR03269 384 DNLTE--AIGL----ELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 196 LDESDQMGVIKAVkdlINAKKG-DVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATI 254
Cdd:TIGR03269 458 MDPITKVDVTHSI---LKAREEmEQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
60-256 |
5.11e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.38 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTVEADVAFGLgkYHDMNQ 139
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGL--MMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 140 EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELttfLDESDQMGVIKAVKDLINAKKGDV 219
Cdd:PRK13545 118 EKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQTFTKKCLDKMNEFKEQGK 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 23296450 220 TALWVTHRLEELK-YADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK13545 195 TIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
56-255 |
5.86e-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: 68.31 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVV---NPSSGTVFVEKPknFVFQNPD----------HQVVMPT 122
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWDGEIYWSGSP--LKASNIRdteragiviiHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYHD-------MNQEEVKSRVIKALEAVGMRDY-MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:TIGR02633 91 PELSVAENIFLGNEitlpggrMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 195 FLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATIS 255
Cdd:TIGR02633 171 SLTEKETEILLDIIRDL---KAHGVACVYISHKLNEVKaVCDTICVIRDGQHVATKDMSTMS 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
71-230 |
6.58e-13 |
|
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: 68.50 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 71 QLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----EKPKNFVFQN----PDHQVVMP--TVEADVAFgLGKYHDMNQ 139
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggkdiETNLDAVRQSlgmcPQHNILFHhlTVAEHILF-YAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 140 EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDV 219
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----RSIWDLLLKYRSGR 1111
|
170
....*....|.
gi 23296450 220 TALWVTHRLEE 230
Cdd:TIGR01257 1112 TIIMSTHHMDE 1122
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
59-254 |
8.32e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFqnPDHQVVMPTV-----EADVAFGLGK 133
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL--PLHARARRGIgylpqEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 134 Y----------HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK10895 96 YdnlmavlqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23296450 204 VIKAVKDLINAKKGdvtALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK10895 176 IKRIIEHLRDSGLG---VLITDHNVREtLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
59-255 |
8.81e-13 |
|
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: 67.91 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGV--VNPSSGTV-----------FVEKPKNFVFQNPDHQVVMPTVEA 125
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVERPSKVGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 D---------------VAFGLGKYHDMNQEE-VKSRVIKALEAVGM--RDYMQRPIQ----------------TLSGGQK 171
Cdd:TIGR03269 95 DfwnlsdklrrrirkrIAIMLQRTFALYGDDtVLDNVLEALEEIGYegKEAVGRAVDliemvqlshrithiarDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 172 QRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGD 250
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA--VKASGISMVLTSHWPEVIeDLSDKAIWLENGEIKEEGT 252
|
....*
gi 23296450 251 AATIS 255
Cdd:TIGR03269 253 PDEVV 257
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
59-249 |
9.58e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG------VVNPS---SGTVfVEKPK-----NFVFQNpDHQVVMPTVE 124
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrspkgvKGSGSvllNGMP-IDAKEmraisAYVQQD-DLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFG----LGKyhDMNQEEVKSRVIKALEAVGMRDYMQRPIQT------LSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:TIGR00955 118 EHLMFQahlrMPR--RVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 195 FLDESDQMGVIKAVKDLinAKKGDvTALWVTH----RLEELkyADGAVYMENGRVVRHG 249
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGL--AQKGK-TIICTIHqpssELFEL--FDKIILMAEGRVAYLG 249
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
69-231 |
1.04e-12 |
|
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: 64.32 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 69 SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFvekpknfvfqnpdhqvvmptveadvafglgkYHDMNQEEVKSRVIK 148
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------YIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 149 ALEAVGMRDYMqrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV---KDLINAKKGDVTALWVT 225
Cdd:smart00382 50 LLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrLLLLLKSEKNLTVILTT 123
|
....*.
gi 23296450 226 HRLEEL 231
Cdd:smart00382 124 NDEKDL 129
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
62-197 |
1.06e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 62 DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPK-NFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQ 139
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKlAYVDQSRDALDPNKTVWEEISGGL-DIIKVGN 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 140 EEVKSRVikaleavgmrdYM----------QRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK11819 421 REIPSRA-----------YVgrfnfkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
40-254 |
1.25e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.88 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCFSVStrqgisVPILRDCSFRIPSGQLWMILGPNGCGKS----TLLKILAGVVNPSSGTVFVE----------- 104
Cdd:PRK10418 5 IELRNIALQAA------QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDgkpvapcalrg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 KPKNFVFQNPD------HQVVMPTVEADVAFGlgkyhdmnQEEVKSRVIKALEAVGMRDyMQRPIQT----LSGGQKQRI 174
Cdd:PRK10418 79 RKIATIMQNPRsafnplHTMHTHARETCLALG--------KPADDATLTAALEAVGLEN-AARVLKLypfeMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLInaKKGDVTALWVTH------RLeelkyADGAVYMENGRVVRH 248
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIV--QKRALGMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQ 222
|
....*.
gi 23296450 249 GDAATI 254
Cdd:PRK10418 223 GDVETL 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
39-255 |
3.65e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.89 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknfVFQN-PDHQ 117
Cdd:PRK10789 315 DVNIRQFTYPQTDH-----PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI--------RFHDiPLTK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 -----------VV--MP-----TVEADVAFGlgkYHDMNQEEVKS------------RVIKALEA-VGMRDYMqrpiqtL 166
Cdd:PRK10789 382 lqldswrsrlaVVsqTPflfsdTVANNIALG---RPDATQQEIEHvarlasvhddilRLPQGYDTeVGERGVM------L 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTAlwvtHRLEELKYADGAVYMENGRVV 246
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISA----HRLSALTEASEILVMQHGHIA 528
|
....*....
gi 23296450 247 RHGDAATIS 255
Cdd:PRK10789 529 QRGNHDQLA 537
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-249 |
4.10e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 1 MNGHCLfaaspPRLFPLRSISSSVSPSGSYRikfSDNVA-----VECRNLCFSVSTRQGI------SVPILRDCSFRIPS 69
Cdd:PRK10261 278 MKGLDY-----PRRFPLISLEHPAKQEPPIE---QDTVVdgepiLQVRNLVTRFPLRSGLlnrvtrEVHAVEKVSFDLWP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 70 GQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------VEKPKNFVFQNPdHQVVMP--TVEADVAFGL 131
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklqaLRRDIQFIFQDP-YASLDPrqTVGDSIMEPL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKD 210
Cdd:PRK10261 429 RVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 23296450 211 LinAKKGDVTALWVTHRL---EELKYADGAVYMenGRVVRHG 249
Cdd:PRK10261 509 L--QRDFGIAYLFISHDMavvERISHRVAVMYL--GQIVEIG 546
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
59-257 |
7.59e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 65.25 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTV---------FV-EKPKNFVFQNPDHQVVMpTVEA 125
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEItyngyrlneFVpRKTSAYISQNDVHVGVM-TVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAF-----GLGKYHDMNQE--------------EV----KSRVIKALEAVGMRDY------------------MQRPIq 164
Cdd:PLN03140 259 TLDFsarcqGVGTRYDLLSElarrekdagifpeaEVdlfmKATAMEGVKSSLITDYtlkilgldickdtivgdeMIRGI- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 165 tlSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGR 244
Cdd:PLN03140 338 --SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQ 415
|
250
....*....|...
gi 23296450 245 VVRHGDAATISDF 257
Cdd:PLN03140 416 IVYQGPRDHILEF 428
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
164-242 |
8.65e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 8.65e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 164 QTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINakKGDVTALWVTHRLEELKYADGAVYMEN 242
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD--KADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
58-249 |
1.00e-11 |
|
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: 62.43 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPKNFVFQNPdhQVVMPTVE 124
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidistipledlrSSLTIIPQDP--TLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVafglgkyhDMNQEEVKSRVIKALEAVGMRDymqrpiqTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:cd03369 100 SNL--------DPFDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23296450 205 IKAVKDLINakkgDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03369 165 QKTIREEFT----NSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
75-250 |
1.15e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSG-------TVF---------VEKPK-NFVFQnpDHQVvMP--TVEADVAFGLGKYh 135
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGrivlngrVLFdaekgiclpPEKRRiGYVFQ--DARL-FPhyKVRGNLRYGMAKS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 dMNQEevKSRVIKALeavGMRDYMQR-PIqTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDesdqmgvIKAVKDLIN- 213
Cdd:PRK11144 105 -MVAQ--FDKIVALL---GIEPLLDRyPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-------LPRKRELLPy 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23296450 214 ----AKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGD 250
Cdd:PRK11144 171 lerlAREINIPILYVSHSLDEiLRLADRVVVLEQGKVKAFGP 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
58-249 |
1.45e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQvvMPTVEADVAFGlgkyHDM 137
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQ--NDSLRENILFG----KAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 138 NQEEVKSrVIKA------LEAV--GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESdqmgVIKAVK 209
Cdd:TIGR00957 726 NEKYYQQ-VLEAcallpdLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIF 800
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23296450 210 DLINAKKG---DVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR00957 801 EHVIGPEGvlkNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
42-234 |
2.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.04 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 42 CRNLCFSVSTRQgisvpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNP-----DH 116
Cdd:PRK13541 4 LHQLQFNIEQKN------LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPyctyiGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 117 QVVMP---TVEADVAFGLGKYhdmNQEEVksrVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK13541 78 NLGLKlemTVFENLKFWSEIY---NSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23296450 194 TFLDESDQmgviKAVKDLI--NAKKGDVTaLWVTHRLEELKYA 234
Cdd:PRK13541 152 TNLSKENR----DLLNNLIvmKANSGGIV-LLSSHLESSIKSA 189
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-268 |
4.37e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGvvNPS----SGTVFVE-------KPKN- 108
Cdd:CHL00131 9 EIKNLHASVNEN-----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKgesildlEPEEr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ------FVFQNPdhqVVMPTVE-AD---VAFGlGKYHDMNQEEVKS----RVIKA-LEAVGMRD-YMQRPI-QTLSGGQK 171
Cdd:CHL00131 82 ahlgifLAFQYP---IEIPGVSnADflrLAYN-SKRKFQGLPELDPleflEIINEkLKLVGMDPsFLSRNVnEGFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 172 QRiaiagalAEACKVLLLDELTTFLDESDQMGVIKAVKDL---INAKKGDVTA-LWVTH--RLEELKYADGAVYMENGRV 245
Cdd:CHL00131 158 KR-------NEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSENSiILITHyqRLLDYIKPDYVHVMQNGKI 230
|
250 260
....*....|....*....|...
gi 23296450 246 VRHGDaATISDFIKAKQSSYIDQ 268
Cdd:CHL00131 231 IKTGD-AELAKELEKKGYDWLKQ 252
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
52-212 |
5.49e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 52 RQGISVPILRDCSFRIPSGQLWM--------------ILGPNGCGKSTLLKILAGVVNPSSGTVF-VEKPKNFVFQNpdH 116
Cdd:PLN03073 503 RPGPPIISFSDASFGYPGGPLLFknlnfgidldsriaMVGPNGIGKSTILKLISGELQPSSGTVFrSAKVRMAVFSQ--H 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 117 QVVMPTVEADVAFGLGK-YHDMNQEEVKSRvikaLEAVGMRDYMQ-RPIQTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:PLN03073 581 HVDGLDLSSNPLLYMMRcFPGVPEQKLRAH----LGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
170
....*....|....*...
gi 23296450 195 FLDesdqmgvIKAVKDLI 212
Cdd:PLN03073 657 HLD-------LDAVEALI 667
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
49-194 |
9.99e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknFVF----QNPDH-QVVMPtv 123
Cdd:NF033858 7 VSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-------EVLggdmADARHrRAVCP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 eaDVAF---GLGK--YHDM---------------NQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:NF033858 77 --RIAYmpqGLGKnlYPTLsvfenldffgrlfgqDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170
....*....|.
gi 23296450 184 CKVLLLDELTT 194
Cdd:NF033858 155 PDLLILDEPTT 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
75-199 |
1.06e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKN--FVFQNP---DHQVVMPTVEADVAFGLG----------KY----H 135
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKvgYLPQEPqldPTKTVRENVEEGVAEIKDaldrfneisaKYaepdA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 DMNQ--EEvKSRVIKALEAVGMRDYMQR---------------PIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD- 197
Cdd:TIGR03719 116 DFDKlaAE-QAELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDa 194
|
..
gi 23296450 198 ES 199
Cdd:TIGR03719 195 ES 196
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
67-233 |
1.18e-10 |
|
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: 59.12 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 67 IPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGtvfvekpknfvfqNPDHQVVMPTVeadvafglgkyhdmnqeevKSRV 146
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------------NDEWDGITPVY-------------------KPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 147 IKaleavgmrdymqrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLInaKKGDVTALWVTH 226
Cdd:cd03222 70 ID-----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS--EEGKKTALVVEH 130
|
....*..
gi 23296450 227 RLEELKY 233
Cdd:cd03222 131 DLAVLDY 137
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
41-197 |
1.28e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKNFVFQ------N 113
Cdd:PRK11147 321 EMENVNYQIDGKQ-----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEVAYFDqhraelD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 114 PDHqvvmpTVEADVAFGlgkyhdmNQE-EVKSRVIKALeavgmrDYMQ----------RPIQTLSGGQKQRIAIAGALAE 182
Cdd:PRK11147 396 PEK-----TVMDNLAEG-------KQEvMVNGRPRHVL------GYLQdflfhpkramTPVKALSGGERNRLLLARLFLK 457
|
170
....*....|....*
gi 23296450 183 ACKVLLLDELTTFLD 197
Cdd:PRK11147 458 PSNLLILDEPTNDLD 472
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
43-249 |
1.40e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQGisvpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKN------------- 108
Cdd:PRK11701 10 RGLTKLYGPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQlrdlyalseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --------FVFQNPdHQVVMPTVEADVAFGlgkyhdmnqeevksrviKALEAVGMRDY----------MQR--------- 161
Cdd:PRK11701 85 rllrtewgFVHQHP-RDGLRMQVSAGGNIG-----------------ERLMAVGARHYgdiratagdwLERveidaarid 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 162 --PiQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINakKGDVTALWVTH-----RLeelkYA 234
Cdd:PRK11701 147 dlP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVR--ELGLAVVIVTHdlavaRL----LA 219
|
250
....*....|....*
gi 23296450 235 DGAVYMENGRVVRHG 249
Cdd:PRK11701 220 HRLLVMKQGRVVESG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
75-199 |
2.51e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVEK----------PKnfvfQNPDHQV---VMPTVeADVAFGLGKYH------ 135
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgikvgylpqePQ----LDPEKTVrenVEEGV-AEVKAALDRFNeiyaay 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 -----DMN---------QE--------EVKSRVIKALEAVGMRDYMQrPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK11819 113 aepdaDFDalaaeqgelQEiidaadawDLDSQLEIAMDALRCPPWDA-KVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
....*..
gi 23296450 194 TFLD-ES 199
Cdd:PRK11819 192 NHLDaES 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
59-226 |
2.72e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------------EKPKNFVFQNpdhQVVMP 121
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeearaklrAKHVGFVFQS---FMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADVAFGL-GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsd 200
Cdd:PRK10584 102 TLNALENVELpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR-- 179
|
170 180
....*....|....*....|....*...
gi 23296450 201 QMGviKAVKDLINAKKGD--VTALWVTH 226
Cdd:PRK10584 180 QTG--DKIADLLFSLNREhgTTLILVTH 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
34-191 |
2.76e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 34 FSDNVAVECRNLCFSVSTrQGISV-PIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQ 112
Cdd:PRK10522 317 FPDWQTLELRNVTFAYQD-NGFSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 NPDHQVVMPTVEADV-AFG--LGkyhDMNQEEVKSRVIKALEAVGMRDYMQ------RPIQtLSGGQKQRIAIAGALAEA 183
Cdd:PRK10522 392 PEDYRKLFSAVFTDFhLFDqlLG---PEGKPANPALVEKWLERLKMAHKLEledgriSNLK-LSKGQKKRLALLLALAEE 467
|
....*...
gi 23296450 184 CKVLLLDE 191
Cdd:PRK10522 468 RDILLLDE 475
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
57-259 |
4.85e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSsGT-----VFVEKPKNF--VFQNPDHQVVMPTVE----- 124
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PH-GSyegeiLFDGEVCRFkdIRDSEALGIVIIHQElalip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ----ADVAFgLG----KYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:NF040905 92 ylsiAENIF-LGneraKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 197 DESDQmgviKAVKDLINA-KKGDVTALWVTHRLEELKY-ADGAVYMENGRVV----RHGDAATISDFIK 259
Cdd:NF040905 171 NEEDS----AALLDLLLElKAQGITSIIISHKLNEIRRvADSITVLRDGRTIetldCRADEVTEDRIIR 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
57-231 |
7.26e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNfvFQNPD----------HQV--VMP-- 121
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVT--FNGPKssqeagigiiHQElnLIPql 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADV--------AFGLGKYHDMNQEevksrVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK10762 95 TIAENIflgrefvnRFGRIDWKKMYAE-----ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 23296450 194 TFLDESDQMGVIKAVKDLINAKKGDVtalWVTHRLEEL 231
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIV---YISHRLKEI 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
49-246 |
7.67e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 49 VSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQN-----------PDHQ 117
Cdd:PRK11614 11 VSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimreavaivPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VVMP--TVEADVAFGlGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPiQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK11614 90 RVFSrmTVEENLAMG-GFFAERDQFQERIKWVYELFPRLHERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23296450 196 LDESdqmgVIKAVKDLINAKKGD-VTALWVTHRLEE-LKYADGAVYMENGRVV 246
Cdd:PRK11614 168 LAPI----IIQQIFDTIEQLREQgMTIFLVEQNANQaLKLADRGYVLENGHVV 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
64-254 |
9.64e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.21 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKS-TLLKILAGVVNPssGTVFVEKpknFVFQNPDHQVVMPT-----VEADVA--------- 128
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEK---LEFNGQDLQRISEKerrnlVGAEVAmifqdpmts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 129 ----FGLG-------KYHDM-NQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK11022 102 lnpcYTVGfqimeaiKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvyPHQ-LSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 193 TTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11022 181 TTALDVTIQAQIIELLLEL--QQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
58-197 |
9.91e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PKNfvfqnpdhqvVMPTVEAD 126
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdpPRN----------VEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 127 VAFGLG-------KYHDMN------------------QEEV--------KSRVIKALEAVGMRDYMqrPIQTLSGGQKQR 173
Cdd:PRK11147 87 VAEGIEeqaeylkRYHDIShlvetdpseknlnelaklQEQLdhhnlwqlENRINEVLAQLGLDPDA--ALSSLSGGWLRK 164
|
170 180
....*....|....*....|....
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
41-191 |
2.16e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHQVV- 119
Cdd:COG1137 5 EAENLVKSYGKRT-----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-----------DGEDIt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 -MP----------------------TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVG---MRDymqRPIQTLSGGQKQR 173
Cdd:COG1137 69 hLPmhkrarlgigylpqeasifrklTVEDNILAVL-ELRKLSKKEREERLEELLEEFGithLRK---SKAYSLSGGERRR 144
|
170
....*....|....*...
gi 23296450 174 IAIAGALAEACKVLLLDE 191
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
53-255 |
2.47e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 53 QGISVP-ILRDCSFRIPSGQlwmIL---GPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF------------------ 109
Cdd:COG1129 260 EGLSVGgVVRDVSFSVRAGE---ILgiaGLVGAGRTELARALFGADPADSGEIRLDgKPVRIrsprdairagiayvpedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ----------VFQNpdhqVVMPTVEADVAFGLgkyhdMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAG 178
Cdd:COG1129 337 kgeglvldlsIREN----ITLASLDRLSRGGL-----LDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 179 ALAEACKVLLLDELTtfldesdqMGV-IKA---VKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDA 251
Cdd:COG1129 408 WLATDPKVLILDEPT--------RGIdVGAkaeIYRLIRelAAEG-KAVIVISSELPElLGLSDRILVMREGRIVGELDR 478
|
....
gi 23296450 252 ATIS 255
Cdd:COG1129 479 EEAT 482
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-249 |
2.57e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSG------------TVF-------VEKPKNFVFQNPDHqvv 119
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrSIFnyrdvleFRRRVGMLFQRPNP--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 MP-TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQT----LSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:PRK14271 113 FPmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 195 FLDESdqmgVIKAVKDLINAKKGDVTALWVTHRL-EELKYADGAVYMENGRVVRHG 249
Cdd:PRK14271 193 ALDPT----TTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-254 |
3.86e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 35 SDNVAVECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknFVFQNP 114
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQK---IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK---MLLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 DHQVV---------MPTVE-ADVA-------------FGLGK--------YHDMNQEEVKSRVIKALEAVGMRD---YMQ 160
Cdd:PRK10261 84 SRQVIelseqsaaqMRHVRgADMAmifqepmtslnpvFTVGEqiaesirlHQGASREEAMVEAKRMLDQVRIPEaqtILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 161 RPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVY 239
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL--QKEMSMGVIFITHDMGVVaEIADRVLV 241
|
250
....*....|....*
gi 23296450 240 MENGRVVRHGDAATI 254
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
43-214 |
4.82e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILA-----GVVnpsSGTVFV---EKPKNF----- 109
Cdd:cd03232 7 KNLNYTVPVKGG-KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILIngrPLDKNFqrstg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -VFQNPDHqvvmptveadvafglgkyhdmnqeEVKSRVIKALE--AVgmrdymqrpIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:cd03232 83 yVEQQDVH------------------------SPNLTVREALRfsAL---------LRGLSVEQRKRLTIGVELAAKPSI 129
|
170 180
....*....|....*....|....*...
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLINA 214
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
64-193 |
5.34e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknFVFQNPdhqvvmptVEAD-------V-----AFGL 131
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-------WLFGQP--------VDAGdiatrrrVgymsqAFSL 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 132 gkY-----------H----DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:NF033858 351 --YgeltvrqnlelHarlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
67-240 |
9.28e-09 |
|
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: 53.52 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 67 IPSGQLWMILGPNGCGKSTLLKILAgvvnpssgtvfvekpknfvfqnpdhqvvmptveadVAFGLGKYHDMNQEEVKSRV 146
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAIG-----------------------------------LALGGAQSATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 147 IKALEAVgmrDYMQRPIQtLSGGQKQRIAIAGALAEA----CKVLLLDELTTFLDESDQMGVIKAVKDLInakKGDVTAL 222
Cdd:cd03227 63 IVAAVSA---ELIFTRLQ-LSGGEKELSALALILALAslkpRPLYILDEIDRGLDPRDGQALAEAILEHL---VKGAQVI 135
|
170
....*....|....*...
gi 23296450 223 WVTHRLEELKYADGAVYM 240
Cdd:cd03227 136 VITHLPELAELADKLIHI 153
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
64-191 |
9.30e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.61 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPknfVFQNPDHQVV----------------MPTVE-- 124
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIlLRGQH---IEGLPGHQIArmgvvrtfqhvrlfreMTVIEnl 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 125 ---------ADVAFGLGKYHDMNQEEVKS--RVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:PRK11300 102 lvaqhqqlkTGLFSGLLKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
48-197 |
1.12e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 48 SVSTRQGISVpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGT-----------VFVEKPK------NFV 110
Cdd:PRK10636 6 SLQIRRGVRV-LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwqlawVNQETPAlpqpalEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 ------FQNPDHQVVMPTVEAD---VAFGLGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGAL 180
Cdd:PRK10636 85 idgdreYRQLEAQLHDANERNDghaIATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170
....*....|....*..
gi 23296450 181 AEACKVLLLDELTTFLD 197
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
75-235 |
1.43e-08 |
|
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: 53.38 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILagvvnpsSGTVFVEKPKNFVFQNPDHQVVMPT---VEADVAFGLGKYHDMnqeeVKSRVIKALE 151
Cdd:cd03240 27 IVGQNGAGKTTIIEAL-------KYALTGELPPNSKGGAHDPKLIREGevrAQVKLAFENANGKKY----TITRSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 152 AV------GMRDYMQRPIQTLSGGQK--QRIAIAGALAEA----CKVLLLDELTTFLDESDqmgVIKAVKDLINAKKGDV 219
Cdd:cd03240 96 NVifchqgESNWPLLDMRGRCSGGEKvlASLIIRLALAETfgsnCGILALDEPTTNLDEEN---IEESLAEIIEERKSQK 172
|
170
....*....|....*...
gi 23296450 220 T--ALWVTHRLEELKYAD 235
Cdd:cd03240 173 NfqLIVITHDEELVDAAD 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
54-230 |
5.59e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVV--MPTVEADVAFGL 131
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgyCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKYH--------DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:TIGR01257 2029 GREHlylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180
....*....|....*....|....*..
gi 23296450 204 VIKAVKDLINAKKGDVTalwVTHRLEE 230
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVL---TSHSMEE 2132
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-226 |
5.83e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHqv 118
Cdd:PRK15064 319 ALEVENLTKGFDNG-----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDH-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 vmptvEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-----DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK15064 392 -----AYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGRllfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190
....*....|....*....|....*....|....
gi 23296450 194 TFLDesdqMGVIKAvkdLINA-KKGDVTALWVTH 226
Cdd:PRK15064 467 NHMD----MESIES---LNMAlEKYEGTLIFVSH 493
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
58-248 |
6.04e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTV-------EADVAFG 130
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIpqspvlfSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 131 LGKYHDMNQEEVksrvIKALEAVGMRDYMQR-PI----------QTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD-E 198
Cdd:PLN03232 1330 IDPFSEHNDADL----WEALERAHIKDVIDRnPFgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDvR 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23296450 199 SDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRH 248
Cdd:PLN03232 1406 TDSL-----IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEY 1450
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
77-216 |
7.39e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 77 GPNGCGKSTLLKILAGVVNPSSGTVFVE--------KPKNFVFQNpdhQVVMPTV------------------------E 124
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklRQDQFAFEE---FTVLDTVimghtelwevkqerdriyalpemsE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 AD---VAFGLGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDesd 200
Cdd:PRK15064 111 EDgmkVADLEVKFAEMDGYTAEARAGELLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD--- 187
|
170
....*....|....*.
gi 23296450 201 qMGVIKAVKDLINAKK 216
Cdd:PRK15064 188 -INTIRWLEDVLNERN 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-255 |
1.94e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 39 AVECRNLCFSVSTRqgISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGT-VFVEKPKNFVFQNPdhQ 117
Cdd:PLN03232 614 AISIKNGYFSWDSK--TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGSVAYVPQVS--W 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VVMPTVEADVAFGlGKYHdmnqeevKSRVIKALEAVGM---------RDYM---QRPIQtLSGGQKQRIAIAGALAEACK 185
Cdd:PLN03232 690 IFNATVRENILFG-SDFE-------SERYWRAIDVTALqhdldllpgRDLTeigERGVN-ISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 186 VLLLDELTTFLDESDQMGVIKA-VKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHGDAATIS 255
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDScMKDELKGK----TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
52-262 |
2.14e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 52 RQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-------------FVEKPKNFVFQNPDHQV 118
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVegvitydgitpeeIKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMP--TVEADVAFGL------GKYHDMNQEE-VKSRVIKALEAVGMR--------DYMQRPIqtlSGGQKQRIAIAGALA 181
Cdd:TIGR00956 149 HFPhlTVGETLDFAArcktpqNRPDGVSREEyAKHIADVYMATYGLShtrntkvgNDFVRGV---SGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 182 EACKVLLLDELTTFLDESDQMGVIKAVKdlINAKKGDVTALWVTHRLEELKYA--DGAVYMENGRVVRHGDAAtisdfiK 259
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALK--TSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQIYFGPAD------K 297
|
...
gi 23296450 260 AKQ 262
Cdd:TIGR00956 298 AKQ 300
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
57-231 |
2.44e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNF-------------VFQNPDhQVVMPT 122
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlFQGKEIDFksskealengismVHQELN-LVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVafGLGKY--------HDMNQEEVKsRVIKALEA-VGMRDymqrPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK10982 90 VMDNM--WLGRYptkgmfvdQDKMYRDTK-AIFDELDIdIDPRA----KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 23296450 194 TFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL 231
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKL---KERGCGIVYISHKMEEI 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
59-245 |
2.49e-07 |
|
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: 50.62 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---------SSGTVFVEK---------PKNFVFQNPDHQVVM 120
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTegdiqidgvSWNSVPLQKwrkafgvipQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTveadvafglGKYHDmnqEEvksrVIKALEAVGMRDYM-QRPIQ----------TLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03289 99 PY---------GKWSD---EE----IWKVAEEVGLKSVIeQFPGQldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 190 DELTTFLDESdqmgVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03289 163 DEPSAHLDPI----TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
58-92 |
3.56e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 3.56e-07
10 20 30
....*....|....*....|....*....|....*
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG 92
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
58-264 |
4.12e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTV-------EADVAFG 130
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpqapvlfSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 131 LGKYHDMNQEEVksrvIKALEAVGMRDYMQRPIQTL-----------SGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PLN03130 1333 LDPFNEHNDADL----WESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 200 DQMGVIKAVKDLINAkkgdVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI-----SDFIKAKQSS 264
Cdd:PLN03130 1409 TDALIQKTIREEFKS----CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlsnegSAFSKMVQST 1474
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-103 |
4.62e-07 |
|
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: 50.57 E-value: 4.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 41 ECRNLCFSVSTRQGISV----PIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV 103
Cdd:COG4615 329 ELRGVTYRYPGEDGDEGftlgPI----DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
41-254 |
5.24e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 41 ECRNLCFSVSTRQGIsVPILRDCSFRIPSGQLWMILGPNGCGKS----TLLKILA--GVVNPSS---GTVFVEKPKN--- 108
Cdd:PRK09473 14 DVKDLRVTFSTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGGSAtfnGREILNLPEKeln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --------FVFQNPdhqvvMPTVEADVAFG------LGKYHDMNQEEVKSRVIKALEAVGM---RDYMQRPIQTLSGGQK 171
Cdd:PRK09473 93 klraeqisMIFQDP-----MTSLNPYMRVGeqlmevLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 172 QRIAIAGALAEACKVLLLDELTTFLDESDQ---MGVIKAVKDLINakkgdvTA-LWVTHRLEELK-YADGAVYMENGRVV 246
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQaqiMTLLNELKREFN------TAiIMITHDLGVVAgICDKVLVMYAGRTM 241
|
....*...
gi 23296450 247 RHGDAATI 254
Cdd:PRK09473 242 EYGNARDV 249
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
81-263 |
6.16e-07 |
|
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: 50.40 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 81 CGKSTLlkilagvvNPSSGTVFVEKpKNFvfqnpdHQVV-MPTVEADvAFGLGKYHDMNQEEVKSRVIKA-------LEA 152
Cdd:TIGR00630 411 CGGTRL--------KPEALAVTVGG-KSI------ADVSeLSIREAH-EFFNQLTLTPEEKKIAEEVLKEirerlgfLID 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 153 VGMrDYM--QRPIQTLSGGQKQRIAIAGAL-AEACKVL-LLDELTTFLDESDQ---MGVIKAVKDLINakkgdvTALWVT 225
Cdd:TIGR00630 475 VGL-DYLslSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNrrlINTLKRLRDLGN------TLIVVE 547
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 23296450 226 HRLEELKYADGAVYM------ENGRVVRHGdaaTISDFIKAKQS 263
Cdd:TIGR00630 548 HDEDTIRAADYVIDIgpgageHGGEVVASG---TPEEILANPDS 588
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
75-235 |
6.21e-07 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 49.18 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLL--------------------KILAGVVNPSSGTVFVEkpknFVFQNPDHQVVMPTVEADVAFGLGKY 134
Cdd:cd03272 28 VVGRNGSGKSNFFaairfvlsdeythlreeqrqALLHEGSGPSVMSAYVE----IIFDNSDNRFPIDKEEVRLRRTIGLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 135 HD----MNQEEVKSRVIKALEAVG--------------------MRDYMQRPIQTLSGGQKQRIAIAGALA-EACK---V 186
Cdd:cd03272 104 KDeyflDKKNVTKNDVMNLLESAGfsrsnpyyivpqgkinsltnMKQDEQQEMQQLSGGQKSLVALALIFAiQKCDpapF 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23296450 187 LLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYAD 235
Cdd:cd03272 184 YLFDEIDAALDAQYR----TAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-222 |
1.19e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 30 YRIKFSD--NVAVECRNLC-----FSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSS--GT 100
Cdd:PLN03211 47 YRVKFENmkNKGSNIKRILghkpkISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 101 VFVEKPK---------NFVFQNpdhQVVMP--TVEADVAF-GLGKYHDMNQEEVKSRVIKA------LEAVGMRDYMQRP 162
Cdd:PLN03211 127 ILANNRKptkqilkrtGFVTQD---DILYPhlTVRETLVFcSLLRLPKSLTKQEKILVAESviselgLTKCENTIIGNSF 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 163 IQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTAL 222
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSM 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-254 |
1.47e-06 |
|
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: 49.17 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 40 VECRNLCfsVSTRQGISVpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK-------NFVFQ 112
Cdd:TIGR00957 1285 VEFRNYC--LRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglhDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 ---NPDHQVVMptvEADVAFGLGKYHDMNQEEVKSrvikALEAVGMRDYMQ-RPI----------QTLSGGQKQRIAIAG 178
Cdd:TIGR00957 1362 itiIPQDPVLF---SGSLRMNLDPFSQYSDEEVWW----ALELAHLKTFVSaLPDkldhecaeggENLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 179 ALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDlETDNL-----IQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
75-197 |
1.99e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVEKP-KNFVFQNpdHQvvMPTVEADVAfGLGKYHDMNQEEVKSRVIKALEAV 153
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiKLGYFAQ--HQ--LEFLRADES-PLQHLARLAPQELEQKLRDYLGGF 417
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 23296450 154 GMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK10636 418 GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-235 |
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 23296450 144 SRVIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTTFLDESDqmgvikaVKDLINA---- 214
Cdd:cd03271 147 ARKLQTLCDVGL-GYIKlgQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHD-------VKKLLEVlqrl 218
|
90 100
....*....|....*....|..
gi 23296450 215 -KKGDvTALWVTHRLEELKYAD 235
Cdd:cd03271 219 vDKGN-TVVVIEHNLDVIKCAD 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
129-249 |
2.41e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 129 FGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:NF000106 108 YMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 23296450 209 KDLInakKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:NF000106 188 RSMV---RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
53-245 |
4.15e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 53 QGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNP-----------------D 115
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVTRSPqdglangivyisedrkrD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 HQVVMPTVEADVA------FGLGKYHDMNQEEVksrvikalEAVGmrDY----------MQRPIQTLSGGQKQRIAIAGA 179
Cdd:PRK10762 340 GLVLGMSVKENMSltalryFSRAGGSLKHADEQ--------QAVS--DFirlfniktpsMEQAIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 180 LAEACKVLLLDELTTFLDesdqMGVIKAVKDLINA-KKGDVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVD----VGAKKEIYQLINQfKAEGLSIILVSSEMPEvLGMSDRILVMHEGRI 473
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
60-254 |
5.40e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTVEaDVAFG---LGkyhd 136
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIE-NIEFKmlcMG---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 MNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELttfLDESDQMGVIKAVKDLINAKK 216
Cdd:PRK13546 115 FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA---LSVGDQTFAQKCLDKIYEFKE 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 23296450 217 GDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13546 192 QNKTIFFVSHNLGQVRqFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
61-245 |
9.52e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 61 RDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN-----FVFQNPDHQVVMPTVEADVA 128
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgkeinalSTAQrlargLVYLPEDRQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 129 FGLGK--YHDMN--QEEVKSRVIkaLE----AVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK15439 360 WNVCAltHNRRGfwIKPARENAV--LEryrrALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23296450 200 DQMGVIKAVKDLinAKKGdVTALWVTHRLEEL-KYADGAVYMENGRV 245
Cdd:PRK15439 438 ARNDIYQLIRSI--AAQN-VAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
43-214 |
1.80e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQGISVpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---SSGTVFVEKPK---------NFV 110
Cdd:TIGR00956 763 RNLTYEVKIKKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPldssfqrsiGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 FQNPDHqVVMPTVEADVAFG--LGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQTLSGGQKQRIAIAGALAEAC 184
Cdd:TIGR00956 842 QQQDLH-LPTSTVRESLRFSayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKP 920
|
170 180 190
....*....|....*....|....*....|.
gi 23296450 185 KVLL-LDELTTFLDESDQMGVIKAVKDLINA 214
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKLADH 951
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
53-251 |
3.04e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 53 QGISVPILR-DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPDHQ-------------- 117
Cdd:PRK11288 261 DGLKGPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-KPIDIRSPRDAiragimlcpedrka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 ---VVMPTVEADVAFGLGKYH-------DMNQE-EVKSRVIKALeAVGMRDYMQrPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK11288 340 egiIPVHSVADNINISARRHHlragcliNNRWEaENADRFIRSL-NIKTPSREQ-LIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 187 LLLDELTTFLDesdqMGVIKAVKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRV---VRHGDA 251
Cdd:PRK11288 418 ILLDEPTRGID----VGAKHEIYNVIYelAAQG-VAVLFVSSDLPEvLGVADRIVVMREGRIageLAREQA 483
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
60-249 |
3.33e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 60 LRDCSFRIPSGQLWMILGPNGCGKSTLlkilagvvnpSSGTVFVEKPKNFV------FQNPDHQvvMPTVEADVAFGLGK 133
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRRYVeslsayARQFLGQ--MDKPDVDSIEGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 134 YHDMNQE--------------EVKS--RVIKALEAVGMR---------DY--MQRPIQTLSGGQKQRIAIAGAL-AEACK 185
Cdd:cd03270 79 AIAIDQKttsrnprstvgtvtEIYDylRLLFARVGIRERlgflvdvglGYltLSRSAPTLSGGEAQRIRLATQIgSGLTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 186 VL-LLDELTTFLDESDQMGVIKAVKDLINAkkGDvTALWVTHRLEELKYADGAVYM------ENGRVVRHG 249
Cdd:cd03270 159 VLyVLDEPSIGLHPRDNDRLIETLKRLRDL--GN-TVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
58-250 |
6.34e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGV--VNPSSGTVfVEKPKNFV---------------FQNPdhqVVM 120
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTV-EFKGKDLLelspedragegifmaFQYP---VEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTVEADvaFGLgkyhdmnQEEV----KSRVIKALEAVGMRDYMQRPIQTL---------------SGGQKQRIAIAGALA 181
Cdd:PRK09580 91 PGVSNQ--FFL-------QTALnavrSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 182 EACKVLLLDELTTFLDesdqMGVIKAVKDLINA-KKGDVTALWVTHRLEELKY--ADGAVYMENGRVVRHGD 250
Cdd:PRK09580 162 LEPELCILDESDSGLD----IDALKIVADGVNSlRDGKRSFIIVTHYQRILDYikPDYVHVLYQGRIVKSGD 229
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-235 |
7.81e-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: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 DMNQEEVK---------SRVIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTTFLDESDQ 201
Cdd:TIGR00630 790 DMTVEEAYeffeavpsiSRKLQTLCDVGL-GYIRlgQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDI 868
|
90 100 110
....*....|....*....|....*....|....
gi 23296450 202 MGVIKAVKDLInaKKGDvTALWVTHRLEELKYAD 235
Cdd:TIGR00630 869 KKLLEVLQRLV--DKGN-TVVVIEHNLDVIKTAD 899
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
60-115 |
2.43e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.52 E-value: 2.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 60 LRDCSFRIPSGQLWMIL-GPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPD 115
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGE 70
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
143-265 |
5.97e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 143 KSRVIKALEAVGMRDY---MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDV 219
Cdd:PRK15093 133 KRRAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRL--NQNNNT 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 23296450 220 TALWVTHRLEEL-KYADGAVYMENGRVVrhgDAATISDFIKAKQSSY 265
Cdd:PRK15093 211 TILLISHDLQMLsQWADKINVLYCGQTV---ETAPSKELVTTPHHPY 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-191 |
8.87e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 43 RNLCFSVSTRQGISVPilrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGT----------VFVEKPKNFV-- 110
Cdd:PRK10938 7 SQGTFRLSDTKTLQLP-----SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFEQLQKLVsd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 -FQNPDHQVVMPTvEADvaFGLgKYHDMNQEEVK--SRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:PRK10938 82 eWQRNNTDMLSPG-EDD--TGR-TTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
....
gi 23296450 188 LLDE 191
Cdd:PRK10938 158 ILDE 161
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-194 |
1.28e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 145 RVIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTT 194
Cdd:COG0178 805 RKLQTLQDVGL-GYIKlgQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTT 858
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
71-129 |
1.36e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 39.94 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 71 QLWMILGPNGCGKSTLLKILAGVVNPSsgtvFVE--KPKNFVFQNPDHQVVMPTVEADVAF 129
Cdd:TIGR00602 111 RILLITGPSGCGKSTTIKILSKELGIQ----VQEwsNPTLPDFQKNDHKVTLSLESCFSNF 167
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-235 |
1.48e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 147 IKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTTFLDESDQMGVIKAVKDLINAKKgdvTA 221
Cdd:PRK00635 790 IHALCSLGL-DYLPlgRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH---TV 865
|
90
....*....|....
gi 23296450 222 LWVTHRLEELKYAD 235
Cdd:PRK00635 866 VIIEHNMHVVKVAD 879
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-245 |
1.90e-03 |
|
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: 39.42 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 37 NVAVECRNL-CFSVSTRQGISVpilRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVV-NPSSGTVFVEKpKNFVFQNP 114
Cdd:TIGR02633 255 DVILEARNLtCWDVINPHRKRV---DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFING-KPVDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 ----DHQVVMptVEAD-------VAFGLGK---YHDMNQEEVKSRVIKALEAVGMRDYMQR----------PIQTLSGGQ 170
Cdd:TIGR02633 331 aqaiRAGIAM--VPEDrkrhgivPILGVGKnitLSVLKSFCFKMRIDAAAELQIIGSAIQRlkvktaspflPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL--AQEG-VAIIVVSSELAEvLGLSDRVLVIGEGKL 481
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
75-215 |
5.10e-03 |
|
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: 37.67 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 75 ILGPNGCGKSTLLKILAGVVNPSSGTVFveKPKNFvFQNPDHQVVMPTVEADVAFGLGK-YHDMNQEEVKSRVIKALEA- 152
Cdd:COG3593 28 LVGENNSGKSSILEALRLLLGPSSSRKF--DEEDF-YLGDDPDLPEIEIELTFGSLLSRlLRLLLKEEDKEELEEALEEl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 153 ---------------------------------------------VGMRDYMQRPIQTLSGGQKQRIAIA--GALAEACK 185
Cdd:COG3593 105 neelkealkalnellseylkelldgldlelelsldeledllkslsLRIEDGKELPLDRLGSGFQRLILLAllSALAELKR 184
|
170 180 190
....*....|....*....|....*....|....*
gi 23296450 186 -----VLLLDELTTFLDESDQMGVIKAVKDLINAK 215
Cdd:COG3593 185 apanpILLIEEPEAHLHPQAQRRLLKLLKELSEKP 219
|
|
|