|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
22-275 |
2.29e-128 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 364.80 E-value: 2.29e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 22 STAAVPLSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR 101
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLElRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDtpeaPATIQRIVTVDRSHPRD---RA 257
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR----PGRIVEEIDVDLPRPRDrelRT 237
|
250
....*....|....*...
gi 1091083680 258 DAEITALRSELLAELGVE 275
Cdd:COG1116 238 SPEFAALRAEILDLLREE 255
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
28-249 |
1.10e-106 |
|
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: 308.25 E-value: 1.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQ 107
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:cd03293 81 QDALLPWLTVLDNVALGLElQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 187 ALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKdtpeAPATIQRIVTVD 249
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA----RPGRIVAEVEVD 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
28-241 |
1.61e-80 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 246.55 E-value: 1.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAI 104
Cdd:COG3842 6 LELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPekrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLrMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL--GK----DTPE----APAT 241
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMndGRieqvGTPEeiyeRPAT 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-272 |
1.21e-79 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 241.30 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQ 107
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRlRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 187 ALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLgkdTPEaPATIQRIVTVDRSH-------PRD-RAD 258
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM---SPG-PGRIVERLELDFSRrflagedARAiKSD 239
|
250
....*....|....
gi 1091083680 259 AEITALRSELLAEL 272
Cdd:COG4525 240 PAFIALREELLDII 253
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
28-231 |
3.31e-75 |
|
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: 228.17 E-value: 3.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAI 104
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-242 |
6.60e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 216.86 E-value: 6.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAI 104
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKlRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL--GK----DTPEA----PATI 242
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMndGRiqqvGTPEElydrPANL 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
47-269 |
2.31e-68 |
|
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: 211.56 E-value: 2.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQEPRLLPWRTVADNVALG-- 124
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAvd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 --LPQgTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLD 202
Cdd:TIGR01184 81 rvLPD-LSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 203 VHRQDPTTILLVTHDVEEALYLSDRVIVLgkdTPEAPATIQRIVTVDRSHPRDRA----DAEITALRSELL 269
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVML---TNGPAANIGQILEVPFPRPRDRLevveDPSYYDLRNEAL 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
28-231 |
1.37e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 209.51 E-value: 1.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------- 100
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 RVAIG--FQEPRLLPWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:COG1136 85 RRHIGfvFQFFNLLPELTALENVALPLlLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDvEEALYLSDRVIVL 231
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
42-241 |
8.67e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 211.16 E-value: 8.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTGLDPR---VAIGFQEPRLLPWRTV 117
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLFTNLPPRerrVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:COG1118 93 AENIAFGLRvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL--GK----DTP----EAPAT 241
Cdd:COG1118 173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMnqGRieqvGTPdevyDRPAT 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
28-231 |
3.69e-66 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 205.42 E-value: 3.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR------ 101
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 ---VAIGFQEPRLLPWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLlLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYlSDRVIVL 231
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIEL 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
30-241 |
2.04e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 206.48 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRI---TAGTVRIGEKAVTGLDP---RVA 103
Cdd:COG1125 4 FENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRM---INRLiepTSGRILIDGEDIRDLDPvelRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGF--QEPRLLPWRTVADNVALgLPQ--GTKKSEGAASVARLLDLVGL--GEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:COG1125 78 IGYviQQIGLFPHMTVAENIAT-VPRllGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK------DTPEA----PAT 241
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREgrivqyDTPEEilanPAN 230
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
47-241 |
2.70e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 208.80 E-value: 2.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---------RVAIGFQEPRLLPWRTV 117
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKkelrelrrkKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:COG4175 123 LENVAFGLEiQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYLSDRvIVLGKD-------TPE----APAT 241
Cdd:COG4175 203 QDELLELQAKLKKTIVFITHDLDEALRLGDR-IAIMKDgrivqigTPEeiltNPAN 257
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-269 |
2.01e-63 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 199.90 E-value: 2.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 23 TAAVPLSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRV 102
Cdd:PRK11247 8 NQGTPLLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPRLLPWRTVADNVALGLpqgtkKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGL-----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 183 EPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL--GKdtpeapatIQRIVTVDRSHPRDRADAE 260
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIeeGK--------IGLDLTVDLPRPRRRGSAR 230
|
....*....
gi 1091083680 261 ITALRSELL 269
Cdd:PRK11247 231 LAELEAEVL 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
28-241 |
3.59e-62 |
|
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: 195.92 E-value: 3.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAI 104
Cdd:cd03300 1 IELENVSKFY---GGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhkrPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK------DTP----EAPAT 241
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKgkiqqiGTPeeiyEEPAN 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
28-254 |
3.63e-62 |
|
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: 195.97 E-value: 3.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------R 101
Cdd:COG1127 6 IEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIG--FQEPRLLPWRTVADNVALGLPQGTKKSEGAAS--VARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:COG1127 82 RRIGmlFQGGALFDSLTVFENVAFPLREHTDLSEAEIRelVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVTVDrsHPR 254
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD--DPW 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
28-231 |
1.17e-60 |
|
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: 191.57 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR------ 101
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 --VAIGFQEPR--LLPWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLG---EYATHRPKEISGGMAQRVSLARALA 173
Cdd:cd03257 82 keIQMVFQDPMssLNPRMTIGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091083680 174 RNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
47-241 |
3.02e-60 |
|
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: 192.09 E-value: 3.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD---------PRVAIGFQEPRLLPWRTV 117
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:cd03294 120 LENVAFGLEvQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYLSDRvIVLGKD-------TPE----APAT 241
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDR-IAIMKDgrlvqvgTPEeiltNPAN 254
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
28-260 |
6.85e-59 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 191.40 E-value: 6.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRV---AI 104
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKrdyGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLkNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVTvdrsHPRDRADAE 260
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYR----HPATPFVAD 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-231 |
3.77e-58 |
|
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: 193.58 E-value: 3.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 5 SAVTDVPTSEKNGRRAVSTAAVPLSFEGVGQSFPVPG-GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRI 83
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 84 TAGTVRIGEKAVTGLDP--------RVAIGFQEPR--LLPWRTVADNVALGLPQ--GTKKSEGAASVARLLDLVGLG-EY 150
Cdd:COG1123 318 TSGSILFDGKDLTKLSRrslrelrrRVQMVFQDPYssLNPRMTVGDIIAEPLRLhgLLSRAERRERVAELLERVGLPpDL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 151 ATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIV 230
Cdd:COG1123 398 ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAV 477
|
.
gi 1091083680 231 L 231
Cdd:COG1123 478 M 478
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-254 |
5.49e-58 |
|
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: 185.01 E-value: 5.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------- 100
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 -RVAIGFQEPRLLPWRTVADNVALGLPQGTKKSEG--AASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:cd03261 77 rRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVTVDrsHPR 254
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD--DPL 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
28-241 |
8.00e-58 |
|
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: 184.81 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRI---TAGTVRIGEKAVTGLDP---R 101
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKM---INRLiepTSGEIFIDGEDIREQDPvelR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGF--QEPRLLPWRTVADNVALgLPQ--GTKKSEGAASVARLLDLVGL--GEYATHRPKEISGGMAQRVSLARALARN 175
Cdd:cd03295 75 RKIGYviQQIGLFPHMTVEENIAL-VPKllKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 176 PGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK------DTPEA----PAT 241
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNgeivqvGTPDEilrsPAN 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
42-231 |
1.38e-57 |
|
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: 182.00 E-value: 1.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGL-------DPRVAIGFQEPRLLPW 114
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelpplRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALGLpqgtkksegaasvarlldlvglgeyathrpkeiSGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:cd03229 91 LTVLENIALGL---------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03229 138 EVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
28-231 |
1.22e-56 |
|
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: 180.91 E-value: 1.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAI 104
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGLPQ-GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLrKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
29-231 |
1.67e-56 |
|
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: 180.36 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 29 SFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RVA 103
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelrrKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGFQEPRL-LPWRTVADNVALGLPQ-GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:cd03225 79 LVFQNPDDqFFGPTVEEEVAFGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQdPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
46-231 |
2.49e-56 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 181.44 E-value: 2.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQEPRLLPWRTVADNVALGL 125
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 126 P-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVH 204
Cdd:PRK11248 96 QlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180
....*....|....*....|....*..
gi 1091083680 205 RQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-231 |
2.96e-56 |
|
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: 181.15 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-----V 102
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafrrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPR--LLPWRTVADNVALGLpQGTKKSEGAASVARLLDLVGLG-EYATHRPKEISGGMAQRVSLARALARNPGVL 179
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAEPL-RIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 180 LLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-233 |
8.41e-56 |
|
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: 179.45 E-value: 8.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RV 102
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrelrrKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPR---LLPwrTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:COG1122 78 GLVFQNPDdqlFAP--TVEEDVAFGPeNLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
28-233 |
1.06e-55 |
|
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: 179.31 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------R 101
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIG--FQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:cd03258 82 RRIGmiFQHFNLLSSRTVFENVALPLEiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
28-231 |
1.24e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 182.20 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------R 101
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIG--FQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:COG1135 82 RKIGmiFQHFNLLSSRTVAENVALPLEiAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVL 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-231 |
3.17e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 177.55 E-value: 3.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-VA--- 103
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReIPylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 --IG--FQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:COG2884 79 rrIGvvFQDFRLLPDRTVYENVALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPKRVLEL 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
28-238 |
2.30e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.64 E-value: 2.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRV--AIG 105
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVrrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 F--QEPRLLPWRTVADNVAL--GLpQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:COG1131 77 YvpQEPALYPDLTVRENLRFfaRL-YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK------DTPEA 238
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKgrivadGTPDE 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
47-233 |
9.34e-54 |
|
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: 174.45 E-value: 9.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVADNVAL 123
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 124 GL-----PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQD 198
Cdd:cd03296 98 GLrvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 199 LLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03296 178 WLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
51-231 |
1.15e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.48 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 51 SFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--R-VAIGFQEPRLLPWRTVADNVALGLPQ 127
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaeRpVSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 128 GTKKSEGA-ASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQ 206
Cdd:COG3840 99 GLKLTAEQrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRE 178
|
170 180
....*....|....*....|....*
gi 1091083680 207 DPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG3840 179 RGLTVLMVTHDPEDAARIADRVLLV 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-231 |
2.63e-52 |
|
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: 170.31 E-value: 2.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 22 STAAVPLSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP- 100
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 --------RVAIGFQEPRLLPWRTVADNVALGLP-QGTKKSEGAAsvARLLDLVGLGEYATHRPKEISGGMAQRVSLARA 171
Cdd:COG4181 83 ararlrarHVGFVFQSFQLLPTLTALENVMLPLElAGRRDARARA--RALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 172 LARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALyLSDRVIVL 231
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRL 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
28-231 |
1.56e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 168.63 E-value: 1.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA---- 103
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 -IG--FQEPRLLPWRTVADNVALGL--PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:COG1126 78 kVGmvFQQFNLFPHLTVLENVTLAPikVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 179 LLLDEPFGALD-ALTRInmqdlLLDVHRQ---DPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1126 158 MLFDEPTSALDpELVGE-----VLDVMRDlakEGMTMVVVTHEMGFAREVADRVVFM 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
28-229 |
1.58e-51 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 167.71 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG-------LDP 100
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknineLRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 RVAIGFQEPRLLPWRTVADNVALGL--PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPikVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 179 LLLDEPFGALDAltriNMQDLLLDVHRQ---DPTTILLVTHDVEEALYLSDRVI 229
Cdd:cd03262 157 MLFDEPTSALDP----ELVGEVLDVMKDlaeEGMTMVVVTHEMGFAREVADRVI 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
30-232 |
4.43e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 170.75 E-value: 4.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------RVA 103
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkaRRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IG--FQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:PRK11153 84 IGmiFQHFNLLSSRTVFDNVALPLElAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLG 232
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVID 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
28-231 |
5.06e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 171.28 E-value: 5.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAI 104
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRmQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-237 |
1.15e-50 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 170.02 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAI 104
Cdd:PRK11650 4 LKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPE 237
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-235 |
4.22e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.83 E-value: 4.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RV 102
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrrQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPRLlpWR-TVADNVALGLpQGTKKSEGAASVARLLDLVGLGEYATHRP-KEISGGMAQRVSLARALARNPGVLL 180
Cdd:COG4619 77 AYVPQEPAL--WGgTVRDNLPFPF-QLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDT 235
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
28-231 |
4.69e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 165.23 E-value: 4.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR------ 101
Cdd:COG3638 3 LELRNLSKRYP--GGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 --VAIGFQEPRLLPWRTVADNVALG-LPQ-GTKKS-------EGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLAR 170
Cdd:COG3638 80 rrIGMIFQQFNLVPRLSVLTNVLAGrLGRtSTWRSllglfppEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 171 ALARNPGVLLLDEPFGALD-ALTRINMqDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG3638 160 ALVQEPKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGL 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
42-231 |
6.99e-49 |
|
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: 162.14 E-value: 6.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-----VAIGFQEPRLLPWRT 116
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarrIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALG-LP-QGTKKSEGA---ASVARLLDLVGLGEYAtHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDA 190
Cdd:COG1120 92 VRELVALGrYPhLGLFGRPSAedrEAVEEALERTGLEHLA-DRPvDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 191 LTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
31-241 |
2.10e-48 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 164.10 E-value: 2.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 31 EGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGL---DPRVAIGFQ 107
Cdd:PRK10851 6 ANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLharDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLPWRTVADNVALG---LPQGTKKSEGA--ASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGltvLPRRERPNAAAikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 183 EPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK------DTPE----APAT 241
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQgnieqaGTPDqvwrEPAT 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
42-231 |
2.24e-48 |
|
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: 160.79 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRV--AIGF--QEPRLLPWRTV 117
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrQIGVlpDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVA-LGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:COG4555 92 RENIRyFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDvHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-233 |
1.09e-47 |
|
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: 161.37 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL---NRITAGTVRIGEKAVTGLDP---- 100
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEkelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 -----RVAIGFQEPR--LLPWRTVADNVA--LGLPQGTKKSEGAASVARLLDLVGL---GEYATHRPKEISGGMAQRVSL 168
Cdd:COG0444 82 kirgrEIQMIFQDPMtsLNPVMTVGDQIAepLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 169 ARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIV--LGK 233
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVmyAGR 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
28-269 |
2.73e-47 |
|
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: 164.69 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITA---GTVRIGEKAVTGLDP---- 100
Cdd:COG1123 5 LEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEalrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 -RVAIGFQEPR--LLPWrTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNP 176
Cdd:COG1123 83 rRIGMVFQDPMtqLNPV-TVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 177 GVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK-------DTPEAPATIQRIVTVD 249
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDgrivedgPPEEILAAPQALAAVP 241
|
250 260
....*....|....*....|
gi 1091083680 250 RSHPRDRADAEITALRSELL 269
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPLL 261
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
42-241 |
3.53e-47 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 157.65 E-value: 3.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVA 118
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARdrkIGFVFQHYALFKHLTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQ 197
Cdd:TIGR00968 91 DNIAFGLEiRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 198 DLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK------DTP----EAPAT 241
Cdd:TIGR00968 171 SWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNgkieqiGSPdevyDHPAN 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
42-233 |
4.23e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.56 E-value: 4.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRvaIGF--QEpRLLPWR---T 116
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR--IGYvpQR-AEVDWDfpiT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGLPQGTK-----KSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:COG1121 94 VRDVVLMGRYGRRGlfrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1091083680 192 TRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:COG1121 174 TEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNR 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
42-231 |
7.21e-47 |
|
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: 156.19 E-value: 7.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRI-----TAGTVRIGEKAVTGLDP-------RVAIGFQEP 109
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVdvlelrrRVGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 110 RLLPwRTVADNVALGLP-QGTKKSEG-AASVARLLDLVGLGEYATHR--PKEISGGMAQRVSLARALARNPGVLLLDEPF 185
Cdd:cd03260 91 NPFP-GSIYDNVAYGLRlHGIKLKEElDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1091083680 186 GALDALTRINMQDLLLDVHRQdpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03260 170 SALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFL 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-231 |
2.30e-46 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 155.42 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------- 100
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 -RVAIGFQEPRLLPWRTVADNVALG----------LPQGTKKSEGAASVArLLDLVGLGEYATHRPKEISGGMAQRVSLA 169
Cdd:cd03256 78 rQIGMIFQQFNLIERLSVLENVLSGrlgrrstwrsLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 170 RALARNPGVLLLDEPFGALD-ALTRINMqDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03256 157 RALMQQPKLILADEPVASLDpASSRQVM-DLLKRINREEGITVIVSLHQVDLAREYADRIVGL 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
62-237 |
2.49e-46 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 158.04 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 62 VIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVADNVALGLP-QGTKKSEGAAS 137
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHlrhINMVFQSYALFPHMTVEENVAFGLKmRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 138 VARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHD 217
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....*.
gi 1091083680 218 VEEALYLSDRVIVL--GK----DTPE 237
Cdd:TIGR01187 161 QEEAMTMSDRIAIMrkGKiaqiGTPE 186
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
50-231 |
1.42e-45 |
|
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: 152.45 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAaPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-------GEKAVTgLDP---RVAIGFQEPRLLPWRTVAD 119
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdSRKKIN-LPPqqrKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPqGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDL 199
Cdd:cd03297 95 NLAFGLK-RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|..
gi 1091083680 200 LLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
42-234 |
3.28e-45 |
|
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: 151.53 E-value: 3.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQEpRLLPWR---TVA 118
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQR-RSIDRDfpiSVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGL-----PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:cd03235 89 DVVLMGLyghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 194 INMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGKD 234
Cdd:cd03235 169 EDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
42-232 |
4.53e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 151.10 E-value: 4.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAG-LNRI--TAGTVRIGEKAVTGLDP---RVAIGFQEPRLLPWR 115
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAeqrRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRIN 195
Cdd:COG4136 92 SVGENLAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 196 MQDLLLDVHRQDPTTILLVTHDVEEALyLSDRVIVLG 232
Cdd:COG4136 172 FREFVFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLG 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
51-231 |
1.12e-44 |
|
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: 150.34 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 51 SFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVADNVALGLPQ 127
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAdrpVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 128 GTK-KSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQ 206
Cdd:cd03298 98 GLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180
....*....|....*....|....*
gi 1091083680 207 DPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
28-231 |
1.81e-44 |
|
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: 150.96 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--RVAIG 105
Cdd:COG0411 5 LEVRGLTKRF---GGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhrIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 ----FQEPRLLPWRTVADNVALGLPQGTKKS----------------EGAASVARLLDLVGLGEYATHRPKEISGGMAQR 165
Cdd:COG0411 81 iartFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 166 VSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-231 |
1.44e-43 |
|
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: 147.97 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--RVAIG 105
Cdd:cd03219 1 LEVRGLTKRF---GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 ----FQEPRLLPWRTVADNVALGLPQGTKKSEGAASVAR-----------LLDLVGLGEYATHRPKEISGGMAQRVSLAR 170
Cdd:cd03219 77 igrtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARReereareraeeLLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 171 ALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVL 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
30-233 |
4.20e-43 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 146.24 E-value: 4.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-------- 101
Cdd:TIGR02673 4 FHNVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlpllrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEvRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRG-TTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-231 |
6.87e-43 |
|
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: 155.38 E-value: 6.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 7 VTDVPTSEKNGRRAVSTAAVP--LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRIT 84
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKgdIELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 85 AGTVRIGEKAVTGLDPRV---AIGF--QEPRLLPwRTVADNVALGLPQgtkksegaASVARL---LDLVGLGEYATHRPK 156
Cdd:COG2274 529 SGRILIDGIDLRQIDPASlrrQIGVvlQDVFLFS-GTIRENITLGDPD--------ATDEEIieaARLAGLHDFIEALPM 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 157 -----------EISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRqdPTTILLVTHDvEEALYLS 225
Cdd:COG2274 600 gydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLA 676
|
....*.
gi 1091083680 226 DRVIVL 231
Cdd:COG2274 677 DRIIVL 682
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
42-231 |
1.58e-42 |
|
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: 143.31 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT--GLDPRVAIGF--QEPRLLPWRTV 117
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkePEEVKRRIGYlpEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALglpqgtkksegaasvarlldlvglgeyathrpkeiSGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQ 197
Cdd:cd03230 91 RENLKL-----------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....
gi 1091083680 198 DLLLDvHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03230 136 ELLRE-LKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
42-233 |
2.05e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 149.22 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVlRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVA 118
Cdd:PRK11607 31 GQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYqrpINMMFQSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGLPQGT-KKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQ 197
Cdd:PRK11607 110 QNIAFGLKQDKlPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 1091083680 198 DLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
46-231 |
4.13e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 144.40 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAIGFQEPRLLPWRTVADNVA 122
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPekrDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 123 LGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLL 201
Cdd:cd03299 94 YGLKkRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|
gi 1091083680 202 DVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
42-232 |
2.70e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 140.26 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRvaigfqeprllpwrTVADNV 121
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK--------------ELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 122 ALgLPQgtkksegaasvarLLDLVGLGEYAtHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLL 200
Cdd:cd03214 76 AY-VPQ-------------ALELLGLAHLA-DRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190
....*....|....*....|....*....|..
gi 1091083680 201 LDVHRQDPTTILLVTHDVEEALYLSDRVIVLG 232
Cdd:cd03214 141 RRLARERGKTVVMVLHDLNLAARYADRVILLK 172
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
28-231 |
3.18e-41 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 142.44 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV--------RIGEKAVTGLD 99
Cdd:TIGR02315 2 LEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 PRVAIGFQEPRLLPWRTVADNV---ALGLPQGTKKSEGAASVA------RLLDLVGLGEYATHRPKEISGGMAQRVSLAR 170
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLGRFSEEdkeralSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 171 ALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
50-231 |
4.83e-41 |
|
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: 144.86 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEK----AVTGLD---PRVAIG--FQEPRLLPWRTVADN 120
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFlppHRRRIGyvFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLPQgTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLL 200
Cdd:COG4148 98 LLYGRKR-APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190
....*....|....*....|....*....|.
gi 1091083680 201 LDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG4148 177 ERLRDELDIPILYVSHSLDEVARLADHVVLL 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-233 |
5.89e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.10 E-value: 5.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 21 VSTAAVPLSFEGVGQSFPVPGG----THEVLR---GVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEK 93
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGlfgrTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 94 AVTGLDP--------RVAIGFQEPR--LLPWRTVADNVALGLP-QGTK-KSEGAASVARLLDLVGLGEYATHR-PKEISG 160
Cdd:COG4608 81 DITGLSGrelrplrrRMQMVFQDPYasLNPRMTVGDIIAEPLRiHGLAsKAERRERVAELLELVGLRPEHADRyPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 161 GMAQRVSLARALARNPGVLLLDEPFGALDALTR---INmqdLLLDVHRQDPTTILLVTHD---VEealYLSDRVIV--LG 232
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQaqvLN---LLEDLQDELGLTYLFISHDlsvVR---HISDRVAVmyLG 234
|
.
gi 1091083680 233 K 233
Cdd:COG4608 235 K 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
28-231 |
6.86e-41 |
|
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: 139.06 E-value: 6.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RV 102
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeslrkNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPRLLPwRTVADNValglpqgtkksegaasvarlldlvglgeyathrpkeISGGMAQRVSLARALARNPGVLLLD 182
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 183 EPFGALDALTRINMQDLLLDVHRQdpTTILLVTHDVEEALyLSDRVIVL 231
Cdd:cd03228 122 EATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIR-DADRIIVL 167
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
44-238 |
7.70e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.21 E-value: 7.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--------RVAIGFQEP-RLLPW 114
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkdlrkKVGLVFQFPeHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALGlPQ--GTKKSEGAASVARLLDLVGLGE-YATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:TIGR04521 98 ETVYKDIAFG-PKnlGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 192 TRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL--GK----DTPEA 238
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMhkGKivldGTPRE 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-231 |
9.19e-41 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 144.40 E-value: 9.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 29 SFEGVGQSFpvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIG 105
Cdd:PRK11000 5 TLRNVTKAY---GDVV-ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 FQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKlAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
28-231 |
1.07e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 140.18 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR------ 101
Cdd:TIGR02211 2 LKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNeraklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 -VAIGF--QEPRLLPWRTVADNVALGLPQGTKKSEGAASVA-RLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:TIGR02211 82 nKKLGFiyQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAyEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLsDRVIVL 231
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEM 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
42-233 |
2.94e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.99 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRvaigfqeprllpwrTVADNV 121
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE--------------ELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 122 ALgLPQgtkksegaasvarlldlvglgeyathrpkeISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLL 201
Cdd:cd00267 76 GY-VPQ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|..
gi 1091083680 202 DvHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd00267 125 E-LAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
42-233 |
1.22e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.01 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT--GLDPR-VAIGFQEPRLLPWRTVA 118
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRdICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQ 197
Cdd:PRK11432 97 ENVGYGLKmLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1091083680 198 DLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK11432 177 EKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
47-185 |
1.33e-39 |
|
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: 135.08 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD---PRVAIG--FQEPRLLPWRTVADNV 121
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErksLRKEIGyvFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 122 ALGLP-QGTKKSEGAASVARLLDLVGLGEYATHR----PKEISGGMAQRVSLARALARNPGVLLLDEPF 185
Cdd:pfam00005 81 RLGLLlKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-231 |
2.79e-39 |
|
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: 143.75 E-value: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 8 TDVPTSEKNGRRAVSTAAVPLSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGT 87
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 88 VRIGEKAVTGLDP---RVAIGF--QEPRLLPWrTVADNVALGLPQGTKksegaASVARLLDLVGLGEYATHRPKEI---- 158
Cdd:COG4988 394 ILINGVDLSDLDPaswRRQIAWvpQNPYLFAG-TIRENLRLGRPDASD-----EELEAALEAAGLDEFVAALPDGLdtpl 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 159 -------SGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQdpTTILLVTHDvEEALYLSDRVIVL 231
Cdd:COG4988 468 geggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHR-LALLAQADRILVL 544
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-232 |
1.24e-38 |
|
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: 134.53 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP----RVA 103
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdyrrRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGFQEPRLLPWRTVADNVALgLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:COG4133 79 YLGHADGLKPELTVRENLRF-WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 184 PFGALDALTRINMQDLLLDvHRQDPTTILLVTHDveEALYLSDRVIVLG 232
Cdd:COG4133 158 PFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ--PLELAAARVLDLG 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-233 |
2.27e-38 |
|
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: 134.07 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-------- 101
Cdd:cd03292 3 FINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipylrrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEvTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHrQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
51-230 |
2.51e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.32 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 51 SFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVADNVALGLPQ 127
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 128 GTK-KSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQ 206
Cdd:PRK10771 99 GLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180
....*....|....*....|....
gi 1091083680 207 DPTTILLVTHDVEEALYLSDRVIV 230
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-233 |
2.96e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.45 E-value: 2.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVtgLDPRVAIG---- 105
Cdd:PRK09493 4 FKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERlirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 -----FQEPRLLPWRTVADNVALGLPQ--GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:PRK09493 78 eagmvFQQFYLFPHLTALENVMFGPLRvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 179 LLLDEPFGALDALTRIN----MQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK09493 158 MLFDEPTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-237 |
5.79e-38 |
|
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: 134.48 E-value: 5.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGekavtGLDP------- 100
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTldeenlw 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 ----RVAIGFQEP-RLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALAR 174
Cdd:TIGR04520 74 eirkKVGMVFQNPdNQFVGATVEDDVAFGLEnLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 175 NPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALyLSDRVIVL--GK----DTPE 237
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMnkGKivaeGTPR 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
28-233 |
1.27e-37 |
|
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: 132.02 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTgLDPRVAIGF- 106
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNRIGYl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 -QEPRLLPWRTVADN-VALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:cd03269 76 pEERGLYPKMKVIDQlVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNK 203
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
51-231 |
1.99e-37 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 131.52 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 51 SFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVADNVALGLPQ 127
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYqrpVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 128 GTK----KSEGAASVARLldlVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDV 203
Cdd:TIGR01277 98 GLKlnaeQQEKVVDAAQQ---VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180
....*....|....*....|....*...
gi 1091083680 204 HRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
41-231 |
6.48e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.25 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 41 GGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP----RVAIGF--QEPRLLPW 114
Cdd:cd03224 11 GKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPheraRAGIGYvpEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALGLpQGTKKSEGAASVARLLDLV-GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:cd03224 90 LTVEENLLLGA-YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1091083680 194 INMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03224 169 EEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVL 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-232 |
6.58e-37 |
|
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: 130.07 E-value: 6.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGF--QEP-RLL 112
Cdd:cd03226 6 SFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYvmQDVdYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVADNVALGLPQGTKKSEGAASVARLLDLVGLGEyaTHrPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDalt 192
Cdd:cd03226 85 FTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKE--RH-PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1091083680 193 RINMQ---DLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLG 232
Cdd:cd03226 159 YKNMErvgELIRELAAQG-KAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
47-231 |
1.37e-36 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 132.89 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR---VAIGFQEPRLLPWRTVADNVAL 123
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEkrgIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 124 GLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLD 202
Cdd:NF040840 96 GLKlRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180
....*....|....*....|....*....
gi 1091083680 203 VHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIM 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-245 |
2.81e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIG-----EKAVTGLDPRV 102
Cdd:PRK13635 6 IRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlsEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEP-RLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVAFGLEnIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYlSDRVIVLGKDTPEAPATIQRI 245
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
40-233 |
4.21e-36 |
|
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: 128.39 E-value: 4.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 40 PGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAV-TGLD---PRVAIGFQEPRLLPWR 115
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKaarQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:cd03263 91 TVREHLRFyARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 195 NMQDLLLDVHRQdpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03263 171 AIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSD 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-231 |
5.74e-36 |
|
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: 134.34 E-value: 5.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 6 AVTDVPTSEKNGRRAVSTA-AVPLSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRIT 84
Cdd:TIGR02857 299 AVLDAAPRPLAGKAPVTAApASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 85 AGTVRIGEKAVTGLDP-----RVAIGFQEPRLLPwRTVADNVALGLPQGTkksegAASVARLLDLVGLGEYATHRPK--- 156
Cdd:TIGR02857 376 EGSIAVNGVPLADADAdswrdQIAWVPQHPFLFA-GTIAENIRLARPDAS-----DAEIREALERAGLDEFVAALPQgld 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 157 --------EISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQdpTTILLVTHDvEEALYLSDRV 228
Cdd:TIGR02857 450 tpigeggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRI 526
|
...
gi 1091083680 229 IVL 231
Cdd:TIGR02857 527 VVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
41-231 |
8.61e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 127.79 E-value: 8.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 41 GGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--RVA--IGF--QEPRLLPW 114
Cdd:COG0410 14 GGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhrIARlgIGYvpEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALGLPQGTKKSEGAASVARLLDL--VgLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT 192
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 193 RINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG0410 172 VEEIFEIIRRLNREG-VTILLVEQNARFALEIADRAYVL 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
47-274 |
1.13e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.98 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG---------LDPRVAIGFQEPR-LLPWRT 116
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkklkpLRKKVGIVFQFPEhQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGlPQ--GTKKSEGAASVARLLDLVGLGE-YATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:PRK13634 103 VEKDICFG-PMnfGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 194 INMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVtvdrSHPRDRAD-----AEITALRSEL 268
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF----ADPDELEAigldlPETVKFKRAL 257
|
....*.
gi 1091083680 269 LAELGV 274
Cdd:PRK13634 258 EEKFGI 263
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-233 |
1.33e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.07 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTgLDPRVAIGF- 106
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDRRRIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 -QEPRLLPWRTVADN-VALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:COG4152 77 pEERGLYPKMKVGEQlVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDpTTILLVTHD---VEEalyLSDRVIVLGK 233
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQmelVEE---LCDRIVIINK 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
45-228 |
1.76e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 127.24 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRV-------AIGF--QEPRLLPWR 115
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelrnqKLGFiyQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALGLPQGTKKSEGAASVAR-LLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALeMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRV 228
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-232 |
2.87e-35 |
|
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: 132.97 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 3 LNSAVTDVPTSEKNGRRAVSTAAVPLSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNR 82
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 83 ITAGTVRIGEKAVTGLDP---RVAIGF--QEPRLLPwRTVADNVALGLPQGTKksegaASVARLLDLVGLGEYATHRPK- 156
Cdd:COG4987 387 PQSGSITLGGVDLRDLDEddlRRRIAVvpQRPHLFD-TTLRENLRLARPDATD-----EELWAALERVGLGDWLAALPDg 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 157 ----------EISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRinmQDLLLDVHRQDPT-TILLVTHDvEEALYLS 225
Cdd:COG4987 461 ldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEALAGrTVLLITHR-LAGLERM 536
|
....*..
gi 1091083680 226 DRVIVLG 232
Cdd:COG4987 537 DRILVLE 543
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-261 |
3.54e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.68 E-value: 3.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR------ 101
Cdd:COG1129 5 LEMRGISKSFG---GVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALGLPQGTK----KSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGglidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 178 VLLLDEPFGAL-----DALTRInMQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIVL--GKDTPEAPA---TIQRIVT 247
Cdd:COG1129 161 VLILDEPTASLterevERLFRI-IRRL-----KAQGVAIIYISHRLDEVFEIADRVTVLrdGRLVGTGPVaelTEDELVR 234
|
250 260
....*....|....*....|.
gi 1091083680 248 -------VDRSHPRDRADAEI 261
Cdd:COG1129 235 lmvgrelEDLFPKRAAAPGEV 255
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
42-231 |
4.97e-35 |
|
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: 125.56 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAV---TGLDPRVAIGFQEPRLLPWRTV 117
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVrepREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:cd03265 91 WENLYIhARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-231 |
9.84e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.44 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 6 AVTDVPTSEKNGRRAVSTAAVP--LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRI 83
Cdd:COG1132 316 ELLDEPPEIPDPPGAVPLPPVRgeIEFENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 84 TAGTVRIGEKAVTGLDP-----RVAIGFQEPRLLPwRTVADNVALGLPQGTKKS-EGAASVARLLDLV-----GLGEYAT 152
Cdd:COG1132 393 TSGRILIDGVDIRDLTLeslrrQIGVVPQDTFLFS-GTIRENIRYGRPDATDEEvEEAAKAAQAHEFIealpdGYDTVVG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 153 HRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDlLLDVHRQDPTTIlLVTHD---VEEAlylsDRVI 229
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTI-VIAHRlstIRNA----DRIL 545
|
..
gi 1091083680 230 VL 231
Cdd:COG1132 546 VL 547
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
42-231 |
2.34e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRI--------TAGTVRIGEKAV--TGLDP-----RVAIGF 106
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRC---LNRMndlipgarVEGEILLDGEDIydPDVDVvelrrRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEPRLLPWrTVADNVALGLP-QGTK-KSEGAASVARLLDLVG--------LGEYAThrpkEISGGMAQRVSLARALARNP 176
Cdd:COG1117 99 QKPNPFPK-SIYDNVAYGLRlHGIKsKSELDEIVEESLRKAAlwdevkdrLKKSAL----GLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 177 GVLLLDEPFGALD--ALTRInmQDLLLDVhRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1117 174 EVLLMDEPTSALDpiSTAKI--EELILEL-KKD-YTIVIVTHNMQQAARVSDYTAFF 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
28-233 |
1.72e-33 |
|
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: 121.17 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTGLDPRVAIG- 105
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIGa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 -FQEPRLLPWRTVADNV-ALGLPQGTKKSEgaasVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:cd03268 77 lIEAPGFYPNLTARENLrLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091083680 184 PFGALDALTRINMQDLLLDvHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03268 153 PTNGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
45-229 |
2.38e-33 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 121.28 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI--------GEKAVTGLDPRVAIGFQEPRLLPWRT 116
Cdd:TIGR02982 19 QVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVlgqelhgaSKKQLVQLRRRIGYIFQAHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNV--ALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:TIGR02982 99 ARQNVqmALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDvEEALYLSDRVI 229
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHD-NRILDVADRIL 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-231 |
2.58e-33 |
|
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: 127.11 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 18 RRAVSTAAVPLSFEGVGQSFPVPGG-------THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRiTAGTVRI 90
Cdd:COG4172 266 RPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 91 GEKAVTGLDP--------RVAIGFQEP--RLLPWRTVADNVALGL---PQGTKKSEGAASVARLLDLVGLGEYATHR-PK 156
Cdd:COG4172 345 DGQDLDGLSRralrplrrRMQVVFQDPfgSLSPRMTVGQIIAEGLrvhGPGLSAAERRARVAEALEEVGLDPAARHRyPH 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 157 EISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM 499
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
42-274 |
3.26e-33 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 122.88 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT----GLDPRVAIGFQEPRLLPWRTV 117
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVreprKVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:TIGR01188 84 RENLEMmGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 197 QDLLLDVHRQDpTTILLVTHDVEEALYLSDRV------IVLGKDTPEApatIQRIVTVDRSHPRDRADAEITALRSELLA 270
Cdd:TIGR01188 164 WDYIRALKEEG-VTILLTTHYMEEADKLCDRIaiidhgRIIAEGTPEE---LKRRLGKDTLESRPRDIQSLKVEVSMLIA 239
|
....
gi 1091083680 271 ELGV 274
Cdd:TIGR01188 240 ELGE 243
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-221 |
5.37e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 120.27 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 33 VGQsfpvpgGTHE--VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR--------- 101
Cdd:PRK10584 16 VGQ------GEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklrakh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:PRK10584 90 VGFVFQSFMLIPTLNALENVELpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEA 221
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
42-231 |
6.06e-33 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 119.64 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA-------IG--FQEPRLL 112
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAskfrrekLGylFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:TIGR03608 89 ENETVEENLDLGLKyKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 192 TRINMQDLLLDVHRQDpTTILLVTHDVEEAlYLSDRVIVL 231
Cdd:TIGR03608 169 NRDEVLDLLLELNDEG-KTIIIVTHDPEVA-KQADRVIEL 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
42-239 |
7.08e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT------------------GLDPRVA 103
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknqlrLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGFQEPRLLPWRTVADNVALGLPQ--GTKKSEGAASVARLLDLVGLGEYATHR-PKEISGGMAQRVSLARALARNPGVLL 180
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVMEAPIQvlGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 181 LDEPFGALDA-----LTRInMQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIVL--GKDTPEAP 239
Cdd:PRK10619 176 FDEPTSALDPelvgeVLRI-MQQL-----AEEGKTMVVVTHEMGFARHVSSHVIFLhqGKIEEEGA 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-231 |
3.62e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.41 E-value: 3.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPG-----GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR- 101
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 -------VAIGFQEP--RLLPWRTVADNVALGLPQGT--KKSEGAASVARLLDLVGLG-EYATHRPKEISGGMAQRVSLA 169
Cdd:PRK10419 84 rkafrrdIQMVFQDSisAVNPRKTVREIIREPLRHLLslDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 170 RALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-231 |
4.00e-32 |
|
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: 118.08 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAIGF 106
Cdd:cd03245 5 FRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPadlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 --QEPRLLpWRTVADNVALGLPQGTKksegaASVARLLDLVGLGEYATHRPK-----------EISGGMAQRVSLARALA 173
Cdd:cd03245 83 vpQDVTLF-YGTLRDNITLGAPLADD-----ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 174 RNPGVLLLDEPFGALD--ALTRI--NMQDLLldvhrqDPTTILLVTHDVeEALYLSDRVIVL 231
Cdd:cd03245 157 NDPPILLLDEPTSAMDmnSEERLkeRLRQLL------GDKTLIIITHRP-SLLDLVDRIIVM 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
42-244 |
1.01e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.91 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RVAIGFQEPRL-LPWr 115
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelarRRAVLPQHSSLaFPF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALA-------RNPGVLLLDEPFGA 187
Cdd:COG4559 91 TVEEVVALGRaPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 188 LDaltrINMQDLLLDVHRQ---DPTTILLVTHDVEEALYLSDRVIVL--GK----DTPEA---PATIQR 244
Cdd:COG4559 171 LD----LAHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLhqGRlvaqGTPEEvltDELLER 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-231 |
1.18e-31 |
|
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: 116.52 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpGGTHeVLRGVSFTAAPGeIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTGLDP-RVAIG 105
Cdd:cd03264 1 LQLENLTKRY---GKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKlRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 F--QEPRLLPWRTVADNVA-LGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:cd03264 76 YlpQEFGVYPNFTVREFLDyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 183 EPFGALDALTRINMQDLLLDVHRQdpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVL 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
42-231 |
2.14e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.02 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-RVAIgfqePRLLPWrTVADN 120
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPqRSEV----PDSLPL-TVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGL-----PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRIN 195
Cdd:NF040873 78 VAMGRwarrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1091083680 196 MQDLLLDVHRQDpTTILLVTHDVEEALyLSDRVIVL 231
Cdd:NF040873 158 IIALLAEEHARG-ATVVVVTHDLELVR-RADPCVLL 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-231 |
3.49e-31 |
|
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: 121.39 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRV---AI 104
Cdd:COG4618 331 LSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgrHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GF--QEPRLLPwRTVADNVA-----------------------LGLPQG--TKKSEGAASvarlldlvglgeyathrpke 157
Cdd:COG4618 409 GYlpQDVELFD-GTIAENIArfgdadpekvvaaaklagvhemiLRLPDGydTRIGEGGAR-------------------- 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 158 ISGGMAQRVSLARALARNPGVLLLDEPFGALD-----ALTRinmqdlLLDVHRQDPTTILLVTHDVeEALYLSDRVIVL 231
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaALAA------AIRALKARGATVVVITHRP-SLLAAVDKLLVL 539
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
42-255 |
4.39e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RVAIGFQEPRL-LPWr 115
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaelarRRAVLPQHSSLsFPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALAR------NPGVLLLDEPFGAL 188
Cdd:PRK13548 92 TVEEVVAMGRaPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 189 DALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL--GK----DTPEA---PATIQRI----VTVDRsHPRD 255
Cdd:PRK13548 172 DLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLhqGRlvadGTPAEvltPETLRRVygadVLVQP-HPET 250
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
46-233 |
5.50e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.06 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQEPRLL----------PWR 115
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLvfqdspsavnPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALGLPQGT--KKSEGAASVARLLDLVGL-GEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT 192
Cdd:TIGR02769 106 TVRQIIGEPLRHLTslDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 193 RINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
44-256 |
1.58e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 114.46 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-------------RVAIGFQEPR 110
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirqlrqHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 LLPWRTVADNVALG--LPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK11264 96 LFPHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 189 DAltriNMQDLLLDVHR---QDPTTILLVTHDVEEALYLSDRVIVL--GKDTPEAPAtiqRIVTVDRSHPRDR 256
Cdd:PRK11264 176 DP----ELVGEVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFMdqGRIVEQGPA---KALFADPQQPRTR 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
46-231 |
1.94e-30 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 112.14 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA----IGF-QEPR----LLPWRT 116
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragIAYvPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGlpqgtkksegaasvaRLLdlvglgeyathrpkeiSGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:cd03215 95 VAENIALS---------------SLL----------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03215 144 YRLIREL-ADAGKAVLLISSELDELLGLCDRILVM 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
31-233 |
2.15e-30 |
|
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: 113.23 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 31 EGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTglDPRVA---IGF 106
Cdd:cd03266 5 DALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVK--EPAEArrrLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 --QEPRLLPWRTVADNVA-LGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:cd03266 83 vsDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091083680 184 PFGALDALTRINMQDLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03266 163 PTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
47-231 |
2.67e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.06 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD---------PRVAIGFQEPRLLPWRTV 117
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:PRK10070 124 LDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-231 |
3.95e-30 |
|
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: 112.63 E-value: 3.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPG------------------GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVR 89
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 90 IGEKAVTGLDprVAIGFQePRLlpwrTVADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSL 168
Cdd:cd03220 81 VRGRVSSLLG--LGGGFN-PEL----TGRENIYLnGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 169 ARALARNPGVLLLDEPFGALDALTRINMQDLLLDvHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
42-233 |
9.80e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 9.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIG-----------EKAVTGLDPRVAIGFQEPR 110
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsqkpsEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 LLPWRTVADNV------ALGLPqgtkKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:COG4161 93 LWPHLTVMENLieapckVLGLS----KEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 185 FGALDAltRINMQ--DLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:COG4161 169 TAALDP--EITAQvvEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEK 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
50-245 |
3.32e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 113.28 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-------GEKAVTgLDP---RVAIGFQEPRLLPWRTVAD 119
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdSRKGIF-LPPekrRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPQgTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDL 199
Cdd:TIGR02142 95 NLRYGMKR-ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1091083680 200 LLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRI 245
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
28-229 |
4.33e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.98 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP------- 100
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 RVAIGF--QEPRLLPWRTVADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:PRK10535 85 REHFGFifQRYHLLSHLTAAQNVEVpAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVhRQDPTTILLVTHDVEEALYlSDRVI 229
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVI 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-231 |
4.74e-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: 108.46 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAI 104
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPnelGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GF--QEPRLLPwRTVADNValglpqgtkksegaasvarlldlvglgeyathrpkeISGGMAQRVSLARALARNPGVLLLD 182
Cdd:cd03246 79 GYlpQDDELFS-GSIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 183 EPFGALDALTRINMQDLLLDVhRQDPTTILLVTHDvEEALYLSDRVIVL 231
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHR-PETLASADRILVL 168
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-233 |
9.18e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.66 E-value: 9.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL--------NRITAGTVRIGEKAVTGLD 99
Cdd:PRK13640 6 VEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 PRVAIGFQEP-RLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGATVGDDVAFGLEnRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALyLSDRVIVLGK 233
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDD 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-231 |
1.94e-28 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 113.63 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKS----TLLRAAAGLNRITAGTVRIGEKAVTGLDP--- 100
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSErel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 ------RVAIGFQEP--RLLPWRTVADNVA--LGLPQGTKKSEGAASVARLLDLVG-------LGEYathrPKEISGGMA 163
Cdd:COG4172 87 rrirgnRIAMIFQEPmtSLNPLHTIGKQIAevLRLHRGLSGAAARARALELLERVGipdperrLDAY----PHQLSGGQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 164 QRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHD---VEEalyLSDRVIVL 231
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVM 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
42-231 |
9.06e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 9.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RVAIGFQEPRLLPwRT 116
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrqQVSYCAQTPTLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNvaLGLP-QGTKKSEGAASVARLLDLVGLGEYATHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK10247 97 VYDN--LIFPwQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDVEEALYlSDRVIVL 231
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-233 |
2.01e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 105.73 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV--------RIGEKAVTGLD 99
Cdd:PRK10908 2 IRFEHVSKAYL---GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 PRVAIGFQEPRLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVG-VTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
43-241 |
2.14e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.12 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 43 THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG---LDPRVAIG--FQEP-RLLPWRT 116
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvWDIRHKIGmvFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRIN 195
Cdd:PRK13650 99 VEDDVAFGLEnKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1091083680 196 MQDLLLDVHRQDPTTILLVTHDVEEaLYLSDRVIVLGKDTPEAPAT 241
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTST 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-231 |
2.36e-27 |
|
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: 103.66 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIgfq 107
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 eprllpwrtvadnvALGLpqgtkksegaASVARLldlvglgeyathrpkeiSGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:cd03216 74 --------------RAGI----------AMVYQL-----------------SVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 188 LDALTRINMQDLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03216 113 LTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
29-233 |
3.53e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.23 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 29 SFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAV-----TGLDPRVA 103
Cdd:PRK13632 9 KVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskenlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGFQEP-RLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:PRK13632 87 IIFQNPdNQFIGATVEDDIAFGLEnKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALyLSDRVIVLGK 233
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSE 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
42-233 |
3.67e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-----------GEKAVTGLDPRVAIGFQEPR 110
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 LLPWRTVADNV------ALGLpqgtKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:PRK11124 93 LWPHLTVQQNLieapcrVLGL----SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 185 FGALDAltRINMQ--DLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK11124 169 TAALDP--EITAQivSIIREL-AETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
47-233 |
4.19e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.29 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG-------LDPRVAIGFQEPRL-LPWRTVA 118
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklsdIRKKVGLVFQYPEYqLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGlPQ--GTKKSEGAASVARLLDLVGLG--EYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK13637 103 KDIAFG-PInlGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
44-233 |
5.45e-27 |
|
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: 104.48 E-value: 5.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-----VAIGFQEPRLLPwRTVA 118
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylhskVSLVGQEPVLFA-RSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGLPQ-GTKKSEGAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT 192
Cdd:cd03248 106 DNIAYGLQScSFECVKEAAQKAHAHSFIselasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 193 RINMQDLLLDVHRQdpTTILLVTH---DVEEAlylsDRVIVLGK 233
Cdd:cd03248 186 EQQVQQALYDWPER--RTVLVIAHrlsTVERA----DQILVLDG 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-233 |
5.74e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.97 E-value: 5.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSF-PVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG--------- 97
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 98 LDPRVAIGFQEPR-LLPWRTVADNVALGlPQ--GTKKSEGAASVARLLDLVGLG-EYATHRPKEISGGMAQRVSLARALA 173
Cdd:PRK13643 82 VRKKVGVVFQFPEsQLFEETVLKDVAFG-PQnfGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 174 RNPGVLLLDEPFGALDALTRINMQDLLLDVHrQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
45-233 |
8.26e-27 |
|
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: 104.34 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekaVTGLDP---------RVAIGFQEPRLLPWR 115
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPwkrrkkflrRIGVVFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 -TVADNVAL-----GLPqgtkKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALD 189
Cdd:cd03267 110 lPVIDSFYLlaaiyDLP----PARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 190 ALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
42-231 |
1.15e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.40 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAG-TVRI-GEK--AVTGLDPRVAIGFQEPRL---LPW 114
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGERrgGEDVWELRKRIGLVSPALqlrFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVAL-------GLPQGTKKSEgAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:COG1119 94 DETVLDVVLsgffdsiGLYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 188 LDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
46-231 |
1.32e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGL-DPRVA--IG--FQEPRL--LPWRTVA 118
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKRAkyIGrvFQDPMMgtAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVAL--------GLPQGTKKSEGAASVARL--LDLvGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:COG1101 101 ENLALayrrgkrrGLRRGLTKKRRELFRELLatLGL-GLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 189 D--------ALT-RInmqdllldVHRQDPTTiLLVTHDVEEALYLSDRVIVL 231
Cdd:COG1101 180 DpktaalvlELTeKI--------VEENNLTT-LMVTHNMEQALDYGNRLIMM 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
47-233 |
1.48e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.82 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--------RVAIGFQEP--RLLPWRT 116
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqkllrqKIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGLPQGTK--KSEGAASVARLLDLVGL-GEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:PRK11308 111 VGQILEEPLLINTSlsAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1091083680 194 INMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIV--LGK 233
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVmyLGR 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
42-227 |
1.68e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRI--------TAGTVRIGEKAVTG-----LDPRVAIG--F 106
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRS---INRMndlnpevtITGSIVYNGHNIYSprtdtVDLRKEIGmvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEPRLLPWrTVADNVALGLP-QGTK-KSEGAASVARLLDLVGLGEYATHRPKE----ISGGMAQRVSLARALARNPGVLL 180
Cdd:PRK14239 93 QQPNPFPM-SIYENVVYGLRlKGIKdKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTHDVEEALYLSDR 227
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
28-231 |
3.55e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.85 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPV------------------PGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVR 89
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 90 IGEKAVTGLDprVAIGFQePRLlpwrTVADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYAtHRP-KEISGGMAQRVS 167
Cdd:COG1134 85 VNGRVSALLE--LGAGFH-PEL----TGRENIYLnGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQPvKTYSSGMRARLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 168 LARALARNPGVLLLDEPFGALDA------LTRinMQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAafqkkcLAR--IREL-----RESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
36-233 |
4.05e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.62 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GE------KAVTGLDPRVAIGFQE 108
Cdd:PRK13639 8 KYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEpikydkKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 109 PR---LLPwrTVADNVALG-LPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:PRK13639 87 PDdqlFAP--TVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-233 |
4.77e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 102.31 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAIGF--QEPRLLPwRTVAD 119
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdslRRAIGVvpQDTVLFN-DTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPQGTKKS-EGAASVARLLDLV-GLGE-YAT---HRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:cd03253 94 NIRYGRPDATDEEvIEAAKAAQIHDKImRFPDgYDTivgERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 194 INMQDLLLDVhRQDPTTIlLVTHDVEEaLYLSDRVIVLGK 233
Cdd:cd03253 174 REIQAALRDV-SKGRTTI-VIAHRLST-IVNADKIIVLKD 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
35-231 |
5.13e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.40 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 35 QSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR--------VAIGF 106
Cdd:PRK15079 25 QWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewravrsdIQMIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEP--RLLPWRTVADNVALGL----PQgTKKSEGAASVARLLDLVGLGEYATHR-PKEISGGMAQRVSLARALARNPGVL 179
Cdd:PRK15079 105 QDPlaSLNPRMTIGEIIAEPLrtyhPK-LSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 180 LLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
36-235 |
5.29e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-----RIGEKAVTGLDPRVAIGFQEP- 109
Cdd:PRK13648 14 SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLRKHIGIVFQNPd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 110 RLLPWRTVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK13648 94 NQFVGSIVKYDVAFGLEnHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091083680 189 DALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYlSDRVIVLGKDT 235
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGT 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
45-231 |
6.66e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.61 E-value: 6.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTG-------------------LDPRVAI 104
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILInGHKLEYGdykyrckhirmifqdpntsLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 G--FQEPRLLpwrtvadNVALGLPQGTKKsegaasVARLLDLVGL-GEYATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:COG4167 107 GqiLEEPLRL-------NTDLTAEEREER------IFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVM 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
47-231 |
6.70e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA----IG--FQEPRLLPWRTVADN 120
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAialgIGmvHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLPQG----TKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL-----DAL 191
Cdd:COG3845 101 IVLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqeaDEL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 192 TRInMQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG3845 181 FEI-LRRL-----AAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
38-231 |
6.84e-26 |
|
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: 101.01 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 38 PVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGekavtgldPRVAIGFQEPRLLPwRTV 117
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------GSIAYVSQEPWIQN-GTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLPQGTKKSEGAASVARLL---------DLVGLGEyathrpKEI--SGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:cd03250 83 RENILFGKPFDEERYEKVIKACALEpdleilpdgDLTEIGE------KGInlSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091083680 187 ALDALT--RInMQDLLLDvHRQDPTTILLVTHDVeEALYLSDRVIVL 231
Cdd:cd03250 157 AVDAHVgrHI-FENCILG-LLLNNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-231 |
7.08e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.03 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLdP-----RV 102
Cdd:COG1137 4 LEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PmhkraRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGF--QEP---RLLpwrTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNP 176
Cdd:COG1137 79 GIGYlpQEAsifRKL---TVEDNILAVLeLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 177 GVLLLDEPFGALDALTRINMQDLLLDVHRQDpttI-LLVT-HDVEEALYLSDRVIVL 231
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERG---IgVLITdHNVRETLGICDRAYII 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
30-228 |
8.45e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIgekavtglDPRVAIGF--Q 107
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLRIGYlpQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLPWRTVADNVALGLP-----------------------------QGTKKSEGA----ASVARLLDLVGLGEYATHR 154
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAelraleaeleeleaklaepdedlerlaelQEEFEALGGweaeARAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 155 P-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLldvhRQDPTTILLVTHDVeealYLSDRV 228
Cdd:COG0488 149 PvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDR----YFLDRV 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-234 |
9.00e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.76 E-value: 9.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT------GLDPR 101
Cdd:PRK11288 5 LSFDGIGKTFP---GV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALG-LPQG---TKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPG 177
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGqLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 178 VLLLDEPFGALDA-----LTRInMQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIVLgKD 234
Cdd:PRK11288 161 VIAFDEPTSSLSAreieqLFRV-IREL-----RAEGRVILYVSHRMEEIFALCDAITVF-KD 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-231 |
1.12e-25 |
|
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: 101.19 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNR---ITAGTVRIGEKAvtgLDP---- 100
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQP---RKPdqfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 101 -RVAIGFQEPRLLPWRTVADNVA----LGLPQGTKKSEGAASVA-RLLDLVGLGEYATHRPKEISGGMAQRVSLARALAR 174
Cdd:cd03234 81 kCVAYVRQDDILLPGLTVRETLTytaiLRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 175 NPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLL 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-233 |
1.43e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.46 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRI--------TAGTVRIGEKAVTG--LDP-----RVAIGF 106
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRT---FNRLlelneearVEGEVRLFGRNIYSpdVDPievrrEVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEPRLLPWRTVADNVALGLP-QGTKKSEG--------AASVARLLDLVG--LGEYathrPKEISGGMAQRVSLARALARN 175
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKlNGLVKSKKeldervewALKKAALWDEVKdrLNDY----PSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 176 PGVLLLDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTHDVEEALYLSDRV--IVLGK 233
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVafLYLGK 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-256 |
4.36e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.17 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 37 FPVPGG-----THEV--LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-------- 101
Cdd:PRK10261 323 FPLRSGllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrd 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEP--RLLPWRTVADNV-----ALGLPQGtkkSEGAASVARLLDLVGL-GEYATHRPKEISGGMAQRVSLARALA 173
Cdd:PRK10261 403 IQFIFQDPyaSLDPRQTVGDSImeplrVHGLLPG---KAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 174 RNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIV--LGKDTPEAPatiQRIVTVDRS 251
Cdd:PRK10261 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVmyLGQIVEIGP---RRAVFENPQ 556
|
....*
gi 1091083680 252 HPRDR 256
Cdd:PRK10261 557 HPYTR 561
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-233 |
5.71e-25 |
|
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: 99.54 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPV-PGgtHEVLRGVSFTAAPGEIISVIGSSGCGKST----LLRaaagLNRITAGTVRIGEKAVTGLDP---R 101
Cdd:cd03249 3 FKNVSFRYPSrPD--VPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLER----FYDPTSGEILLDGVDIRDLNLrwlR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGF--QEPRLLPwRTVADNVALGLPQGTKKS-EGAASVARLLDLV-GLGE-YATH---RPKEISGGMAQRVSLARALA 173
Cdd:cd03249 77 SQIGLvsQEPVLFD-GTIAENIRYGKPDATDEEvEEAAKKANIHDFImSLPDgYDTLvgeRGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 174 RNPGVLLLDEPFGALDALTRINMQDLLLDVHRQdpTTILLVTHDveealyLS-----DRVIVLGK 233
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAHR------LStirnaDLIAVLQN 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
47-231 |
1.07e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGE----------KAVTGLDPRVAIGFQEPRL-LPWR 115
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVKRLRKEIGLVFQFPEYqLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALG-LPQGTKKSEGAASVARLLDLVGLG-EYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:PRK13645 107 TIEKDIAFGpVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1091083680 194 INMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
40-238 |
1.20e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 40 PGGTHEV--LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI---------GEKAVTGLDPRVAIGFQE 108
Cdd:PRK13641 14 PGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetGNKNLKKLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 109 PRL-LPWRTVADNVALGlPQGTKKSEGAASVARL--LDLVGLGE-YATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:PRK13641 94 PEAqLFENTVLKDVEFG-PKNFGFSEDEAKEKALkwLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDPTTIlLVTHDVEEALYLSDRVIVL--GK----DTPEA 238
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVI-LVTHNMDDVAEYADDVLVLehGKlikhASPKE 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
42-260 |
1.43e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.09 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRI-----TAGTVRIGEKAV--TGLDP-----RVAIGFQEP 109
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPvevrrRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 110 RLLPwRTVADNVALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKE----ISGGMAQRVSLARALARNPGVLLLDEPF 185
Cdd:PRK14243 101 NPFP-KSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 186 GALDALTRINMQDLLLDVHRQdpTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVTVDRS-----HPRDRADAE 260
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTekifnSPQQQATRD 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-231 |
1.50e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 18 RRAVSTAAVPLSFEGVGqsfpvpggTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG 97
Cdd:COG1129 247 KRAAAPGEVVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 98 LDPRVAI--GF---QEPR----LLPWRTVADNVAL---------GLPQGTKKSEGAASVARLLDLVglgeyaTHRP---- 155
Cdd:COG1129 319 RSPRDAIraGIayvPEDRkgegLVLDLSIRENITLasldrlsrgGLLDRRRERALAEEYIKRLRIK------TPSPeqpv 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 156 KEISGGMAQRVSLARALARNPGVLLLDEPF-----GALDALTRInMQDLlldvhRQDPTTILLVTHDVEEALYLSDRVIV 230
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTrgidvGAKAEIYRL-IREL-----AAEGKAVIVISSELPELLGLSDRILV 466
|
.
gi 1091083680 231 L 231
Cdd:COG1129 467 M 467
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
42-231 |
1.51e-24 |
|
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: 98.38 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP----RVAIGF--QEPRLLPWR 115
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkraRLGIGYlpQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:cd03218 91 TVEENILAVLEiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 195 NMQDLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03218 171 DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYII 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
42-249 |
1.56e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRvaigfQEPR---LLPWR--- 115
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR-----QLARrlaLLPQHhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 ----TVADNVALG----LPQ-GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:PRK11231 88 pegiTVRELVAYGrspwLSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 187 ALDaltrINMQDLLLDVHR---QDPTTILLVTHDVEEALYLSDRVIVL------GKDTPE---APATIQRIVTVD 249
Cdd:PRK11231 168 YLD----INHQVELMRLMRelnTQGKTVVTVLHDLNQASRYCDHLVVLanghvmAQGTPEevmTPGLLRTVFDVE 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-226 |
2.10e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 43 THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRITA--GTVRIGEKA-------------VTGLDPRVAIGFQ 107
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC---LNRMNEleSEVRVEGRVeffnqniyerrvnLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLPwRTVADNVALGL------PQGTKKS--EGAASVARLLDLVglgEYATHRPK-EISGGMAQRVSLARALARNPGV 178
Cdd:PRK14258 96 KPNLFP-MSVYDNVAYGVkivgwrPKLEIDDivESALKDADLWDEI---KHKIHKSAlDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSD 226
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
49-254 |
2.30e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 49 GVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLdPRVAIG-------FQEPRLLPWRTVADN- 120
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIArmgvvrtFQHVRLFREMTVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 -VA-------------LGLPqGTKKSEGAA--SVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:PRK11300 102 lVAqhqqlktglfsglLKTP-AFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIvtvdRSHPR 254
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI----RNNPD 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
46-231 |
2.82e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.00 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-----------RIGE------------------KAVT 96
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEkekvleklviqktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 97 GLDPRVAIGFQ--EPRLLPwRTVADNVALG-LPQGTKKSEGAASVARLLDLVGLGE-YATHRPKEISGGMAQRVSLARAL 172
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFE-QTIEKDIIFGpVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 173 ARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVLEWTKRTIFF 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
36-231 |
3.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.27 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG-----LDPRVAIGFQEPR 110
Cdd:PRK13647 11 HFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwVRSKVGLVFQDPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 -LLPWRTVADNVALG-LPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK13647 90 dQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1091083680 189 DALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQG-KTVIVATHDVDLAAEWADQVIVL 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-233 |
4.26e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRI--------TAGTVRIGEKAVTGLD-----PRVAIGFQE 108
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRV---FNRLielypearVSGEVYLDGQDIFKMDvielrRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 109 PRLLPWRTVADNVALGLPQG---TKKSEGAASVARLLDLVGLGEYATHR----PKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNrlvKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQdpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYK 220
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
49-231 |
5.53e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 96.67 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 49 GVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL----NRITAGTVRIGEKAVTGLDPR---VAIGFQEPR--LLPWRTVAD 119
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRgrhIATIMQNPRtaFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPQGTKKSEGA-ASVARLLDLVGLGEYAT---HRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRIN 195
Cdd:TIGR02770 84 HAIETLRSLGKLSKQArALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1091083680 196 MQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVM 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-231 |
5.75e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 27 PLSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP----RV 102
Cdd:PRK13537 7 PIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARharqRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPRLLPWRTVADNV-ALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVI 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
36-231 |
8.81e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.26 E-value: 8.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL---NRITAGTVRIGEKAVTGLDPR---------VA 103
Cdd:PRK09473 21 TFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKelnklraeqIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGFQEP--RLLPWRTVADNVA--LGLPQGTKKSEGAASVARLLDLVGLGEyATHR----PKEISGGMAQRVSLARALARN 175
Cdd:PRK09473 101 MIFQDPmtSLNPYMRVGEQLMevLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKRmkmyPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 176 PGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
46-233 |
9.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.00 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGE---------------------KAVTGLDPRVAI 104
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpyskkiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWR-TVADNVALG-LPQGTKKSEGAASVARLLDLVGLGE-YATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:PRK13631 121 VFQFPEYQLFKdTIEKDIMFGpVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKANN-KTVFVITHTMEHVLEVADEVIVMDK 251
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
47-231 |
9.76e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 9.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKA----VTGLDPRVAIGFQEP-RLLPWRTVADN 120
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLP-QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDL 199
Cdd:PRK13642 103 VAFGMEnQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|..
gi 1091083680 200 LLDVHRQDPTTILLVTHDVEEALYlSDRVIVL 231
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVM 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-233 |
1.10e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 94.93 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTH--EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNR--ITAGTVRIGEKAVTGLDPRVA 103
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGF--QEPRLLPWRTVADNVALglpqgtkksegaasVARLldlvglgeyathrpKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:cd03213 84 IGYvpQDDILHPTLTVRETLMF--------------AAKL--------------RGLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVhRQDPTTILLVTHDV-EEALYLSDRVIVLGK 233
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQ 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
46-231 |
1.20e-23 |
|
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: 95.58 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI----GEKAVTGLDPRV-------AIGF--QEPRLL 112
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREilalrrrTIGYvsQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVADNVALGL-PQGTKKSEGAASVARLLDLVGLGEyathR-----PKEISGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:COG4778 106 PRVSALDVVAEPLlERGVDREEARARARELLARLNLPE----RlwdlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1091083680 187 ALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG4778 182 SLDAANRAVVVELIEEAKARG-TAIIGIFHDEEVREAVADRVVDV 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-217 |
1.62e-23 |
|
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: 99.36 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 20 AVSTAAVPLSFEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD 99
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 P---RVAIGF--QEPRLLPwRTVADNVALGLPQGTKksegaASVARLLDLVGLGEYATHRP-----------KEISGGMA 163
Cdd:TIGR02868 404 QdevRRRVSVcaQDAHLFD-TTVRENLRLARPDATD-----EELWAALERVGLADWLRALPdgldtvlgeggARLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 164 QRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTHD 217
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-231 |
1.74e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLraaAGLNRI---TAGTVRI-GE--KAVTGLDPRVA 103
Cdd:PRK13657 337 FDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRVfdpQSGRILIdGTdiRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IG--FQEPRLLPwRTVADNVALGLPQGTKKS-EGAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARN 175
Cdd:PRK13657 411 IAvvFQDAGLFN-RSIEDNIRVGRPDATDEEmRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 176 PGVLLLDEPFGALDALTRINMQDlLLDVHRQDPTTiLLVTH---DVEEAlylsDRVIVL 231
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKA-ALDELMKGRTT-FIIAHrlsTVRNA----DRILVF 542
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
47-233 |
2.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.35 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG---------LDPRVAIGFQEPR-LLPWRT 116
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdikqIRKKVGLVFQFPEsQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGlPQ--GTKKSEGAASVARLLDLVGLGEYATHR-PKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTR 193
Cdd:PRK13649 103 VLKDVAFG-PQnfGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 194 INMQDLLLDVHrQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13649 182 KELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
36-233 |
2.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIgeKAVTGLDPR--------VAIGFQ 107
Cdd:PRK13644 8 SYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSklqgirklVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRL-LPWRTVADNVALG-----LPqgtkKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLL 181
Cdd:PRK13644 85 NPETqFVGRTVEEDLAFGpenlcLP----PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEaLYLSDRVIVLGK 233
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKG-KTIVYITHNLEE-LHDADRIIVMDR 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-217 |
2.69e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 26 VPLSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKavtgldprVAIG 105
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 106 F--QEPRLL-PWRTVADNVALGLPQGTKKSegaasvARllDLVGL----GEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:COG0488 382 YfdQHQEELdPDKTVLDELRDGAPGGTEQE------VR--GYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVhrqdPTTILLVTHD 217
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDF----PGTVLLVSHD 488
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
45-216 |
3.10e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.17 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGFQEPR--LLPWRTVADNVA 122
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 123 -----LGlpqgtkksEGAASVARLLDLVGLGEyATHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTrinm 196
Cdd:PRK13539 96 fwaafLG--------GEELDIAAALEAVGLAP-LAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA---- 162
|
170 180
....*....|....*....|...
gi 1091083680 197 QDLLLDV---HRQDPTTILLVTH 216
Cdd:PRK13539 163 VALFAELiraHLAQGGIVIAATH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-245 |
3.82e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 18 RRAVSTAAVPLSFEGVgqSFPVPGGtHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG 97
Cdd:COG3845 248 KAPAEPGEVVLEVENL--SVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 98 LDPRVA----IGF--QEPR---LLPWRTVADNVALGLPQGTKKSEGAasvarLLDLVGLGEYATH-------RPKEI--- 158
Cdd:COG3845 325 LSPRERrrlgVAYipEDRLgrgLVPDMSVAENLILGRYRRPPFSRGG-----FLDRKAIRAFAEElieefdvRTPGPdtp 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 159 ----SGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDvHRQDPTTILLVTHDVEEALYLSDRVIVL--G 232
Cdd:COG3845 400 arslSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMyeG 478
|
250
....*....|....*.
gi 1091083680 233 KDTPEAP---ATIQRI 245
Cdd:COG3845 479 RIVGEVPaaeATREEI 494
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-231 |
4.45e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 13 SEKNGRRAVSTAAVPLSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGE 92
Cdd:PRK13536 27 SEAKASIPGSMSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 93 KAVTGLD--PRVAIGF--QEPRLLPWRTVADN-VALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVS 167
Cdd:PRK13536 103 VPVPARArlARARIGVvpQFDNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 168 LARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVL 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
42-234 |
4.50e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RVAIGFQEP----RLl 112
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakRLAILRQENhinsRL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 pwrTVADNVALG-LP--QGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALD 189
Cdd:COG4604 91 ---TVRELVAFGrFPysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1091083680 190 ALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLgKD 234
Cdd:COG4604 168 MKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM-KD 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
49-228 |
7.62e-23 |
|
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: 97.57 E-value: 7.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 49 GVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGT--VRIGEKAVTGLDPRVA--------IGF--QEPRLLPWRT 116
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDgrgrakryIGIlhQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADN----VALGLPqgtkKSEGAASVARLLDLVGLGE-YATH----RPKEISGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:TIGR03269 382 VLDNlteaIGLELP----DELARMKAVITLKMVGFDEeKAEEildkYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 188 LDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRV 228
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRA 498
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
44-231 |
2.86e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.77 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLnrITAGTV-------------RIGEKAVTGLDPRVAIG--FQE 108
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSagshiellgrtvqREGRLARDIRKSRANTGyiFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 109 PRLLPWRTVADNVALGLPQGT-------------KKSEGAASVARlldlVGLGEYATHRPKEISGGMAQRVSLARALARN 175
Cdd:PRK09984 95 FNLVNRLSVLENVLIGALGSTpfwrtcfswftreQKQRALQALTR----VGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 176 PGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-231 |
2.91e-22 |
|
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: 91.90 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFpvpGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD-----PRVAI 104
Cdd:cd03254 5 FENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPwRTVADNVALGLPQGTKKSE-GAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:cd03254 82 VLQDTFLFS-GTIMENIRLGRPNATDEEViEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTHDVEEALYlSDRVIVL 231
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKN-ADKILVL 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-234 |
3.92e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 11 PTSEKNGRRAVSTAAVPLSFEGVGQSFP----VPggtheVLRGVSFTAAPGEIISVIGSSGCGKSTLlraAAGLNRI--- 83
Cdd:TIGR00958 462 PNIPLTGTLAPLNLEGLIEFQDVSFSYPnrpdVP-----VLKGLTFTLHPGEVVALVGPSGSGKSTV---AALLQNLyqp 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 84 TAGTVRIGEKAVTGLDPR-----VAIGFQEPRLLPwRTVADNVALGLPQGTKKSEGAASV-ARLLDLVG---------LG 148
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHylhrqVALVGQEPVLFS-GSVRENIAYGLTDTPDEEIMAAAKaANAHDFIMefpngydteVG 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 149 EYATHRpkeiSGGMAQRVSLARALARNPGVLLLDEPFGALDAltriNMQDLLLDVHRQDPTTILLVTHD---VEEAlyls 225
Cdd:TIGR00958 613 EKGSQL----SGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRlstVERA---- 680
|
....*....
gi 1091083680 226 DRVIVLGKD 234
Cdd:TIGR00958 681 DQILVLKKG 689
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
46-233 |
9.50e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.69 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI------GEKAVTGLDPRVAIGFQEP-RLLPWRTVA 118
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsDEENLWDIRNKAGMVFQNPdNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGlPQ--GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:PRK13633 105 EDVAFG-PEnlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYlSDRVIVLGK 233
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
42-249 |
1.27e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-----VAIGFQEPRLLPWR- 115
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevrkfVGLVFQNPDDQIFSp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALG-LPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK13652 95 TVEQDIAFGpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVTVD 249
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-233 |
2.35e-21 |
|
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: 93.33 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLN--RITAGTV-----------------RIGEK-AVTG------- 97
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpsKVGEPcPVCGgtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 98 -------------LDPRVAIGFQEP-RLLPWRTVADNVALGLPQ-GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGM 162
Cdd:TIGR03269 94 vdfwnlsdklrrrIRKRIAIMLQRTfALYGDDTVLDNVLEALEEiGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 163 AQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-236 |
2.93e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 2 TLNSAVTDVPTSEKNGRRAVSTAAVPLSFEGVgqSFPVPGGtHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLN 81
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEDGALALEDL--TLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 82 RITAGTVRIGEKAVTGLDPrvaigfQEPRlLPWRTVADnvALGLPQGTKKSEGAAsVARLLDLVGLGEYATH------RP 155
Cdd:COG4178 414 PYGSGRIARPAGARVLFLP------QRPY-LPLGTLRE--ALLYPATAEAFSDAE-LREALEAVGLGHLAERldeeadWD 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 156 KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDvhRQDPTTILLVTHDVEEALYlSDRVIVLGKDT 235
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAF-HDRVLELTGDG 560
|
.
gi 1091083680 236 P 236
Cdd:COG4178 561 S 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-233 |
2.98e-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: 89.47 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RV 102
Cdd:cd03252 1 ITFEHV--RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawlrrQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPRLLPwRTVADNVALGLP-QGTKKSEGAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNP 176
Cdd:cd03252 79 GVVLQENVLFN-RSIRDNIALADPgMSMERVIEAAKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 177 GVLLLDEPFGALD-----ALTRiNMQDLLldvhrqDPTTILLVTHDVeEALYLSDRVIVLGK 233
Cdd:cd03252 158 RILIFDEATSALDyesehAIMR-NMHDIC------AGRTVIIIAHRL-STVKNADRIIVMEK 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
50-231 |
5.51e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.57 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGL----NRITAGTV--------RIGEKA---VTGLDprVAIGFQEP--RLL 112
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLefngqdlqRISEKErrnLVGAE--VAMIFQDPmtSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVADNV--ALGLPQGTKKSEGAASVARLLDLVGLGEYATH---RPKEISGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:PRK11022 104 PCYTVGFQImeAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 188 LDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
57-219 |
1.50e-20 |
|
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: 87.39 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 57 GEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-----RIGEKAVTGLDPR----VAIGFQEPRLLPwRTVADNVALGLP- 126
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRnrysVAYAAQKPWLLN-ATVEENITFGSPf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 127 --QGTKKSEGAASVARLLDLVGLGEYAT--HRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDA-LTRINMQDLLL 201
Cdd:cd03290 106 nkQRYKAVTDACSLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGIL 185
|
170
....*....|....*...
gi 1091083680 202 DVHRQDPTTILLVTHDVE 219
Cdd:cd03290 186 KFLQDDKRTLVLVTHKLQ 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
42-226 |
2.03e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.90 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD--------PRVAIGFQEPRLLP 113
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlytvrKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 114 WRTVADNVALGLPQGTKKSEGA--ASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLlhSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 192 TRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSD 226
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-231 |
2.08e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG------LDPR 101
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALGlpqG--TKKSEGAASVARLLDLVG-LGEYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG---GffAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
43-276 |
2.19e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.61 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 43 THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekaVTGLDP---RVA----IGF---QEPRL- 111
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPfkrRKEfarrIGVvfgQRSQLw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 112 --LPwrtVADNVAL-----GLPqgtkKSEGAASVARLLDLVGLGEYAtHRP-KEISGGmaQRV--SLARALARNPGVLLL 181
Cdd:COG4586 109 wdLP---AIDSFRLlkaiyRIP----DAEYKKRLDELVELLDLGELL-DTPvRQLSLG--QRMrcELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 182 DEPFGALDALTRINMQDLLLDVHRQDPTTILLVTH---DVEEalyLSDRVIVLGK------------------------- 233
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHdmdDIEA---LCDRVIVIDHgriiydgsleelkerfgpyktivle 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1091083680 234 -DTPEAPATIQRIVTVDRSHPRD-----RADAEITALRSELLAELGVED 276
Cdd:COG4586 256 lAEPVPPLELPRGGEVIEREGNRvrlevDPRESLAEVLARLLARYPVRD 304
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
43-236 |
4.37e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.17 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 43 THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAG--LNRITAGTVRIgekavtgldPRVAIGfQEprllpwRTVADN 120
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV---------PDNQFG-RE------ASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VAlglPQGTKKsegaaSVARLLDLVGLGEYATHR--PKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT-RI--- 194
Cdd:COG2401 106 IG---RKGDFK-----DAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKRvar 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 195 NMQDLLldvhRQDPTTILLVTH--DVEEALyLSDRVIVLGKDTP 236
Cdd:COG2401 178 NLQKLA----RRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGV 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
40-231 |
4.65e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.04 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 40 PGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLN----RITAGTVRIGEKAVTGLDPR---------VAIGF 106
Cdd:COG4170 16 PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRerrkiigreIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEPR--LLPWRTVADNVALGLPQGT-------KKSEGAASVARLLDLVGLGEyatHR------PKEISGGMAQRVSLARA 171
Cdd:COG4170 96 QEPSscLDPSAKIGDQLIEAIPSWTfkgkwwqRFKWRKKRAIELLHRVGIKD---HKdimnsyPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 172 LARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
48-231 |
5.85e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 86.42 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 48 RGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDpRVAIGFQEPRLL---PWRTVADNVALG 124
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELE-LYQLSEAERRRLmrtEWGFVHQNPRDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 LPQGTkkSEGAASVARLLDlVGLGEYATHR--------------------PKEISGGMAQRVSLARALARNPGVLLLDEP 184
Cdd:TIGR02323 99 LRMRV--SAGANIGERLMA-IGARHYGNIRataqdwleeveidptriddlPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091083680 185 FGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-231 |
6.55e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.52 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDpRVAIGFQ 107
Cdd:PRK11701 7 LSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD-LYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLpWRT----VADNVALGLPQGTkkSEGAASVARLLDlVGLGEYATHR--------------------PKEISGGMA 163
Cdd:PRK11701 82 ERRRL-LRTewgfVHQHPRDGLRMQV--SAGGNIGERLMA-VGARHYGDIRatagdwlerveidaariddlPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 164 QRVSLARALARNPGVLLLDEPFGALDaltrINMQDLLLDVHRQDPTT----ILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRElglaVVIVTHDLAVARLLAHRLLVM 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-231 |
7.70e-20 |
|
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: 89.01 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 6 AVTDVPTSEKNGRRAVSTAAVPLSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITA 85
Cdd:TIGR02203 309 TLLDSPPEKDTGTRAIERARGDVEFRNV--TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 86 GT-----VRIGEKAVTGLDPRVAIGFQEPRLLPwRTVADNVALGLPQGTKKS--EGAASVARLLDLV-----GLGEYATH 153
Cdd:TIGR02203 387 GQilldgHDLADYTLASLRRQVALVSQDVVLFN-DTIANNIAYGRTEQADRAeiERALAAAYAQDFVdklplGLDTPIGE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 154 RPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLldVHRQDPTTILLVTH---DVEEAlylsDRVIV 230
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL--ERLMQGRTTLVIAHrlsTIEKA----DRIVV 539
|
.
gi 1091083680 231 L 231
Cdd:TIGR02203 540 M 540
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
48-231 |
9.99e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 48 RGVSFTAAPGEIISVIGSSGCGKSTLLRAA-----AGLNRiTAGTVRIGEKAVTGLDPR---VAIGFQEPR--LLPWRTV 117
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAAlgilpAGVRQ-TAGRVLLDGKPVAPCALRgrkIATIMQNPRsaFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNV-----ALGLPQGtkksegAASVARLLDLVGLGEyaTHR-----PKEISGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:PRK10418 99 HTHAretclALGKPAD------DATLTAALEAVGLEN--AARvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 188 LDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVM 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-231 |
1.68e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 24 AAVPLSFEGVGQSFPVPGGT-------HEVLRGVSFTAAPGEIISVIGSSGCGKST----LLRAAAGLNRITAGTV---R 89
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQplhN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 90 IGEKAVTGLDPRVAIGFQEPR--LLPWRTVADNVALGL----PQGTKKsEGAASVARLLDLVGLGEYATHR-PKEISGGM 162
Cdd:PRK15134 352 LNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGLrvhqPTLSAA-QREQQVIAVMEEVGLDPETRHRyPAEFSGGQ 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 163 AQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
56-231 |
1.82e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.47 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 56 PGEIISVI-GSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA-------IG--FQEPRLLPWRTVADNvalgL 125
Cdd:PRK11144 22 PAQGITAIfGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppekrrIGyvFQDARLFPHYKVRGN----L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 126 PQGTKKSEgAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDaLTRIN-----MQDLL 200
Cdd:PRK11144 98 RYGMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKRellpyLERLA 175
|
170 180 190
....*....|....*....|....*....|.
gi 1091083680 201 LDVHrqdpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11144 176 REIN----IPILYVSHSLDEILRLADRVVVL 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
50-231 |
1.90e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.59 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITaGTVRIGEKAVTGLDP---RVAIGF--QEPrLLPWRTVADNVALG 124
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPeswRKHLSWvgQNP-QLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 LPQGTKksegaASVARLLDLVGLGEYATHRPK-----------EISGGMAQRVSLARALARNPGVLLLDEPFGALDALT- 192
Cdd:PRK11174 447 NPDASD-----EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSe 521
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 193 RINMQDLLLDVHRQdptTILLVTHDVEEaLYLSDRVIVL 231
Cdd:PRK11174 522 QLVMQALNAASRRQ---TTLMVTHQLED-LAQWDQIWVM 556
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
42-231 |
3.64e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP-----RVAIGFQEPRLLPWRT 116
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraasrRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALG-LPQ----GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDal 191
Cdd:PRK09536 94 VRQVVEMGrTPHrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1091083680 192 trINMQDLLLDVHR---QDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK09536 172 --INHQVRTLELVRrlvDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-231 |
5.06e-19 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 83.43 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGL---DPRVAI 104
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlaSLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GF--QEPRLLPwRTVADNVALGLPQGTKKS-EGAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNP 176
Cdd:cd03251 79 GLvsQDVFLFN-DTVAENIAYGRPGATREEvEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 177 GVLLLDEPFGALDALTRINMQDLL--LDVHRqdptTILLVTH---DVEEAlylsDRVIVL 231
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALerLMKNR----TTFVIAHrlsTIENA----DRIVVL 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-211 |
5.34e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 86.41 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 1 MTLNSAVTDVPtseknGRRAVSTAAVPLSFEGVGQSFpvpGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL 80
Cdd:COG5265 336 LDQPPEVADAP-----DAPPLVVGGGEVRFENVSFGY---DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 81 NRITAGTVRIGE---KAVTGLDPRVAIGF--QEPRLLPwRTVADNVALGLPQGTKKS-EGAASVARLLDLV-GLGE-YAT 152
Cdd:COG5265 408 YDVTSGRILIDGqdiRDVTQASLRAAIGIvpQDTVLFN-DTIAYNIAYGRPDASEEEvEAAARAAQIHDFIeSLPDgYDT 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 153 ---HRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhRQDPTTI 211
Cdd:COG5265 487 rvgERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTL 547
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
44-255 |
5.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG---------LDPRVAIGFQEPRLlpw 114
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyirpVRKRIGMVFQFPES--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALGLPQGTKK-----SEGAASVARLLDLVGLG-EYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK13646 97 QLFEDTVEREIIFGPKNfkmnlDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 189 DALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTpeapatiqrivTVDRSHPRD 255
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGS-----------IVSQTSPKE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-231 |
6.80e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAV-----------TGLDPRVAIGFQEPRLLPW 114
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALGL-PQGTK-KSEGAASVARLLDLVGLGEYATHR----PKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK14246 105 LSIYDNIAYPLkSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1091083680 189 DALTRINMQDLLLDVHRQdpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-257 |
7.75e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 7.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKST-------LLRAAAG--------LNRITAGTVRIGE 92
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGlvqcdkmlLRRRSRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 93 KA------VTGLDprVAIGFQEP--RLLPWRTVADNVA--LGLPQGTKKSEGAASVARLLDLVGLGEYAT---HRPKEIS 159
Cdd:PRK10261 93 QSaaqmrhVRGAD--MAMIFQEPmtSLNPVFTVGEQIAesIRLHQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 160 GGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAP 239
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250
....*....|....*...
gi 1091083680 240 ATIQRIVTVDrSHPRDRA 257
Cdd:PRK10261 251 GSVEQIFHAP-QHPYTRA 267
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
37-231 |
1.12e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.08 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 37 FPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLN----RITAGTVRIGEKAVTGLDPR---------VA 103
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRerrklvghnVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGFQEPR--LLPWRTVADNVALGLPQGTKKSEGAASVA-------RLLDLVGLGEyatHR------PKEISGGMAQRVSL 168
Cdd:PRK15093 93 MIFQEPQscLDPSERVGRQLMQNIPGWTYKGRWWQRFGwrkrraiELLHRVGIKD---HKdamrsfPYELTEGECQKVMI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 169 ARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-239 |
1.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 20 AVSTAAVPLSFEGVGQSfpvpggtheVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNRIT--------AGTVRIG 91
Cdd:PRK14271 19 APAMAAVNLTLGFAGKT---------VLDQVSMGFPARAVTSLMGPTGSGKTTFLRT---LNRMNdkvsgyrySGDVLLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 92 EKA------VTGLDPRVAIGFQEPRLLPwRTVADNVALGLPQGT----KKSEGAASvARLLDlVGLGEYATHR----PKE 157
Cdd:PRK14271 87 GRSifnyrdVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlvprKEFRGVAQ-ARLTE-VGLWDAVKDRlsdsPFR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 158 ISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTHDVEEALYLSDRVIVL--GKDT 235
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFfdGRLV 241
|
....
gi 1091083680 236 PEAP 239
Cdd:PRK14271 242 EEGP 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
50-238 |
1.29e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.56 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTG--LDPRVAIGF--QEPRLLPWRTVADNVAL-- 123
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdIATRRRVGYmsQAFSLYGELTVRQNLELha 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 124 ---GLPqgtkKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLL 200
Cdd:NF033858 365 rlfHLP----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 201 LDVHRQDPTTILLVTHDVEEALyLSDRVI------VLGKDTPEA 238
Cdd:NF033858 441 IELSREDGVTIFISTHFMNEAE-RCDRISlmhagrVLASDTPAA 483
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-231 |
1.81e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 3 LNSAVTDVPTSEKNGRRAVSTAAVPLSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAaagLNR 82
Cdd:PRK11160 314 INEITEQKPEVTFPTTSTAAADQVSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 83 ---ITAGTVRIGEKAVTGLDP---RVAIGF--QEPRLLPwRTVADNVALGLPQgtkksegaASVARLLDL---VGLGEYA 151
Cdd:PRK11160 389 awdPQQGEILLNGQPIADYSEaalRQAISVvsQRVHLFS-ATLRDNLLLAAPN--------ASDEALIEVlqqVGLEKLL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 152 TH------------RPkeISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDvHRQDpTTILLVTHDVe 219
Cdd:PRK11160 460 EDdkglnawlgeggRQ--LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQN-KTVLMITHRL- 534
|
250
....*....|..
gi 1091083680 220 EALYLSDRVIVL 231
Cdd:PRK11160 535 TGLEQFDRICVM 546
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-231 |
3.40e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 19 RAVSTAAVPLSFEGVGQSFpvpGGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGL 98
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQY---SGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 99 DPRVAIGF------QEPRLLPWRTVADNVALGLPQgtkkseGAASVARLLDLvgLGEYATHRPKEISGGM-----AQRVS 167
Cdd:PRK15439 79 TPAKAHQLgiylvpQEPLLFPNLSVKENILFGLPK------RQASMQKMKQL--LAALGCQLDLDSSAGSlevadRQIVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 168 LARALARNPGVLLLDEPFGAL-----DALTRiNMQDLLldvhrQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLtpaetERLFS-RIRELL-----AQGVGIVFISHKLPEIRQLADRISVM 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-238 |
3.99e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekavtgLDPRVAIGFQ 107
Cdd:PRK09544 5 VSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLPWRTVADNVA--LGLPQGTKKSEGAASVARlldlVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPF 185
Cdd:PRK09544 73 PQKLYLDTTLPLTVNrfLRLRPGTKKEDILPALKR----VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091083680 186 GALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKD-----TPEA 238
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHiccsgTPEV 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-234 |
6.11e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA---- 103
Cdd:PRK09700 6 ISMAGIGKSF---GPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 --IGFQEPRLLPWRTVADNVALG-LPqgTKKSEGAASV---------ARLLDLVGLGEYATHRPKEISGGMAQRVSLARA 171
Cdd:PRK09700 82 igIIYQELSVIDELTVLENLYIGrHL--TKKVCGVNIIdwremrvraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 172 LARNPGVLLLDEPFGALDAlTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLgKD 234
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM-KD 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
36-192 |
7.64e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD-----PRVAIGFQEPR 110
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswrSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 LLPwRTVADNVALGLPQGTKksEGAASVARLL----DLVGLGE-YATH---RPKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:PRK10789 400 LFS-DTVANNIALGRPDATQ--QEIEHVARLAsvhdDILRLPQgYDTEvgeRGVMLSGGQKQRISIARALLLNAEILILD 476
|
170
....*....|
gi 1091083680 183 EPFGALDALT 192
Cdd:PRK10789 477 DALSAVDGRT 486
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
40-231 |
1.76e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 40 PGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIG-------EKAVTGLDPRVAIGFQEP-RL 111
Cdd:PRK13636 16 SDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidysRKGLMKLRESVGMVFQDPdNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 112 LPWRTVADNVALG-LPQGTKKSEGAASVARLLDLVGLgEYATHRPKE-ISGGMAQRVSLARALARNPGVLLLDEPFGALD 189
Cdd:PRK13636 95 LFSASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1091083680 190 ALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-233 |
2.24e-17 |
|
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: 81.98 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 40 PGGTHEVLRgVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAV-TGLDP-RVAIGF--QEPRLLPWR 115
Cdd:TIGR01257 940 PSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAvRQSLGMcpQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:TIGR01257 1019 TVAEHILFyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 195 NMQDLLLDVhrQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:TIGR01257 1099 SIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-216 |
2.43e-17 |
|
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: 78.17 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA-----IGFQePRLLPWRT 116
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHenilyLGHL-PGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVAL--GLPQGTKKSEGAAsvarlLDLVGLGEYAtHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDAlTR 193
Cdd:TIGR01189 90 ALENLHFwaAIHGGAQRTIEDA-----LAAVGLTGFE-DLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AG 162
|
170 180
....*....|....*....|...
gi 1091083680 194 INMQDLLLDVHRQDPTTILLVTH 216
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-249 |
2.62e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 34 GQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-----RIGEKAVTGLDPRVAIGFQE 108
Cdd:PRK10253 10 GEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgeHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 109 PRLLPWRTVADNVALG----LPQGTK-KSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:PRK10253 90 ATTPGDITVQELVARGryphQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 184 PFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQRIVTVD 249
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
36-231 |
2.68e-17 |
|
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: 77.35 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--RVAIGF--QEPRL 111
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKalSSLISVlnQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 112 LPwRTVADNVAlglpqgtkksegaasvarlldlvglgeyathrpKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:cd03247 87 FD-TTLRNNLG---------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 192 TRINMQDLLLDVHRQdpTTILLVTHDVeEALYLSDRVIVL 231
Cdd:cd03247 133 TERQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFL 169
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
42-217 |
9.43e-17 |
|
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: 75.18 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGekavtgldPRVAIGFqeprllpwrtvadnv 121
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--------STVKIGY--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 122 algLPQgtkksegaasvarlldlvglgeyathrpkeISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLl 201
Cdd:cd03221 68 ---FEQ------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL- 113
|
170
....*....|....*.
gi 1091083680 202 dvhRQDPTTILLVTHD 217
Cdd:cd03221 114 ---KEYPGTVILVSHD 126
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
42-231 |
1.89e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAglNRITAGTVRIGEKAVTGldprVAIGFQEPR----------- 110
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA--FRSPKGVKGSGSVLLNG----MPIDAKEMRaisayvqqddl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 LLPWRTVADNVA----LGLPQGTKKSEGAASVARLLDLVGLGEYA------THRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:TIGR00955 110 FIPTLTVREHLMfqahLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVhRQDPTTILLVTHDVEEALY-LSDRVIVL 231
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELFeLFDKIILM 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
45-231 |
2.04e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-------RIGEKAVTGLDPRVAIGFQEPRLLPWRTV 117
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkplDYSKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 AD-NVALGLPQ-GTKKSEGAASVARLLDLVGlGEYATHRPKE-ISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK13638 95 IDsDIAFSLRNlGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 195 NMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK13638 174 QMIAIIRRIVAQG-NHVIISSHDIDLIYEISDAVYVL 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
46-233 |
2.12e-16 |
|
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: 75.99 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAIGF--QEPRLLPwRTVADN 120
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhdlRSRISIipQDPVLFS-GTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VAlglPQGtKKSEGAasVARLLDLVGLGEY-----------ATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALD 189
Cdd:cd03244 98 LD---PFG-EYSDEE--LWQALERVGLKEFveslpggldtvVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 190 ALTRINMQDLLLDVHRQdpTTILLVTHDVeEALYLSDRVIVLGK 233
Cdd:cd03244 172 PETDALIQKTIREAFKD--CTVLTIAHRL-DTIIDSDRILVLDK 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
45-231 |
2.79e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD-----PRVAIGFQEP--RLLPWRTV 117
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDysyrsQRIRMIFQDPstSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 AD--NVALGLPQGTKKSEGAASVARLLDLVGL-GEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK15112 107 SQilDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 195 NMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-217 |
3.85e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.05 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 32 GVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekavtgLDPRVAIGF--QEP 109
Cdd:TIGR03719 9 RVSKVVP---PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGIKVGYlpQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 110 RLLPWRTVADNVALGLPQGTKK------------------SEGAASVARLLDLVGLG---------EYATH--------- 153
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKDAldrfneisakyaepdadfDKLAAEQAELQEIIDAAdawdldsqlEIAMDalrcppwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 154 RPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRinmqdLLLDVHRQD-PTTILLVTHD 217
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-----AWLERHLQEyPGTVVAVTHD 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-231 |
4.85e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 36 SFPVPGGTheVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-----VAIgfqEPR 110
Cdd:PRK10575 18 SFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafarkVAY---LPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 111 LLP---WRTVADNVALGL-----PQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:PRK10575 93 QLPaaeGMTVRELVAIGRypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 183 EPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
44-218 |
7.38e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTGLDPRVAIGFQEPRLLPWR---TVAD 119
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRQALQKNLVAYVPQSEEVDWSfpvLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPQGT-----KKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK15056 100 VVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|....
gi 1091083680 195 NMQDLLLDVhRQDPTTILLVTHDV 218
Cdd:PRK15056 180 RIISLLREL-RDEGKTMLVSTHNL 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
45-231 |
7.67e-16 |
|
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: 77.09 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP---RVAIGF--QEPRLLPwRTVAD 119
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRhtlRQFINYlpQEPYIFS-GSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPQGTKKSE--GAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT 192
Cdd:TIGR01193 567 NLLLGAKENVSQDEiwAACEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 193 RINMQDLLLDVHRQdptTILLVTHDVEEAlYLSDRVIVL 231
Cdd:TIGR01193 647 EKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVL 681
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
46-233 |
9.87e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD----PRVAIGF--QEPRLLPWRTVAD 119
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlharARRGIGYlpQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NV--ALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQ 197
Cdd:PRK10895 98 NLmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1091083680 198 DLLLDVhRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK10895 178 RIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQ 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
50-231 |
2.50e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRiTAGTVRIGEKAVTGLDP-----RVAIGFQEPRLLPWRTVADNVALG 124
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAaelarHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 LPQGTKKSEGAASVARLLDLVGLGEyATHRP-KEISGGMAQRVSLARAL-----ARNPG--VLLLDEPFGALDaLTRINM 196
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDD-KLGRSvNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLD-VAQQAA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK03695 172 LDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLL 206
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
42-216 |
3.25e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA-----IGFQ---EPRLLP 113
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdllyLGHQpgiKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 114 WRTVADNVALGLPQgtkkseGAASVARLLDLVGLGEYAtHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDA-- 190
Cdd:PRK13538 92 LENLRFYQRLHGPG------DDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKqg 164
|
170 180
....*....|....*....|....*....
gi 1091083680 191 ---LTRinmqdlLLDVHRQDPTTILLVTH 216
Cdd:PRK13538 165 varLEA------LLAQHAEQGGMVILTTH 187
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-216 |
3.61e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 6 AVTDVPTSEKNGRRAVSTAAVPLSFEGVgqSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLlraAAGLNR--- 82
Cdd:PRK11176 320 AILDLEQEKDEGKRVIERAKGDIEFRNV--TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfyd 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 83 -----ITAGTVRIGEKAVTGLDPRVAIGFQEPRLLPwRTVADNVALglPQGTKKS----EGAASVARLLDLV-----GL- 147
Cdd:PRK11176 395 idegeILLDGHDLRDYTLASLRNQVALVSQNVHLFN-DTIANNIAY--ARTEQYSreqiEEAARMAYAMDFInkmdnGLd 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 148 ---GEYAThrpkEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTH 216
Cdd:PRK11176 472 tviGENGV----LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH 537
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
46-231 |
6.41e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGlnRITA----GTVRIGEKAVTGLDPRvAIGF--QEPRLLPWRTVAD 119
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGnnftGTILANNRKPTKQILK-RTGFvtQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVA----LGLPQGTKKSEG---AASVARLLDLVGLGEYATHRP--KEISGGMAQRVSLARALARNPGVLLLDEPFGALDA 190
Cdd:PLN03211 160 TLVfcslLRLPKSLTKQEKilvAESVISELGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1091083680 191 LTRINMQDLLLDVhRQDPTTILLVTHDVEEALY-LSDRVIVL 231
Cdd:PLN03211 240 TAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVYqMFDSVLVL 280
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
47-228 |
1.57e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRiTAGTVRIGEKAVTGLDPRV-----AIGFQEPRLLPWRTVADNV 121
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhrAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 122 ALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARAL-----ARNPG--VLLLDEPFGALDALTRI 194
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQQA 170
|
170 180 190
....*....|....*....|....*....|....
gi 1091083680 195 NMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRV 228
Cdd:COG4138 171 ALDRLLRELCQQG-ITVVMSSHDLNHTLRHADRV 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
47-264 |
2.45e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL--------------NRITAGTVRIGEKAvtgldpRVAIGFQEPRLL 112
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegEELQASNIRDTERA------GIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVADNVALG---LPQG-TKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK13549 95 KELSVLENIFLGneiTPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 189 -DALTRInMQDLLLDVHRQDPTTIlLVTHDVEEALYLSDRVIVL--GKDTPEAPA---TIQRIVT--VDRshprdradaE 260
Cdd:PRK13549 175 tESETAV-LLDIIRDLKAHGIACI-YISHKLNEVKAISDTICVIrdGRHIGTRPAagmTEDDIITmmVGR---------E 243
|
....
gi 1091083680 261 ITAL 264
Cdd:PRK13549 244 LTAL 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
46-190 |
4.17e-14 |
|
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: 69.44 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA-----IGFQePRLLPWRTVADN 120
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllyLGHA-PGIKTTLSVLEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 121 VALGLPQGtkkseGAASVARLLDLVGLGEYAtHRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDA 190
Cdd:cd03231 94 LRFWHADH-----SDEQVEEALARVGLNGFE-DRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
47-251 |
5.19e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL--------------NRITAGTVRIGEKAvtGldprVAIGFQEPRLL 112
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegeilfdgEVCRFKDIRDSEAL--G----IVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVADNVALGLPQGTKK----SEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:NF040905 91 PYLSIAENIFLGNERAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 189 DALTRINMQDLLLDVHRQDPTTIlLVTHDVEEALYLSDRVIVL--GK-----DTPEAPATIQRIVT--VDRS 251
Cdd:NF040905 171 NEEDSAALLDLLLELKAQGITSI-IISHKLNEIRRVADSITVLrdGRtietlDCRADEVTEDRIIRgmVGRD 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-231 |
5.34e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTllrAAAGLNRI--------TAGTVRIGEKAVTGLD 99
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSV---TALSILRLlpsppvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 P---------RVAIGFQEP--RLLPWRTVADNVA--LGLPQGTKKSEGAASVARLLDLVGLGEYATHR---PKEISGGMA 163
Cdd:PRK15134 83 EqtlrgvrgnKIAMIFQEPmvSLNPLHTLEKQLYevLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGER 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091083680 164 QRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-217 |
7.57e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 32 GVGQSFPvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekavtgLDPRVAIGF--QEP 109
Cdd:PRK11819 11 RVSKVVP---PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PAPGIKVGYlpQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 110 RLLPWRTVADNVALGLPQGTKK------------------SEGAASVARL---LDLVGLGEY---------ATHRP---- 155
Cdd:PRK11819 80 QLDPEKTVRENVEEGVAEVKAAldrfneiyaayaepdadfDALAAEQGELqeiIDAADAWDLdsqleiamdALRCPpwda 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 156 --KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRinmqdLLLDVHRQD-PTTILLVTHD 217
Cdd:PRK11819 160 kvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-----AWLEQFLHDyPGTVVAVTHD 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-190 |
2.11e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAG-LNRITAGTVRI-GEKAVTgldPRVAIGFQEprllpwrTVADNVALG 124
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIrGTVAYV---PQVSWIFNA-------TVRDNILFG 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 125 LPQGTKKSEGAASVARLL---------DLVGLGEyathRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDA 190
Cdd:PLN03130 703 SPFDPERYERAIDVTALQhdldllpggDLTEIGE----RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-216 |
2.47e-13 |
|
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: 66.41 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGtHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAvtgldprvAIGFq 107
Cdd:cd03223 1 IELENL--SLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------DLLF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 eprlLPWRTVadnvalgLPQGTKKSegaaSVARLLDlvglgeyathrpKEISGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:cd03223 69 ----LPQRPY-------LPLGTLRE----QLIYPWD------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*....
gi 1091083680 188 LDAltriNMQDLLLDVHRQDPTTILLVTH 216
Cdd:cd03223 122 LDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-231 |
3.49e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpgGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR------ 101
Cdd:PRK10762 5 LQLKGIDKAFP---GV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 102 VAIGFQEPRLLPWRTVADNVALGlpQGTKKSEGA-------ASVARLLDLVGLgEYATHRP-KEISGGMAQRVSLARALA 173
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLG--REFVNRFGRidwkkmyAEADKLLARLNL-RFSSDKLvGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 174 RNPGVLLLDEPfgaLDALTRINMQDLLLDVH--RQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10762 158 FESKVIIMDEP---TDALTDTETESLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-217 |
3.75e-13 |
|
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: 69.19 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKavtgldprVAIGF- 106
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--------VKLAYv 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 --QEPRLLPWRTVADNVALGLPQ---GTKKSEGAASVARLldlvGL-GEYATHRPKEISGGMAQRVSLARALARNPGVLL 180
Cdd:TIGR03719 391 dqSRDALDPNKTVWEEISGGLDIiklGKREIPSRAYVGRF----NFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091083680 181 LDEPFGALDALTRINMQDLLLDVhrqdPTTILLVTHD 217
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNF----AGCAVVISHD 499
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
57-230 |
1.08e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.28 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 57 GEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIgekavtgldPRVAIGFQEPRLLPWR--TVADNVALGLPQGTKKSEG 134
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---------ELDTVSYKPQYIKADYegTVRDLLSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 135 AASVARLLDLVGLGEyatHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLV 214
Cdd:cd03237 96 KTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVV 172
|
170
....*....|....*.
gi 1091083680 215 THDVEEALYLSDRVIV 230
Cdd:cd03237 173 EHDIIMIDYLADRLIV 188
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
50-231 |
1.21e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAI--GFQ---EPR----LLPWRTVADN 120
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIraGIMlcpEDRkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALG----------LPQGTKKSEGAASVARLLDLvglgeyATHRPKE----ISGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:PRK11288 352 INISarrhhlragcLINNRWEAENADRFIRSLNI------KTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1091083680 187 ALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGVADRIVVM 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-217 |
1.24e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFPVPGGTheVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKavtgLDprVAIgFQEP 109
Cdd:PRK11147 320 FEMENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LE--VAY-FDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 110 R--LLPWRTVADNVALGlpqgtKKSEGAASVAR-----LLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:PRK11147 391 RaeLDPEKTVMDNLAEG-----KQEVMVNGRPRhvlgyLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 183 EPFGALDALTRINMQDLLLDVhrqdPTTILLVTHD 217
Cdd:PRK11147 466 EPTNDLDVETLELLEELLDSY----QGTVLLVSHD 496
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-231 |
5.54e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 43 THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDP--RVAIGF-------QEPRL-- 111
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqRLARGLvylpedrQSSGLyl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 112 ---LPWRTVADNV-ALGLPQGTKKSegAASVARLLDLVGLG-EYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFG 186
Cdd:PRK15439 355 dapLAWNVCALTHnRRGFWIKPARE--NAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1091083680 187 ALDALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
46-233 |
7.14e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIGF--QEPRLLPWRTVADNVAL 123
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYlgHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 124 --GLpQGTKKSEGAASVarlLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDaLTRINMQDLLL 201
Cdd:PRK13543 106 lcGL-HGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMI 180
|
170 180 190
....*....|....*....|....*....|..
gi 1091083680 202 DVHRQDPTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13543 181 SAHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-247 |
9.46e-12 |
|
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: 64.85 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL--------------NRITAGTVRIGEK 93
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgeiywsgSPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 94 AvtgldpRVAIGFQEPRLLPWRTVADNVALG----LPQG-TKKSEGAASVARLLDLVGLGEYATHRP-KEISGGMAQRVS 167
Cdd:TIGR02633 78 A------GIVIIHQELTLVPELSVAENIFLGneitLPGGrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 168 LARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTIlLVTHDVEEALYLSDRVIVLgKD------TPEAPAT 241
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACV-YISHKLNEVKAVCDTICVI-RDgqhvatKDMSTMS 229
|
....*.
gi 1091083680 242 IQRIVT 247
Cdd:TIGR02633 230 EDDIIT 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
45-231 |
1.21e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLN--RITAGTVRIGEKAVTGLDP--RVAIG----FQEPRLLPWRT 116
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPeeRARLGiflaFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADnvalglpqgtkksegaasvarLLDLVGLGeyathrpkeISGGMAQRVSLARALARNPGVLLLDEPFGALD--ALTRI 194
Cdd:cd03217 94 NAD---------------------FLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidALRLV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 1091083680 195 NMQdllLDVHRQDPTTILLVTHDVEEALYL-SDRVIVL 231
Cdd:cd03217 144 AEV---INKLREEGKSVLIITHYQRLLDYIkPDRVHVL 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
44-247 |
1.23e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGlnRITAGtVRIGEKAVTG---LDPRVAIGFQEPRLLPWRTVadn 120
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGG-GAPRGARVTGdvtLNGEPLAAIDAPRLARLRAV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 valgLPQGTKKseGAASVARllDLVGLGEY--------ATHRPKEI---------------------SGGMAQRVSLARA 171
Cdd:PRK13547 88 ----LPQAAQP--AFAFSAR--EIVLLGRYpharragaLTHRDGEIawqalalagatalvgrdvttlSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 172 LA---------RNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATI 242
Cdd:PRK13547 160 LAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
....*
gi 1091083680 243 QRIVT 247
Cdd:PRK13547 240 ADVLT 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
47-231 |
1.77e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAIG-----FQEPR----LLPWRTV 117
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAngivyISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVAL-GLPQGTKKS---EGAASVARLLDLVGLGEYATHRPKEI----SGGMAQRVSLARALARNPGVLLLDEPFGALD 189
Cdd:PRK10762 348 KENMSLtALRYFSRAGgslKHADEQQAVSDFIRLFNIKTPSMEQAigllSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091083680 190 --ALTRINMqdlLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10762 428 vgAKKEIYQ---LINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
41-183 |
2.45e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 41 GGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTgldprVAIGFQEPRLLpwrTVADN 120
Cdd:PRK13545 34 GEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL-----IAISSGLNGQL---TGIEN 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091083680 121 VAL-GLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:PRK13545 106 IELkGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
45-237 |
3.37e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVrIGEKAVtgldprvAIGFQEPRLLPwRTVADNVALG 124
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSI-------AYVPQQAWIMN-ATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 LPQGTKKSEGAASVARL-LDLVGLGEYATHRPKE----ISGGMAQRVSLARALARNPGVLLLDEPFGALDALT--RInMQ 197
Cdd:PTZ00243 745 DEEDAARLADAVRVSQLeADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRV-VE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 198 DLLLDvhRQDPTTILLVTHDVeEALYLSDRVIVLGKDTPE 237
Cdd:PTZ00243 824 ECFLG--ALAGKTRVLATHQV-HVVPRADYVVALGDGRVE 860
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
46-231 |
3.38e-11 |
|
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: 62.18 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekavtgLDPRVAIGFQEPRLLPwRTVADNVALGL 125
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------HSGRISFSSQFSWIMP-GTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 126 PQGTKKSEGAASVARLL-DLVGLGEYATHRPKE----ISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLL 200
Cdd:cd03291 123 SYDEYRYKSVVKACQLEeDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
170 180 190
....*....|....*....|....*....|.
gi 1091083680 201 LDVHRQDPTTIlLVTHDVEEaLYLSDRVIVL 231
Cdd:cd03291 203 VCKLMANKTRI-LVTSKMEH-LKKADKILIL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-221 |
3.45e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 29 SFEGVGQSFpvpGGTHeVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekaVTGLD--------- 99
Cdd:NF033858 3 RLEGVSHRY---GKTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE-----VLGGDmadarhrra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 --PRVA-----IGfqePRLLPWRTVADNVAL-----GLPqgtkKSEGAASVARLLDLVGLGEYAtHRP-KEISGGMAQRV 166
Cdd:NF033858 74 vcPRIAympqgLG---KNLYPTLSVFENLDFfgrlfGQD----AAERRRRIDELLRATGLAPFA-DRPaGKLSGGMKQKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 167 SLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPT-TILLVTHDVEEA 221
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGmSVLVATAYMEEA 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-231 |
3.88e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRigekavtgLDPRVAIGFQEPRLLPwRTVADNVALGL 125
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------HSGRISFSPQTSWIMP-GTIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 126 PQGTKKSEGAASVARL---------LDLVGLGEYAThrpkEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:TIGR01271 512 SYDEYRYTSVIKACQLeedialfpeKDKTVLGEGGI----TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*
gi 1091083680 197 QDLLLDVHRQDPTTIlLVTHDVEEaLYLSDRVIVL 231
Cdd:TIGR01271 588 FESCLCKLMSNKTRI-LVTSKLEH-LKKADKILLL 620
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-190 |
4.32e-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: 63.04 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 32 GVGQSFPVPGGTHE-------VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIgeKAVTGLDPRVAi 104
Cdd:TIGR00957 632 GEGNSITVHNATFTwardlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQQA- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 gfqeprllpW---RTVADNVALGLPQGTKKSEGAASVARLL---------DLVGLGEYATHrpkeISGGMAQRVSLARAL 172
Cdd:TIGR00957 709 ---------WiqnDSLRENILFGKALNEKYYQQVLEACALLpdleilpsgDRTEIGEKGVN----LSGGQKQRVSLARAV 775
|
170
....*....|....*...
gi 1091083680 173 ARNPGVLLLDEPFGALDA 190
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDA 793
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
45-231 |
5.08e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL--NRITAGTVRIGEKAVTGLDP--RVAIG----FQEPRLLPWRT 116
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPdeRARAGiflaFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VAD--NVALGLPQGTKKSEGA--ASVARLLDLVGLGEYATHRP--KEISGGMAQRVSLARALARNPGVLLLDEPFGALD- 189
Cdd:COG0396 94 VSNflRTALNARRGEELSAREflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDi 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1091083680 190 -ALtRInMQDLLLDVHRQDpTTILLVTHdVEEAL-YLS-DRVIVL 231
Cdd:COG0396 174 dAL-RI-VAEGVNKLRSPD-RGILIITH-YQRILdYIKpDFVHVL 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
43-234 |
8.18e-11 |
|
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: 59.97 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 43 THEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGlnrITAGTVRI-GEKAVTGLDprvaigFQEPRLLPWRTVADNV 121
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVeGDIHYNGIP------YKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 122 A--LGLPQGTkksegaasVARLLDLVGL---GEYAthrpKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINM 196
Cdd:cd03233 90 EedVHFPTLT--------VRETLDFALRckgNEFV----RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 197 -QDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVLGKD 234
Cdd:cd03233 158 lKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
56-255 |
1.61e-10 |
|
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: 61.57 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 56 PGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTgldPRVAIGFQEPRLLPWRTVADNVALGLP--------Q 127
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGREhlylyarlR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 128 GTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQD 207
Cdd:TIGR01257 2041 GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG 2120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 208 pTTILLVTHDVEEALYLSDRVIVLGKDTPEAPATIQR---------IVTVDRSHPRD 255
Cdd:TIGR01257 2121 -RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHlkskfgdgyIVTMKIKSPKD 2176
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-233 |
2.11e-10 |
|
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: 58.96 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLD-----PRVAIGFQEPRLLPwRTVAD 119
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlrSSLTIIPQDPTLFS-GTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALGLPQGTKKSEGAASVArlldlvGLGEyathrpkEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDL 199
Cdd:cd03369 101 NLDPFDEYSDEEIYGALRVS------EGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190
....*....|....*....|....*....|....
gi 1091083680 200 LLDVHRQdpTTILLVTHDVEEALYLsDRVIVLGK 233
Cdd:cd03369 168 IREEFTN--STILTIAHRLRTIIDY-DKILVMDA 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-192 |
3.00e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 38 PVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGlnRITAGTVRIGEKAVTG--LDPRVA--IGF--QEPRL 111
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGrpLDSSFQrsIGYvqQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 112 LPWRTVADNV----ALGLPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMA----QRVSLARALARNPGVLL-LD 182
Cdd:TIGR00956 848 LPTSTVRESLrfsaYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNveqrKRLTIGVELVAKPKLLLfLD 927
|
170
....*....|
gi 1091083680 183 EPFGALDALT 192
Cdd:TIGR00956 928 EPTSGLDSQT 937
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-231 |
5.45e-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: 57.20 E-value: 5.45e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 157 EISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
107-231 |
5.93e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEPRLLPwRTVADNVALGLPQGTKKSegaasVARLLDLVGLGEYATHRP-----------KEISGGMAQRVSLARALARN 175
Cdd:PTZ00265 1303 QEPMLFN-MSIYENIKFGKEDATRED-----VKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091083680 176 PGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHDVeEALYLSDRVIVL 231
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVF 1431
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-217 |
1.35e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 30 FEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKavtgldprVAIGF--Q 107
Cdd:PRK11819 327 AENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET--------VKLAYvdQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EpR--LLPWRTVADNValglpqgtkkSEGaasvarlLDLVGLGEYATH-----------------RPKEISGGMAQRVSL 168
Cdd:PRK11819 395 S-RdaLDPNKTVWEEI----------SGG-------LDIIKVGNREIPsrayvgrfnfkggdqqkKVGVLSGGERNRLHL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091083680 169 ARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhrqdPTTILLVTHD 217
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF----PGCAVVISHD 501
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
57-233 |
2.02e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 57 GEIISVIGSSGCGKSTLLRAAAG-LNRITAGTVRIgeKAVTGLDPRVAIGFQEprllpwrTVADNVALGLPQGTKKSEGA 135
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI--RGSVAYVPQVSWIFNA-------TVRENILFGSDFESERYWRA 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 136 ASVARLL---------DLVGLGEyathRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQ 206
Cdd:PLN03232 714 IDVTALQhdldllpgrDLTEIGE----RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK 789
|
170 180
....*....|....*....|....*..
gi 1091083680 207 DPTTIlLVTHDVeEALYLSDRVIVLGK 233
Cdd:PLN03232 790 GKTRV-LVTNQL-HFLPLMDRIILVSE 814
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-200 |
2.73e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.33 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGlnRITAGTVRiGEKAVTGLDPRVA---- 103
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEILINGRPLDKNfqrs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 104 IGF--QEPRLLPWRTVadNVALglpqgtkksEGAAsvarllDLVGLGeyATHRpkeisggmaQRVSLARALARNPGVLLL 181
Cdd:cd03232 81 TGYveQQDVHSPNLTV--REAL---------RFSA------LLRGLS--VEQR---------KRLTIGVELAAKPSILFL 132
|
170
....*....|....*....
gi 1091083680 182 DEPFGALDALTRINMQDLL 200
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFL 151
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-229 |
2.93e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFpvpgGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-VAIGF 106
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 107 QEPRLL-----PWRTVADN-----VALGlpqgtkksegaasvaRLLdlvGLGEYATHRPKEISGGMAQRVSLARALARNP 176
Cdd:PRK15064 396 ENDLTLfdwmsQWRQEGDDeqavrGTLG---------------RLL---FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 177 GVLLLDEPFGALDaLTRINMQDLLLDVHrqdPTTILLVTHDVEEALYLSDRVI 229
Cdd:PRK15064 458 NVLVMDEPTNHMD-MESIESLNMALEKY---EGTLIFVSHDREFVSSLATRII 506
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-237 |
3.04e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT--GL-DPRVAIGF--QEPRLLPwRTVADN 120
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLtDLRRVLSIipQSPVLFS-GTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLPQGTKKSEGAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRIN 195
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091083680 196 MQDLLLDVHRQdpTTILLVTH------DVEEALYLSDRViVLGKDTPE 237
Cdd:PLN03232 1410 IQRTIREEFKS--CTMLVIAHrlntiiDCDKILVLSSGQ-VLEYDSPQ 1454
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
46-216 |
3.74e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIG----EKAVTGLDPRVAIGFQEPRLLPWRTVADNV 121
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsiKKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 122 ALGLpqgtKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDlLL 201
Cdd:PRK13540 96 LYDI----HFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT-KI 170
|
170
....*....|....*
gi 1091083680 202 DVHRQDPTTILLVTH 216
Cdd:PRK13540 171 QEHRAKGGAVLLTSH 185
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
56-233 |
4.56e-09 |
|
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: 53.92 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 56 PGEIISVIGSSGCGKSTLLRAAAG-LNRITAGTVRIgekavtgldprvaigfqeprllpwrtvadnvalglpqgtkkseG 134
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYI-------------------------------------------D 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 135 AASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDL-----LLDVHRQDPT 209
Cdd:smart00382 38 GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNL 117
|
170 180
....*....|....*....|....*....
gi 1091083680 210 TILLVTHDVE-----EALYLSDRVIVLGK 233
Cdd:smart00382 118 TVILTTNDEKdlgpaLLRRRFDRRIVLLL 146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
55-231 |
6.62e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 55 APGEIISVIGSSGCGKSTLLRAAAG-----LNRIT------------AGT-VRIGEKAVTGLDPRVAIGFQEPRLLPwRT 116
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDdppdwdeildefRGSeLQNYFTKLLEGDVKVIVKPQYVDLIP-KA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVALGLpqgTKKSEGAA--SVARLLDLVGLGEYAThrpKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:cd03236 103 VKGKVGELL---KKKDERGKldELVDQLELRHVLDRNI---DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 195 NMQDLlldVHR--QDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:cd03236 177 NAARL---IRElaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
131-233 |
1.02e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 131 KSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRqDPTT 210
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGAT 196
|
90 100
....*....|....*....|...
gi 1091083680 211 ILLVTHDVEEALYLSDRVIVLGK 233
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDR 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
46-216 |
1.08e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPR-----VAIGFQEPRLLPwRTVADN 120
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrqgVAMVQQDPVVLA-DTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLPQGTKKSEGAASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRIN 195
Cdd:PRK10790 435 VTLGRDISEEQVWQALETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180
....*....|....*....|.
gi 1091083680 196 MQDLLLDVHRQdpTTILLVTH 216
Cdd:PRK10790 515 IQQALAAVREH--TTLVVIAH 533
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
39-233 |
1.21e-08 |
|
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: 53.48 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 39 VPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLR---AAAGLNRITAGTVRIGEkavtglDPRVAIGfqeprllpwr 115
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglYASGKARLISFLPKFSR------NKLIFID---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 tvadnvalglpqgtkksegaaSVARLLDlVGLGEYATHRP-KEISGGMAQRVSLARALARNPG--VLLLDEPFGALDalt 192
Cdd:cd03238 67 ---------------------QLQFLID-VGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH--- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1091083680 193 rinMQDL--LLDVHR---QDPTTILLVTHDvEEALYLSDRVIVLGK 233
Cdd:cd03238 122 ---QQDInqLLEVIKgliDLGNTVILIEHN-LDVLSSADWIIDFGP 163
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-193 |
1.54e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPvpGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVR-----IGEKAVTGLDPRV 102
Cdd:PTZ00243 1309 LVFEGVQMRYR--EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRvngreIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 103 AIGFQEPRLLPwRTVADNVALGLpqgtkkSEGAASVARLLDLVGLGEYATHRPKEI-----------SGGMAQRVSLARA 171
Cdd:PTZ00243 1387 SMIPQDPVLFD-GTVRQNVDPFL------EASSAEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARA 1459
|
170 180
....*....|....*....|....
gi 1091083680 172 -LARNPGVLLLDEPFGALD-ALTR 193
Cdd:PTZ00243 1460 lLKKGSGFILMDEATANIDpALDR 1483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
53-230 |
1.69e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 53 TAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVrigekavtglDPRVAIGFQeprllPWRTVAD---NVALGLPQGT 129
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPELKISYK-----PQYIKPDydgTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 130 KKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPT 209
Cdd:PRK13409 426 DDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREA 505
|
170 180
....*....|....*....|.
gi 1091083680 210 TILLVTHDVEEALYLSDRVIV 230
Cdd:PRK13409 506 TALVVDHDIYMIDYISDRLMV 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
57-230 |
2.26e-08 |
|
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: 54.79 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 57 GEIISVIGSSGCGKSTLLRAAAGLNRITAGTVrigekavtglDPRVAIGFQEPRLLP--WRTVADNVALGLPQGTKKSEG 134
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKISYKPQYISPdyDGTVEEFLRSANTDDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 135 AASVARLLDLVGLGEyathRP-KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILL 213
Cdd:COG1245 436 KTEIIKPLGLEKLLD----KNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMV 511
|
170
....*....|....*..
gi 1091083680 214 VTHDVEEALYLSDRVIV 230
Cdd:COG1245 512 VDHDIYLIDYISDRLMV 528
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
42-254 |
2.33e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRiTAGTVRI---GEKAVTGLDPRVAIGFQEPRLL----PW 114
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIdgvSWNSVPLQKWRKAFGVIPQKVFifsgTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADnvalglPQGTKKSEGAASVArllDLVGLGEYATHRPKE-----------ISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:cd03289 94 RKNLD------PYGKWSDEEIWKVA---EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 184 PFGALDALTRINMQDLLldVHRQDPTTILLVTHDVeEALYLSDRVIVLGKDTPEAPATIQRIVTvDRSHPR 254
Cdd:cd03289 165 PSAHLDPITYQVIRKTL--KQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLN-EKSHFK 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
44-215 |
6.35e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 44 HEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-----RIGEKAVTGLDPRVAIGFQEPR---LLPW- 114
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfsHITRLSFEQLQKLVSDEWQRNNtdmLSPGe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 ----RTVADNVALGlpqgtkkSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDA 190
Cdd:PRK10938 96 ddtgRTTAEIIQDE-------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|....*
gi 1091083680 191 LTRINMQDLLLDVHRQDPTTILLVT 215
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLN 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
48-231 |
7.43e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 48 RGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVA----IGF-----QEPRLLPWRTVA 118
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgMAYitesrRDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVA-------------LGLPQGTKKSEGAASVARLLDL--VGLGEYAThrpkEISGGMAQRVSLARALARNPGVLLLDE 183
Cdd:PRK09700 360 QNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLALkcHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1091083680 184 PFGALDALTRINMQDLLldvhRQ---DPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVM----RQladDGKVILMVSSELPEIITVCDRIAVF 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
50-233 |
9.40e-08 |
|
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: 52.52 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGL-NRITAGTVRIGEKAVTGLDPRVAIG-----FQEPR----LLPWRTVAD 119
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRagiamVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALG-LPQGTKKS--EGAASVARLLDLVGLGEYATHRP----KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT 192
Cdd:TIGR02633 359 NITLSvLKSFCFKMriDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 193 RINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:TIGR02633 439 KYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGE 478
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
46-233 |
1.20e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTL-------LRAAAGLNRITAgtVRIGEKAVTGLDPRVAIGFQEPRLLpwrtvA 118
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfriNESAEGEIIIDG--LNIAKIGLHDLRFKITIIPQDPVLF-----S 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGL-PQGTKKSEG---AASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALD 189
Cdd:TIGR00957 1374 GSLRMNLdPFSQYSDEEvwwALELAHLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1091083680 190 ALTrinmQDLLLDVHRQ--DPTTILLVTHDVEEALYLSdRVIVLGK 233
Cdd:TIGR00957 1454 LET----DNLIQSTIRTqfEDCTVLTIAHRLNTIMDYT-RVIVLDK 1494
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-237 |
1.23e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL-----NRITAGTVRIGEKAVTGLDPRVAIGFQEPRLLpwrtvADN 120
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIvelerGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF-----SGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLPQGTKKSEG----AASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:PLN03130 1329 VRFNLDPFNEHNDAdlweSLERAHLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 192 TRINMQDLLLDVHRQdpTTILLVTHDVeEALYLSDRVIVL--GK----DTPE 237
Cdd:PLN03130 1409 TDALIQKTIREEFKS--CTMLIIAHRL-NTIIDCDRILVLdaGRvvefDTPE 1457
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
41-220 |
1.24e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 41 GGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTV-RIGEKAV----TGLDPRVaigfqeprllpwr 115
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSViaisAGLSGQL------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 TVADNVALG-LPQGTKKSEGAASVARLLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK13546 101 TGIENIEFKmLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180
....*....|....*....|....*.
gi 1091083680 195 NMQDLLLDVHRQDpTTILLVTHDVEE 220
Cdd:PRK13546 181 KCLDKIYEFKEQN-KTIFFVSHNLGQ 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
46-221 |
1.40e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAG------LNRITA-GTVR-IGEkavTGLDPRVAIGFQEPRL-LPWR- 115
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTLfGRRRgSGE---TIWDIKKHIGYVSSSLhLDYRv 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 116 -TVADNVAL-------GLPQGTkkSEGAASVAR-LLDLVGLGEYATHRP-KEISGGMaQRVSL-ARALARNPGVLLLDEP 184
Cdd:PRK10938 352 sTSVRNVILsgffdsiGIYQAV--SDRQQKLAQqWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEP 428
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 185 FGALDALTRINMQ---DLLLdvhRQDPTTILLVTHDVEEA 221
Cdd:PRK10938 429 LQGLDPLNRQLVRrfvDVLI---SEGETQLLFVSHHAEDA 465
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
63-217 |
2.25e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 63 IGSSGCGKSTLLRAAAGLNRITAGTVrigekavtGLDPRVAIG--------FQEprllpwRTVADNVALG---------- 124
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNV--------SLDPNERLGklrqdqfaFEE------FTVLDTVIMGhtelwevkqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 ------LPQGTKksEGAASVARL------LD-----------LVGLG---EYATHRPKEISGGMAQRVSLARALARNPGV 178
Cdd:PRK15064 99 rdriyaLPEMSE--EDGMKVADLevkfaeMDgytaearagelLLGVGipeEQHYGLMSEVAPGWKLRVLLAQALFSNPDI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 179 LLLDEPFGALDaltrINMQDLLLDVHRQDPTTILLVTHD 217
Cdd:PRK15064 177 LLLDEPTNNLD----INTIRWLEDVLNERNSTMIIISHD 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
50-233 |
2.85e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 50 VSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNR-ITAGTVRIGEKAVTGLDPRVAIGFQ-----EPR----LLPWRTVAD 119
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGiamvpEDRkrdgIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 NVALG-LPQGTKKS--EGAASVARLLDLVGLGEYATHRP----KEISGGMAQRVSLARALARNPGVLLLDEPFGALDALT 192
Cdd:PRK13549 361 NITLAaLDRFTGGSriDDAAELKTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1091083680 193 RINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVLGK 233
Cdd:PRK13549 441 KYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHE 480
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
42-217 |
4.01e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRI-GEKAVTGLD---PRVAIGfqeprllpwrTV 117
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQqdpPRNVEG----------TV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLPQ---------------GTKKSEGA----ASVARLLD--------------LVGLGEYATHRPKEISGGMAQ 164
Cdd:PRK11147 84 YDFVAEGIEEqaeylkryhdishlvETDPSEKNlnelAKLQEQLDhhnlwqlenrinevLAQLGLDPDAALSSLSGGWLR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091083680 165 RVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhrqdPTTILLVTHD 217
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHD 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
42-216 |
4.52e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAG--LNRITAGTVRIGEKAVTGLDPR------VAIGFQEPRLLP 113
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEerahlgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 114 WRTVADNVALGLPQgTKKSEGAASVARL---------LDLVGLGEYATHR--PKEISGGMAQRVSLARALARNPGVLLLD 182
Cdd:CHL00131 98 GVSNADFLRLAYNS-KRKFQGLPELDPLefleiinekLKLVGMDPSFLSRnvNEGFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1091083680 183 EPFGAL--DALTRINMQdllLDVHRQDPTTILLVTH 216
Cdd:CHL00131 177 ETDSGLdiDALKIIAEG---INKLMTSENSIILITH 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
141-231 |
6.09e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 141 LLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDpTTILLVTHDVee 220
Cdd:COG1245 196 LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG-KYVLVVEHDL-- 272
|
90
....*....|...
gi 1091083680 221 AL--YLSDRVIVL 231
Cdd:COG1245 273 AIldYLADYVHIL 285
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-276 |
6.38e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRiTAGTVRIGekavtgldprvAIGFQEPRLLPWRTvadnvALG- 124
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID-----------GVSWNSVTLQTWRK-----AFGv 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 125 LPQ------GTKKSE-------GAASVARLLDLVGLGEYATHRPKE-----------ISGGMAQRVSLARALARNPGVLL 180
Cdd:TIGR01271 1297 IPQkvfifsGTFRKNldpyeqwSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 181 LDEPFGALDALTRINMQDLLldVHRQDPTTILLVTHDVEEALYLSDRVIVLGKDTPEAPAtIQRIVTvDRSH------PR 254
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTL--KQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS-IQKLLN-ETSLfkqamsAA 1452
|
250 260 270
....*....|....*....|....*....|....*..
gi 1091083680 255 DRAD---------------AEITALRSEllAELGVED 276
Cdd:TIGR01271 1453 DRLKlfplhrrnsskrkpqPKITALREE--AEEEVQN 1487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-217 |
7.12e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVgqSFPVPGGTHEVlRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPrvaigfQ 107
Cdd:PRK10522 323 LELRNV--TFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP------E 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 108 EPRLLpWRTVADNV-----ALGlPQGTKKSEgaASVARLLDLVGLGEYATHRPKEI-----SGGMAQRVSLARALARNPG 177
Cdd:PRK10522 394 DYRKL-FSAVFTDFhlfdqLLG-PEGKPANP--ALVEKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAEERD 469
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091083680 178 VLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVTHD 217
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
45-231 |
9.96e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGE----KAVTGLDPRVAIGF--QEPrLLPWRTVA 118
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSKIGVvsQDP-LLFSNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 119 DNVALGL--------------PQGTKKSEGAAS--------------VARLLDLVGL----GEYATHRPKEI-------- 158
Cdd:PTZ00265 478 NNIKYSLyslkdlealsnyynEDGNDSQENKNKrnscrakcagdlndMSNTTDSNELiemrKNYQTIKDSEVvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 159 -----------------------SGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVHRQDPTTILLVT 215
Cdd:PTZ00265 558 ihdfvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250
....*....|....*.
gi 1091083680 216 HDVEEALYlSDRVIVL 231
Cdd:PTZ00265 638 HRLSTIRY-ANTIFVL 652
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
141-233 |
1.08e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 141 LLDLVGLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDVhrQDPTTILLVTHDVee 220
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDL-- 271
|
90
....*....|....*.
gi 1091083680 221 AL--YLSDRV-IVLGK 233
Cdd:PRK13409 272 AVldYLADNVhIAYGE 287
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
47-231 |
1.65e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGLDPRVAI--GF----QEPR---LLPWRTV 117
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhGFalvtEERRstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 118 ADNVALGLPQGTKKSEGAASVARL-------LDLVGLgEYATHRPK--EISGGMAQRVSLARALARNPGVLLLDEPFGAL 188
Cdd:PRK10982 344 GFNSLISNIRNYKNKVGLLDNSRMksdtqwvIDSMRV-KTPGHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1091083680 189 DALTRINMQDLLLDVHRQDpTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKD-KGIIIISSEMPELLGITDRILVM 464
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
42-217 |
2.82e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 42 GTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEK-------------AVTGLDpRVAIGFQE 108
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALE-YVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 109 PRLLPWRTVADNV-----ALGLPQGTKKSEGAASV----ARLLDLVGLGEYATHRP-KEISGGMAQRVSLARALARNPGV 178
Cdd:PRK10636 91 YRQLEAQLHDANErndghAIATIHGKLDAIDAWTIrsraASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1091083680 179 LLLDEPFGALDALTRINMQDLLldvhRQDPTTILLVTHD 217
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHD 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
45-190 |
7.10e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGlnRITAGTVRiGEKAVTGLdPRVAIGF--------QEPRLLPWRT 116
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGF-PKKQETFarisgyceQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 117 VADNVA----LGLPQGTKKSEGAA---SVARLLDLVGLGEYATHRP--KEISGGMAQRVSLARALARNPGVLLLDEPFGA 187
Cdd:PLN03140 970 VRESLIysafLRLPKEVSKEEKMMfvdEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
...
gi 1091083680 188 LDA 190
Cdd:PLN03140 1050 LDA 1052
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
45-113 |
8.47e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 8.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 45 EVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLN--RITAGTVRIGEKAVTGLDPR------VAIGFQEPRLLP 113
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdragegIFMAFQYPVEIP 91
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
46-237 |
8.73e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.06 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGL-----NRITAGTVRIGEKAVTGLDPRVAIGFQEPRLLpwrtvADN 120
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMvdifdGKIVIDGIDISKLPLHTLRSRLSIILQDPILF-----SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 121 VALGLPQGTKKSEG----AASVARLLDLV-----GLGEYATHRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDAL 191
Cdd:cd03288 111 IRFNLDPECKCTDDrlweALEIAQLKNMVkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 192 TRINMQDLLLDVHRQdpTTILLVTHDVEEALYlSDRVIVLGK------DTPE 237
Cdd:cd03288 191 TENILQKVVMTAFAD--RTVVTIAHRVSTILD-ADLVLVLSRgilvecDTPE 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-96 |
1.06e-05 |
|
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: 46.33 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 28 LSFEGVGQSFPVPGGTHE-VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT 96
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-216 |
2.26e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 35 QSFPVPGGTHEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAA-----GLNRiTAGTVRIgEKAVTGLD---------- 99
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPK-NCQILHV-EQEVVGDDttalqcvlnt 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 100 --PRVAIGFQEPRLLPW-RTVADNVALGLPQGTKK--------SEGAASVARLLDLV--------------GLG---EYA 151
Cdd:PLN03073 259 diERTQLLEEEAQLVAQqRELEFETETGKGKGANKdgvdkdavSQRLEEIYKRLELIdaytaearaasilaGLSftpEMQ 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091083680 152 THRPKEISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLdvhrQDPTTILLVTH 216
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-231 |
8.03e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 31 EGVGQSFPvpgGThEVLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVT------GLDPRVAI 104
Cdd:PRK10982 2 SNISKSFP---GV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskeALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 105 GFQEPRLLPWRTVADNVALG--------LPQGTKKSEGAASVARL-LDLvglgeyathRPKE----ISGGMAQRVSLARA 171
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGryptkgmfVDQDKMYRDTKAIFDELdIDI---------DPRAkvatLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091083680 172 LARNPGVLLLDEPfgaLDALTRINMQDL--LLDVHRQDPTTILLVTHDVEEALYLSDRVIVL 231
Cdd:PRK10982 149 FSYNAKIVIMDEP---TSSLTEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
47-232 |
1.83e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.86 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 47 LRGVSFTAAPGEIISVIGSSGCGKSTL---LRAAAGLNRI-----TAGTVRIGE------KAVTGLDPRVAIGFQEPRLL 112
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdTIYAEGQRRYveslsAYARQFLGQmdkpdvDSIEGLSPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 113 PWRTVadnvalglpqGTKKS-----------EGAASVARLLDLVGLGEYATHRPKE-ISGGMAQRVSLARALARN-PGVL 179
Cdd:cd03270 91 PRSTV----------GTVTEiydylrllfarVGIRERLGFLVDVGLGYLTLSRSAPtLSGGEAQRIRLATQIGSGlTGVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091083680 180 -LLDEPFGAL---DALTRINmqdlLLDVHRQDPTTILLVTHDvEEALYLSDRVIVLG 232
Cdd:cd03270 161 yVLDEPSIGLhprDNDRLIE----TLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIG 212
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
41-233 |
2.00e-04 |
|
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: 40.81 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 41 GGTHEVLRGVSF-TAAPGEIISVIGSSGCGKSTLLRAAaglnritaGTVRIGEKAVTGLDPRVAIGFQEPrllpwrtvad 119
Cdd:cd03227 4 LGRFPSYFVPNDvTFGEGSLTIITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGVKAGCIVA---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 120 nvalglpqgtkksegAASVARLLDLVGLgeyathrpkeiSGGMAQRVSLARALA---RNPGVL-LLDEPFGALDALTRIN 195
Cdd:cd03227 66 ---------------AVSAELIFTRLQL-----------SGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 1091083680 196 MQDLLLDvHRQDPTTILLVTHDvEEALYLSDRVIVLGK 233
Cdd:cd03227 120 LAEAILE-HLVKGAQVIVITHL-PELAELADKLIHIKK 155
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-232 |
2.08e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 141 LLDlVGLGEYATHRPKE-ISGGMAQRVSLARAL-ARNPGVL-LLDEPFGAL---DAL----TRINMQDLlldvhrqdPTT 210
Cdd:TIGR00630 472 LID-VGLDYLSLSRAAGtLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLhqrDNRrlinTLKRLRDL--------GNT 542
|
90 100
....*....|....*....|..
gi 1091083680 211 ILLVTHDvEEALYLSDRVIVLG 232
Cdd:TIGR00630 543 LIVVEHD-EDTIRAADYVIDIG 563
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-216 |
3.00e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 46 VLRGVSFTAAPGEIISVIGSSGCGKSTLLRAAAGLNRITAGTVRIGEKAVTGL-DPRVA-IGFQ---------EPRLLPW 114
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIaKPYCTyIGHNlglklemtvFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 115 RTVADNVALglpqgtkkSEGAASVARLLDLVGLGEYAthrpkeISGGMAQRVSLARALARNPGVLLLDEPFGALDALTRI 194
Cdd:PRK13541 95 SEIYNSAET--------LYAAIHYFKLHDLLDEKCYS------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|..
gi 1091083680 195 NMQDLLLdVHRQDPTTILLVTH 216
Cdd:PRK13541 161 LLNNLIV-MKANSGGIVLLSSH 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
159-234 |
6.38e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 159 SGG------MAQRVSLARALARNPGVLLLDEPFGALD------ALTRInMQDLLLDVHRQdpttILLVTHDvEEALYLSD 226
Cdd:cd03240 117 SGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDeenieeSLAEI-IEERKSQKNFQ----LIVITHD-EELVDAAD 190
|
....*...
gi 1091083680 227 RVIVLGKD 234
Cdd:cd03240 191 HIYRVEKD 198
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
151-233 |
1.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091083680 151 ATHRPKEISGG------MAQRVSLARALARNPGVLLLDEPFGALDALTRINMQDLLLDV--HRQdpttILLVTHDVEEAL 222
Cdd:COG4717 552 RTRPVEELSRGtreqlyLALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELakGRQ----VIYFTCHEELVE 627
|
90
....*....|....
gi 1091083680 223 YLSD---RVIVLGK 233
Cdd:COG4717 628 LFQEegaHVIELES 641
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
59-101 |
2.99e-03 |
|
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.
Pssm-ID: 238984 [Multi-domain] Cd Length: 273 Bit Score: 38.47 E-value: 2.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091083680 59 IISVIGSSGCGKSTLLRaaaGLNRITAG---TV----------RIG--EKAVTGLDPR 101
Cdd:cd02026 1 IIGVAGDSGCGKSTFLR---RLTSLFGSdlvTViclddyhsldRKGrkETGITALDPR 55
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
133-184 |
6.41e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 6.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091083680 133 EGAASVARLLDL---VGLGEYATHRP-KEISGGMAQRVSLARALAR---NPGVLLLDEP 184
Cdd:cd03271 141 ENIPKIARKLQTlcdVGLGYIKLGQPaTTLSGGEAQRIKLAKELSKrstGKTLYILDEP 199
|
|
| |
