|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
3.06e-95 |
|
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: 279.36 E-value: 3.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGD----QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDRGVVF 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-DRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVLGNVLLGREFSGArykaklfgaARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGV---------PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRRdrpeekERYGATITKDI 235
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP------GRIVAEVEVDL 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-241 |
3.42e-94 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 278.13 E-value: 3.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY----GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDRGVVF 79
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-DRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:COG1116 87 QEPALLPWLTVLDNVALG---------LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERrrdRPeekerygATITKDIAIWP 239
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA---RP-------GRIVEEIDVDL 227
|
..
gi 499747244 240 PR 241
Cdd:COG1116 228 PR 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
8.22e-79 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 242.31 E-value: 8.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--V 78
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVgmV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVllgrEFsGARYKaklfGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:COG3842 83 FQDYALFPHLTVAENV----AF-GLRMR----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEE 223
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRieqvGTPEE 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-212 |
2.28e-74 |
|
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: 225.86 E-value: 2.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIgmVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03259 81 YALFPHLTVAENIAFG---------LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIA 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-212 |
3.01e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 213.70 E-value: 3.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------GV 77
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrrkvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFPHLTVLGNVLLGREfsgarykaKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPI--------KVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHEtQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVV 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-212 |
1.25e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 213.40 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--V 78
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIamV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREFsgarykAKLFGAARRNAIEEArqliAE-VGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKL------RKVPKAEIDRRVREA----AElLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIA 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-212 |
2.41e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 212.70 E-value: 2.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSeLKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD-GEPLPPEPGPDRGV-- 77
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgRDLFTNLPPRERRVgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFPHLTVLGNVLLG---REFSGARYKAKlfgaarrnaieeARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGlrvRPPSKAEIRAR------------VEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-218 |
3.83e-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: 205.03 E-value: 3.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI----VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ----GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfgaaRRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLAL 151
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVP---------KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFtLASRVVAFERRR 218
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-214 |
4.33e-66 |
|
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: 205.55 E-value: 4.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGREFsgarykAKLFGAARRNAIEEARQLiaeVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03300 81 YALFPHLTVFENIAFGLRL------KKLPKAEIKERVAEALDL---VQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-215 |
1.11e-65 |
|
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: 203.92 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------GV 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFPHLTVLGNVLLGrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA--------PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHEtQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-215 |
1.98e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 203.74 E-value: 1.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGD----QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ----GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfgaaRRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLAL 151
Cdd:COG1136 85 rrhiGFVFQFFNLLPELTALENVALPLLLAGVS---------RKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAfTLASRVVAFE 215
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLR 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-218 |
1.85e-64 |
|
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: 201.80 E-value: 1.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQ 80
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVgfVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVLLGREfsgARYKAKLFGAARRNaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLR---VKPRSERPPEAEIR--AKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-218 |
2.26e-64 |
|
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: 201.36 E-value: 2.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-------G 76
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrrriG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFPHLTVLGNVLLG-REFSgarykaKLfgaaRRNAIEE-ARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPlREHT------DL----SEAEIRElVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
2.36e-63 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 199.70 E-value: 2.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYG----DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDRG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFPHLTVLGNVLLGREFSGArykaklfGAARRNAIeeARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFGLRLRGV-------PKAERRAR--AEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLV 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
2.79e-63 |
|
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: 196.64 E-value: 2.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------GV 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplrrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFPHLTVLGNVLLGrefsgarykaklfgaarrnaieearqliaevglagsqdkypaqLSGGMQQRLALAQALIM 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-230 |
1.62e-62 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 196.56 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQRYS 83
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIgfVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTVLGNVLLGREFSgarykaKLFGAARRNAIEEARQLiaeVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIR------KHPKAKIKARVEELLEL---VQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEEKERYGAT 230
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKieqiGSPDEVYDHPAN 224
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-212 |
2.34e-61 |
|
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: 197.57 E-value: 2.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--GVVFQR 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRdyGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGreFSGARYKaklfgaaRRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:TIGR03265 85 YALFPNLTVADNIAYG--LKNRGMG-------RAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:TIGR03265 156 LLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIV 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-212 |
7.26e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.20 E-value: 7.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVllgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG1131 81 EPALYPDLTVRENL---------RFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-223 |
9.19e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 189.15 E-value: 9.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGD-QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GVVF 79
Cdd:COG1125 3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElRrriGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVLGNVLLgrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQ--DKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG1125 83 QQIGLFPHMTVAENIAT---------VPRLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEE 223
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRivqyDTPEE 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-218 |
2.69e-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: 185.78 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-------GVV 78
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlrrrmGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLG-REFSgaRYKAKLfgaarrnaIEE-ARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPlREHT--RLSEEE--------IREiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-212 |
3.37e-58 |
|
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: 184.77 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGREFSGARykaklfgaarRNAIEEARQLIAEV-GLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVP----------KDEIDERVREVAELlQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIA 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-218 |
2.07e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 182.94 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------- 75
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfgaaRRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL 155
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKS---------RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-212 |
2.57e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 180.72 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVleDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVsmLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGRefsgaRYKAKLfGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:COG3840 80 NNLFPHLTVAQNIGLGL-----RPGLKL-TAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-218 |
4.25e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 177.98 E-value: 4.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKieKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----- 75
Cdd:PRK09493 1 MIEFK--NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 -GVVFQRYSVFPHLTVLGNVLLGrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:PRK09493 79 aGMVFQQFYLFPHLTALENVMFG--------PLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETqMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-222 |
1.09e-54 |
|
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: 176.50 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDRGVVFQRYSVFPHLTVLGNVLLGR 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 99 EfsgaRYKAKLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAE 178
Cdd:TIGR01184 80 D----RVLPDLSKSERRAIVEEH---IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 179 IHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVA----------------FERRRDRPE 222
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMltngpaanigqilevpFPRPRDRLE 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-230 |
4.43e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 178.74 E-value: 4.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSeLKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--GVV 78
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRkvGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLG------REF-SGARYKAKlfgaarrnaieeARQLIAEVGLAGSQDKYPAQLSGGMQQRLAL 151
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltvlprRERpNAAAIKAK------------VTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER----RRDRPEEKERY 227
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQgnieQAGTPDQVWRE 227
|
...
gi 499747244 228 GAT 230
Cdd:PRK10851 228 PAT 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-212 |
5.15e-54 |
|
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: 175.18 E-value: 5.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGD-QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD--R--GVV 78
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRkiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLgrefsgaryKAKLFGAARRNAIEEARQLIAEVGL--AGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL---------VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIA 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-214 |
3.00e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 177.06 E-value: 3.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVntVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGrefsgARYKaKLFGAARRNAIEEARQLiaeVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK09452 95 YALFPHMTVFENVAFG-----LRMQ-KTPAAEITPRVMEALRM---VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-212 |
1.61e-52 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 171.81 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDRGVVFQRYS 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTVLGNVLLGREfsgarykakLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQ---------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELV 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
1.85e-52 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 171.40 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKiLLDGEPLPPEPGPDRGVVFQRYS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTVLGNVLLGrefsgarykakLFGAARrnaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK11247 92 LLPWKKVIDNVGLG-----------LKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
2.67e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.65 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgEPLPPEPGPDRGVVFQ 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-GKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSV---FPhLTVLGNVLLGRefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG1121 83 RAEVdwdFP-ITVRDVVLMGR-----YGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-218 |
5.01e-52 |
|
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: 168.80 E-value: 5.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQ--IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVV 78
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQrysvFP-----HLTVLGNVLLGREfsgarykakLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQ 153
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLE---------NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-218 |
9.59e-52 |
|
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: 168.66 E-value: 9.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI-VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVV 78
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQrysvFP-----HLTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQ 153
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFG---------PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-212 |
1.01e-51 |
|
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: 176.25 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY-----GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ----GVVFQ--RYSVFPHLTVLGNVLLGrefsgarykAKLFGAARRNAIEE-ARQLIAEVGL-AGSQDKYPAQLSGGMQQ 147
Cdd:COG1123 341 rrrvQMVFQdpYSSLNPRMTVGDIIAEP---------LRLHGLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 148 RLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-215 |
1.69e-50 |
|
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: 166.13 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYG----DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRY--SVFPHLTV---LGNVLlgrefsgarykaKLFGaaRRNAIEEARQLIAEVGLAGSQ-DKYPAQLSGGMQQRL 149
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVdriLAEPL------------RIHG--LPDREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQ 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-246 |
3.48e-50 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 168.36 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKieKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQ 80
Cdd:PRK11432 8 VLK--NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIcmVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVllgrefsgaRYKAKLFGAARrnaiEEARQLIAE----VGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:PRK11432 86 SYALFPHMSLGENV---------GYGLKMLGVPK----EERKQRVKEalelVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER----RRDRPEE-----KERY 227
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKgkimQIGSPQElyrqpASRF 232
|
250
....*....|....*....
gi 499747244 228 GATITKDIAIWPPRLAGQS 246
Cdd:PRK11432 233 MASFMGDANIFPATLSGDY 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-216 |
4.99e-50 |
|
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: 165.21 E-value: 4.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVV-- 78
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIArt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREF-SGARYKAKLFG-----AARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALA 152
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAAHArLGRGLLAALLRlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-217 |
5.97e-50 |
|
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: 163.47 E-value: 5.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDRGVVFQRYSV 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-RIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 85 ---FPhLTVLGNVLLGRefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03235 80 drdFP-ISVRDVVLMGL-----YGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERR 217
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-211 |
1.49e-49 |
|
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: 164.35 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI---------------VLEDVSLTVASRA----------FVaLVGPSGCGKTTFLRMLLGQEQPTKG 58
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkskeeILKKTGQTVGVNDvsldvregeiFV-IMGLSGSGKSTLLRCINRLIEPTSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 59 KILLDGEPLPPEPGPD----R----GVVFQRYSVFPHLTVLGNVLLGREfsgarykakLFGAARRNAIEEARQLIAEVGL 130
Cdd:cd03294 80 KVLIDGQDIAAMSRKElrelRrkkiSMVFQSFALLPHRTVLENVAFGLE---------VQGVPRAEREERAAEALELVGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 131 AGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASR 210
Cdd:cd03294 151 EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDR 230
|
.
gi 499747244 211 V 211
Cdd:cd03294 231 I 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-216 |
2.44e-49 |
|
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: 162.61 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL---DGEPLPPEPGPDRGVV-- 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgeDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREF-SGARYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQArTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-213 |
3.38e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 162.92 E-value: 3.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------- 75
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrrri 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGR--EFSGARYkakLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQ 153
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgRTSTWRS---LLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVA 213
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
4.45e-49 |
|
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: 161.96 E-value: 4.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML-----LGQEQPTKGKILLDGEPLPPEPGPD---- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 --RGVVFQRYSVFPhLTVLGNVLLGrefsgarykAKLFGAARRNAIEE-ARQLIAEVGLAG--SQDKYPAQLSGGMQQRL 149
Cdd:cd03260 81 rrVGMVFQKPNPFP-GSIYDNVAYG---------LRLHGIKLKEELDErVEEALRKAALWDevKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-223 |
5.28e-49 |
|
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: 164.59 E-value: 5.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 34 LVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--GVVFQRYSVFPHLTVLGNVllgrefsgaRYKAKLFG 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhiNMVFQSYALFPHMTVEENV---------AFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 112 AARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQ 191
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 499747244 192 MTVVMVTHDMREAFTLASRVVAFERRR----DRPEE 223
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKiaqiGTPEE 187
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
1.03e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.84 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI------------LLDGEPLP 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 69 PEPGPDRGVVFQRYSVFPHLTVLGNVLLGrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQR 148
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEG--------PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 149 LALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-218 |
1.34e-48 |
|
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: 160.15 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVaSRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI------LLDGEPLPPEPGPDR--GVVFQRYSVFPHLTVLG 92
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQQRkiGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLGrefsgarykakLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03297 95 NLAFG-----------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 173 PGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-213 |
1.79e-48 |
|
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: 160.98 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVF 79
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarriAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVLGNVLLGRefsgARYKaKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:COG1120 82 QEPPAPFGLTVRELVALGR----YPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVA 213
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-212 |
2.23e-48 |
|
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: 160.19 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDqIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--GVVFQR 81
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRdiSYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVllgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03299 80 YALFPHMTVYKNI---------AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVA 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
3.82e-48 |
|
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: 157.56 E-value: 3.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVllgrefsgarykaklfgaarrnaieearqliaevglagsqdkypaQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03230 81 EPSLYENLTVRENL---------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVA 166
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-218 |
1.07e-47 |
|
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: 158.04 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVleDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVsmLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGREfSGARYKAKlfgaaRRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLS-PGLKLTAE-----DRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-218 |
3.45e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.48 E-value: 3.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSeLKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL----------DGEPLPPE 70
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 71 PGPDRGVVFQRYSVFPHLTVLGNVLlgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLA 150
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTVQQNLI--------EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 151 LAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-223 |
1.99e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 159.23 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQR 81
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPInmMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGREfsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQdkyPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLK------QDKLPKAEIASRVNEMLGLVHMQEFAKRK---PHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEE 223
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvqiGEPEE 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
2.17e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.56 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSeLKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD----------GEPLPPE 70
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsqkpSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 71 PGPDRGVVFQRYSVFPHLTVLGNVLlgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLA 150
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHLTVMENLI--------EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 151 LAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-212 |
3.77e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.34 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLR---MLlgqEQPTKGKILLD-------GEPLPPEPGP 73
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRcinLL---ETPDSGEIRVGgeeirlkPDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 74 DR----------GVVFQRYSVFPHLTVLGNVLLGrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSG 143
Cdd:COG4598 86 DRrqlqrirtrlGMVFQSFNLWSHMTVLENVIEA--------PVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 144 GMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHEtQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-212 |
4.87e-46 |
|
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: 154.20 E-value: 4.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI----VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ---GVVFQR-YSVF-PHLTVLGNVLLGREFSGARYKAKlfgAARRNAIEEARQliaeVGLAGSQ-DKYPAQLSGGMQQRL 149
Cdd:cd03257 82 keiQMVFQDpMSSLnPRMTIGEQIAEPLRIHGKLSKKE---ARKEAVLLLLVG----VGLPEEVlNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-212 |
5.66e-46 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 157.71 E-value: 5.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 11 KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------GVVFQRY 82
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrrkkiGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHLTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR01186 81 ALFPHMTILQNTSLG---------PELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIV 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-215 |
7.57e-46 |
|
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: 157.18 E-value: 7.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI------LLDGEPLPPEPGPDR--GVVFQRYSVFPHLTVLG 92
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevLQDSARGIFLPPHRRriGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLGREFSGArykaklfgAARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:COG4148 97 NLLYGRKRAPR--------AERRISFDE---VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 173 PGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLE 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-210 |
1.01e-45 |
|
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: 153.36 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------GVVFQRYSVFPHLT 89
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrarhvGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGREFSGarykaklfgaaRRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:COG4181 107 ALENVMLPLELAG-----------RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMReaftLASR 210
Cdd:COG4181 176 NLDAATGEQIIDLLFELNRERGTTLVLVTHDPA----LAAR 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
2.04e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD--RGV--VF 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVayVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRySVFPHLTVLGNVLLGREFSGARYKaklfgaarrnaIEEARQLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMK 158
Cdd:COG4619 81 QE-PALWGGTVRDNLPFPFQLRERKFD-----------RERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-212 |
4.43e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 151.93 E-value: 4.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQ 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqiGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVllgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG4555 82 ERGLYDRLTVRENI---------RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-211 |
1.33e-44 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 153.69 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKV---WKEYGdqivLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--V 78
Cdd:NF040840 2 IRIENLskdWKEFK----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIayV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREFSGARykaklfgaarRNAIEEARQLIAEV-GLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:NF040840 78 YQNYMLFPHKTVFENIAFGLKLRKVP----------KEEIERKVKEIMELlGISHLLHRKPRTLSGGEQQRVALARALII 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRV 211
Cdd:NF040840 148 EPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRV 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-215 |
1.70e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 154.03 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--V 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREFSGARyKAKLfgAARRNAIEEARQLiaevglAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAK-KEEI--NQRVNQVAEVLQL------AHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 159 PKVLLLDEPFGALDPGI----RAEIHTLMKRLwhetQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALrvqmRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLD 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-219 |
4.02e-44 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 148.40 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP---TKGKILLDGEPLPPEPGPDR--GVV 78
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRriGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGrefsgarYKAKLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFA-------LPPTIGRAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAfTLASRVVAFERRRD 219
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDLGNWQH 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-212 |
5.76e-44 |
|
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: 155.83 E-value: 5.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY--GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPT---KGKILLDGEPLPPEPGPDRG-- 76
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 --VVFQ--RYSVFPhLTVLGNVLLGREfsgarykakLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALA 152
Cdd:COG1123 85 igMVFQdpMTQLNP-VTVGDQIAEALE---------NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-218 |
6.16e-44 |
|
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: 148.88 E-value: 6.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQ----IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ---GVVFQRYSVFPHLTVLGNVLlgrefsgarYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALA 152
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVA---------LPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-211 |
8.90e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 152.56 E-value: 8.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQI---------------VLE---------DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPT 56
Cdd:COG4175 1 MPKIEVRNLYKIFGKRPeralklldqgkskdeILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 57 KGKILLDGEPLPPEPGPD----R----GVVFQRYSVFPHLTVLGNVLLGREFSGArykaklfGAARRNAIeeARQLIAEV 128
Cdd:COG4175 81 AGEVLIDGEDITKLSKKElrelRrkkmSMVFQHFALLPHRTVLENVAFGLEIQGV-------PKAERRER--AREALELV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 129 GLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLA 208
Cdd:COG4175 152 GLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLG 231
|
...
gi 499747244 209 SRV 211
Cdd:COG4175 232 DRI 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-200 |
1.14e-43 |
|
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: 147.24 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQ 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVllgrefsgaRYKAKLFGAARRNaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG4133 83 ADGLKPELTVRENL---------RFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRlWHETQMTVVMVTHD 200
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-213 |
1.70e-43 |
|
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: 148.10 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQ-IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD----R--- 75
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSGARYKAkLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRS-LFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVA 213
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVG 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-216 |
2.58e-43 |
|
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: 148.37 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 16 QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-------GVVFQrysvFPH- 87
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkvGLVFQ----FPEh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 ----LTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR04521 94 qlfeETVYKDIAFG---------PKNLGLSEEEAEERVKEALELVGLDEEYlERSPFELSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-218 |
1.04e-42 |
|
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: 143.15 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpdrgvvfqrysv 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 85 fphltvlgnvllGREFSgarykaklfgaarRNAIEEARQLIAEVGlagsqdkypaQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:cd00267 60 ------------GKDIA-------------KLPLEELRRRIGYVP----------QLSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 165 DEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-216 |
3.13e-42 |
|
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: 143.70 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 7 EKVWKEYGDQIV-LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGP-------DRGVV 78
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipylrrKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREFSGArykaklfgaARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGV---------PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-214 |
3.80e-42 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 144.75 E-value: 3.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML-----LGQEQPTKGKILL------DGEPLPPEPG 72
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFdgqdiyDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 73 PDRGVVFQRYSVFPhLTVLGNVLLGREFSGARYKAKLFGAARRNAIEEArqLIAEVglAGSQDKYPAQLSGGMQQRLALA 152
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAA--LWDEV--KDRLHDSALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFF 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-213 |
7.84e-42 |
|
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: 143.59 E-value: 7.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI-VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------- 75
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGReFSGARYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGR-LGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVA 213
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVG 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
1.46e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.14 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV-- 77
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFPHLTVLGNVLLG---REFSGARYKAKLFGAARrnaIEEARQLIaevglagsqDKYPAQLSGGMQQRLALAQA 154
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGlkiRGMPKAEIEERVAEAAR---ILELEPLL---------DRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRA----EIHTLMKRLwhetQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRL----KTTSLYVTHDQVEAMTLADRVV 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-201 |
2.52e-41 |
|
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: 141.21 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGP--------DRGV 77
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFPHLTVLGNVLLGREFSgarykaKLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYK------KLSKKEKREKKKEA---LEKVGLNLKLKQKIYELSGGEQQRVALARAILK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDM 201
Cdd:TIGR03608 152 PPPLILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP 194
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-218 |
5.45e-41 |
|
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: 140.46 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD----R--- 75
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllRrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfgaarRNAIEEARQLIAE-VGLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKK----------EREIQRRVGAALRqVGLEHKADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-201 |
9.65e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 143.29 E-value: 9.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY----GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ---GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfGAARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALA 152
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVP------KAEIRKRVAE---LLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEM 201
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
1.09e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 137.78 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRYSVFPHLTVLGNV 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 95 LLGREFSGARYKAKLfgaarrnaiEEARQLIAEVGLAG----SQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:pfam00005 81 RLGLLLKGLSKREKD---------ARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-218 |
7.04e-40 |
|
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: 137.69 E-value: 7.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 23 SLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQRYSVFPHLTVLGNVLLGref 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVsmLFQENNLFAHLTVRQNIGLG--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 101 sgarykakLFGAARRNAIEEAR--QLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAE 178
Cdd:TIGR01277 95 --------LHPGLKLNAEQQEKvvDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 179 IHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-212 |
2.61e-39 |
|
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: 136.48 E-value: 2.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGD--QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVV 78
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVllgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03263 81 PQFDALFDELTVREHL---------RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTHDMREAFTLASRVV 212
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIA 203
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-212 |
3.84e-39 |
|
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: 135.78 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVaSRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGVVF---Q 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVlgnvllgREFsgARYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03264 80 EFGVYPNFTV-------REF--LDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTHDMREAFTLASRVV 212
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVA 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-218 |
4.42e-39 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 134.49 E-value: 4.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpdrgvvfqrysv 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 85 fphltvlgnvllGREFsgARYKAKLFgaARRNAIeeARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:cd03214 60 ------------GKDL--ASLSPKEL--ARKIAY--VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 165 DEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-223 |
6.53e-39 |
|
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: 135.58 E-value: 6.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL---LDGEPLPPEPGPDRGVVFQRY 82
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvagHDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHLTVLGNVLLgrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03265 83 SVDDELTGWENLYI---------HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEE 223
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRiiaeGTPEE 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
2.41e-38 |
|
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: 133.50 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--GVVFQR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRriGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTvlgnvllGREFsgARYKAKLFGaARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03268 81 PGFYPNLT-------AREN--LRLLARLLG-IRKKRIDE---VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 162 LLLDEPFGALDP-GIrAEIHTLMkRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03268 148 LILDEPTNGLDPdGI-KELRELI-LSLRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-214 |
1.27e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.24 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML--LGQEQP---TKGKILLDgeplppepgpDR------------ 75
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLD----------GEdiydpdvdvvel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ----GVVFQRYSVFPHlTVLGNVLLGREFSGARYKAKLfgaarRNAIEEA-RQ--LIAEVG--LagsqDKYPAQLSGGMQ 146
Cdd:COG1117 91 rrrvGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSEL-----DEIVEESlRKaaLWDEVKdrL----KKSALGLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 147 QRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREaftlASRV---VAF 214
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQ----AARVsdyTAF 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-212 |
3.40e-37 |
|
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: 133.64 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY----GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP---TKGKILLDGEPLPPEPGPD-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 --RG----VVFQR-YSVF-PHLTV---LGNVLLGREfsgarykaklfGAARRNAIEEARQLIAEVGLAGSQ---DKYPAQ 140
Cdd:COG0444 82 kiRGreiqMIFQDpMTSLnPVMTVgdqIAEPLRIHG-----------GLSKAEARERAIELLERVGLPDPErrlDRYPHE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-212 |
4.04e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 131.24 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 23 SLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV--VFQRYSVFPHLTVLGNVLLGREF 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVsmLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 101 SgarykAKLFGAARRNAIEEARQliaeVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIH 180
Cdd:PRK10771 99 G-----LKLNAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190
....*....|....*....|....*....|..
gi 499747244 181 TLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSL 201
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
7-223 |
8.74e-37 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 134.13 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 7 EKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL-DGEPLPPEPGPDR---------- 75
Cdd:TIGR03415 28 EEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkDGDGSVDVANCDAatlrrlrthr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 -GVVFQRYSVFPHLTVLGNVLLGREFSGArykAKlfgAARRNAIEEARQLiaeVGLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:TIGR03415 108 vSMVFQQFALLPWRTVEENVAFGLEMQGM---PK---AERRKRVDEQLEL---VGLAQWADRKPGELSGGMQQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEE 223
Cdd:TIGR03415 179 FATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRiiqhGTPEE 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-212 |
1.29e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.47 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSE--LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---- 74
Cdd:PRK10619 1 MSEnkLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 -------------RGVVFQRYSVFPHLTVLGNVLlgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAG-SQDKYPAQ 140
Cdd:PRK10619 81 vadknqlrllrtrLTMVFQHFNLWSHMTVLENVM--------EAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVV 212
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVI 223
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
18-215 |
1.34e-36 |
|
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: 129.37 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKG--KIL---LDGEPLPPEPGPDR--GVVFQRYSVFPHLTV 90
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGslKVLgqeLHGASKKQLVQLRRriGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLGREFSGarykaklfGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:TIGR02982 100 RQNVQMALELQP--------NLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499747244 171 LDPGIRAEIHTLMKRLWHETQMTVVMVTHDMReAFTLASRVVAFE 215
Cdd:TIGR02982 172 LDSKSGRDVVELMQKLAKEQGCTILMVTHDNR-ILDVADRILQME 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-218 |
2.85e-36 |
|
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: 132.16 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL------DGEPLPPEPGPDR--GVVFQRYSVFPHLTVLG 92
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfDSRKGIFLPPEKRriGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLGREFSGARYkaklfgaarRNAIEEArqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:TIGR02142 95 NLRYGMKRARPSE---------RRISFER--VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 173 PGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-216 |
5.88e-36 |
|
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: 127.94 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-----GVV 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGrefsgarykaklfgaARRNAIEEARQLIAEV------------GLAGsqdkypaQLSGGMQ 146
Cdd:cd03224 81 PEGRRIFPELTVEENLLLG---------------AYARRRAKRKARLERVyelfprlkerrkQLAG-------TLSGGEQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 147 QRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLER 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-218 |
4.94e-35 |
|
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: 123.65 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGD--QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GV 77
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFpHLTVLGNVllgrefsgarykaklfgaarrnaieearqliaevglagsqdkypaqLSGGMQQRLALAQALIM 157
Cdd:cd03228 81 VPQDPFLF-SGTIRENI----------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMrEAFTLASRVVAFERRR 218
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-216 |
5.76e-35 |
|
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: 126.39 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY--GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPpepgpDR------ 75
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL-----DEenlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ----GVVFQRysvfPH-----LTVLGNVLLGREFSGARYkaklfgaarrnaiEEARQLIAE----VGLAGSQDKYPAQLS 142
Cdd:TIGR04520 76 rkkvGMVFQN----PDnqfvgATVEDDVAFGLENLGVPR-------------EEMRKRVDEalklVGMEDFRDREPHLLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 143 GGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAfTLASRVVAFER 216
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNK 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-216 |
4.36e-34 |
|
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: 130.34 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYGDQ--IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----G 76
Cdd:COG2274 473 DIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrrqiG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFpHLTVLGNVLLGREFSGaryKAKLFGAARR-NAIEEARQL-------IAEVGlagsqdkypAQLSGGMQQR 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDPDAT---DEEIIEAARLaGLHDFIEALpmgydtvVGEGG---------SNLSGGQRQR 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 149 LALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHetQMTVVMVTHDMrEAFTLASRVVAFER 216
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDK 684
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-211 |
6.17e-34 |
|
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: 122.65 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVF- 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 -QRYSVFPHLTVLGNVLLGREFsgarykaklFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEI---------RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRV 211
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRA 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
7.35e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.36 E-value: 7.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYG-----DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-- 75
Cdd:PRK13634 2 DITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ------GVVFQrysvFPHL-----TVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGS-QDKYPAQLSG 143
Cdd:PRK13634 82 plrkkvGIVFQ----FPEHqlfeeTVEKDICFG---------PMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 144 GMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER----RRD 219
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKgtvfLQG 228
|
....
gi 499747244 220 RPEE 223
Cdd:PRK13634 229 TPRE 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-216 |
1.05e-33 |
|
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: 122.40 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GV 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VF--QRYSVFPHLTVLGNVLLGrefsgarykaklfgAARRNAIEEARQLIAEV------------GLAGsqdkypaQLSG 143
Cdd:COG0410 81 GYvpEGRRIFPSLTVEENLLLG--------------AYARRDRAEVRADLERVyelfprlkerrrQRAG-------TLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 144 GMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLER 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-230 |
4.06e-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: 122.50 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 11 KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL---LDGEPLPPEPGPDRGVVFQRYSVFPH 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARvagYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 LTVLGNVLLgrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:TIGR01188 81 LTGRENLEM---------MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 168 FGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEE-KERYGAT 230
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRiiaeGTPEElKRRLGKD 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-212 |
6.87e-33 |
|
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: 119.31 E-value: 6.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGVVFQRYS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTVLGNVLlgrefsgarYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03269 81 LYPKMKVIDQLV---------YLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 164 LDEPFGALDPgIRAEihtLMKRLWHETQ---MTVVMVTHDMREAFTLASRVV 212
Cdd:cd03269 152 LDEPFSGLDP-VNVE---LLKDVIRELAragKTVILSTHQMELVEELCDRVL 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-215 |
1.32e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.22 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-------- 75
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrkki 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSGarykaklFGAARRNaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAG-------INAEERR--EKALDALRQVGLENYAHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-201 |
6.57e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 6.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELK-IEKVWKEYGDQIV-LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---- 74
Cdd:PRK11153 1 MIELKnISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 R---GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfgaarRNAIEeAR--QLIAEVGLAGSQDKYPAQLSGGMQQRL 149
Cdd:PRK11153 81 RrqiGMIFQHFNLLSSRTVFDNVALPLELAGTP----------KAEIK-ARvtELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEM 201
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-204 |
6.87e-32 |
|
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: 117.07 E-value: 6.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQ----IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---- 75
Cdd:TIGR02211 2 LKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ----GVVFQRYSVFPHLTVLGNV---LLGREFSgarykaklfgaaRRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQR 148
Cdd:TIGR02211 82 nkklGFIYQFHHLLPDFTALENVampLLIGKKS------------VKEAKERAYEMLEKVGLEHRINHRPSELSGGERQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 149 LALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREA 204
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.59e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 118.29 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-------RG 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 vvfqrysVFPHLTVlGNVLLgrefsgarYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:COG4152 82 -------LYPKMKV-GEQLV--------YLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 157 MKPKVLLLDEPFGALDP----GIRAEIHTLMKRlwhetQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4152 146 HDPELLILDEPFSGLDPvnveLLKDVIRELAAK-----GTTVIFSSHQMELVEELCDRIV 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
2.10e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.28 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpDRGV--- 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD----------GEDIthl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 -VFQR------Y-----SVFPHLTVLGNVLLGREFsgaRYKAKlfgAARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGM 145
Cdd:COG1137 71 pMHKRarlgigYlpqeaSIFRKLTVEDNILAVLEL---RKLSK---KEREERLEE---LLEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 146 QQRLALAQALIMKPKVLLLDEPFGALDP----GIRAEIHTLMKR 185
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPiavaDIQKIIRHLKER 185
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-218 |
4.32e-31 |
|
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: 121.02 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 2 SELKIEKVWKEYGD-QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----G 76
Cdd:COG4988 335 PSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWrrqiA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRySVFPHLTVLGNVLLGREfsgarykaklfgAARRNAIEEArqlIAEVGLAGSQDKYP-----------AQLSGGM 145
Cdd:COG4988 415 WVPQN-PYLFAGTIRENLRLGRP------------DASDEELEAA---LEAAGLDEFVAALPdgldtplgeggRGLSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTHDMREAfTLASRVVAFERRR 218
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRILVLDDGR 548
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-219 |
6.37e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.12 E-value: 6.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---RGV--V 78
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIaiI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREFSGarykaklFGAARRNAI-EEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRR-------GGLIDWRAMrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 158 KPKVLLLDEPFGALDpgiRAEIHTL---MKRLwHETQMTVVMVTHDMREAFTLASRVVAFerrRD 219
Cdd:COG1129 158 DARVLILDEPTASLT---EREVERLfriIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL---RD 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-212 |
6.92e-31 |
|
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: 114.28 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQI-VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-GVVFQ--R 81
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSiGYVMQdvD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHlTVLGNVLLGREFSGARYkaklfgaarrnaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03226 82 YQLFTD-SVREELLLGLKELDAGN-------------EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVV 212
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-204 |
8.66e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 8.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppEPGPDRGVVF--QRYSV---FPh 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYvpQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 LTVLGNVLLGRefSGARYKAKLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:NF040873 72 LTVRDLVAMGR--WARRGLWRRLTRDDRAAVDDA---LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 499747244 168 FGALDPGIRAEIHTLMKRlWHETQMTVVMVTHDMREA 204
Cdd:NF040873 147 TTGLDAESRERIIALLAE-EHARGATVVVVTHDLELV 182
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-218 |
1.03e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 119.87 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRysvfPHL- 88
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrrriAVVPQR----PHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 89 --TVLGNVLLGREfsgarykaklfGAARrnaiEEARQLIAEVGLAGSQDKYP-----------AQLSGGMQQRLALAQAL 155
Cdd:COG4987 422 dtTLRENLRLARP-----------DATD----EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHEtqMTVVMVTHDMREAfTLASRVVAFERRR 218
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGL-ERMDRILVLEDGR 546
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-201 |
1.05e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.75 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-----RGV--VFQR-YSVF-PHLT 89
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMqmVFQDpYASLnPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 V---LGNVLlgrefsgarykaKLFGAARRNAIEE-ARQLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:COG4608 114 VgdiIAEPL------------RIHGLASKAERRErVAELLELVGLRPEHaDRYPHEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 499747244 165 DEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:COG4608 182 DEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDL 218
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-208 |
1.12e-30 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 114.03 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGVVFQRYS 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTVLGNV-----LLGREFSgarykaklfgaarrnAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:TIGR03740 81 LYENLTARENLkvhttLLGLPDS---------------RIDE---VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 159 PKVLLLDEPFGALDP-GIRaEIHTLMkRLWHETQMTVVMVTHDMREAFTLA 208
Cdd:TIGR03740 143 PKLLILDEPTNGLDPiGIQ-ELRELI-RSFPEQGITVILSSHILSEVQQLA 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-214 |
3.10e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 113.78 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML-----LGQEQPTKGKILL------DGEPLPPEPGPDRGVVFQR 81
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLfgrniySPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGREFSGARYKAKLFGAARRNAIEEArQLIAEVglAGSQDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKA-ALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 162 LLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAfTLASRVVAF 214
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQA-ARVSDYVAF 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-212 |
4.66e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.99 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------GVVFQ--RYSVFPHlTV 90
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirkkvGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 lgnvllgrefsgarYKAKLFGAARRNAIEE-----ARQLIAEVGLA--GSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK13637 102 --------------EKDIAFGPINLGLSEEeienrVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-199 |
5.66e-30 |
|
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: 112.87 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKG---KILldgeplppepgpdrGVVFQ 80
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--------------GERRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVF------------------PHLTVLgNVLLgrefSGARYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLS 142
Cdd:COG1119 70 GEDVWelrkriglvspalqlrfpRDETVL-DVVL----SGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 143 GGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTH 199
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-218 |
9.23e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.54 E-value: 9.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIE--KVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--- 75
Cdd:PRK13536 37 MSTVAIDlaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARari 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLL-GREFsgaRYKAKLFGAARRNAIEEARqliaevgLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVfGRYF---GMSTREIEAVIPSLLEFAR-------LESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRaeiHTLMKRLWH--ETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHAR---HLIWERLRSllARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-212 |
1.20e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.66 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---RGV--V 78
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIgmV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREfsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLE------PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 159 PKVLLLDEPFGALDPgirAEIHTL---MKRLWHEtQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG3845 160 ARILILDEPTAVLTP---QEADELfeiLRRLAAE-GKSIIFITHKLREVMAIADRVT 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
1.45e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 112.44 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSEL----KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML-----LGQEQPTKGKI------LLDGE 65
Cdd:PRK14258 1 MSKLipaiKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVeffnqnIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 66 PLPPEPGPDRGVVFQRYSVFPhLTVLGNVLLGREFSGARYKAKLFGAARrNAIEEArQLIAEVglAGSQDKYPAQLSGGM 145
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVE-SALKDA-DLWDEI--KHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRRDRPEEKE 225
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
....*
gi 499747244 226 RYGAT 230
Cdd:PRK14258 236 EFGLT 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-212 |
1.55e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 17 IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpDRGV----VFQRYS----VF--- 85
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID----------GKDVtklpEYKRAKyigrVFqdp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 -----PHLTVLGNVLLgrefsgARYKAKLFG---AARRNAIEEARQLIAEVGLaGSQDKYPAQ---LSGGMQQRLALAQA 154
Cdd:COG1101 90 mmgtaPSMTIEENLAL------AYRRGKRRGlrrGLTKKRRELFRELLATLGL-GLENRLDTKvglLSGGQRQALSLLMA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-200 |
3.20e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.98 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD----RGVVFQRYSV-FPh 87
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAVLPQHSSLaFP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 LTVLGNVLLGREfsgarykAKLFGAARRNAIeeARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI-------MKPK 160
Cdd:COG4559 90 FTVEEVVALGRA-------PHGSSAAQDRQI--VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPgirAEIHTLMK--RLWHETQMTVVMVTHD 200
Cdd:COG4559 161 WLFLDEPTSALDL---AHQHAVLRlaRQLARRGGGVVAVLHD 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-212 |
3.64e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.55 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQeQPTKGKILLDGEPLPPEPGPDR-------GVVFQR-YSVF-PHLT 89
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALrplrrrmQVVFQDpFGSLsPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VL-----GNVLLGREFSGArykaklfgaARRNAIEEArqlIAEVGL-AGSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:COG4172 381 VGqiiaeGLRVHGPGLSAA---------ERRARVAEA---LEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVM 497
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-218 |
3.84e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------GVVFQrysvFPHL-- 88
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikqirkkvGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 89 ---TVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:PRK13649 99 feeTVLKDVAFG---------PQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 165 DEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-212 |
3.88e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD----RGVVFQRYSV-FPh 87
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrRAVLPQHSSLsFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 LTVLGNVLLGREFSGARYKAKlfgaarRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI------MKPKV 161
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAED------DALVAAA---LAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 162 LLLDEPFGALDpgIRAEIHTL--MKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK13548 162 LLLDEPTSALD--LAHQHHVLrlARQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-200 |
5.19e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPpepgpdrGVVFQRYSVF 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRI-------GYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 PHLTVLGNVLLGR--------------------EFSGARYkAKLFGA-ARRNAIE---EARQLIAEVGLAGSQ-DKYPAQ 140
Cdd:COG0488 74 DDLTVLDTVLDGDaelraleaeleeleaklaepDEDLERL-AELQEEfEALGGWEaeaRAEEILSGLGFPEEDlDRPVSE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgiraeIHTLmkrLWHET-----QMTVVMVTHD 200
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESI---EWLEEflknyPGTVLVVSHD 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-210 |
5.85e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.87 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL--------DGEPLPPEPGPDRGVVFQRYSVFPHLT 89
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLgrefsgaryKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK10584 105 ALENVEL---------PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMReaftLASR 210
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQ----LAAR 212
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-212 |
6.19e-29 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 110.67 E-value: 6.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGD----QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPE--------- 70
Cdd:COG4107 9 LSVRGLSKRYGPgcgtVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDGGPRdlfalseae 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 71 ----PGPDRGVVFQRysvfPHL------TVLGNV---LLGrefSGARYkaklFGAARrnaiEEARQLIAEVGLAGSQ-DK 136
Cdd:COG4107 89 rrrlRRTDWGMVYQN----PRDglrmdvSAGGNIaerLMA---AGERH----YGDIR----ARALEWLERVEIPLERiDD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 137 YPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4107 154 LPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTM 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-214 |
7.70e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML-----LGQEQPTKGKILLDGEPLPPEPGPD- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 -RGV--VFQRYSVFPHLTVLGNVLLGREFSG-ARYKAKLFgAARRNAIEEArQLIAEVglAGSQDKYPAQLSGGMQQRLA 150
Cdd:PRK14247 81 rRRVqmVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQ-ERVRWALEKA-QLWDEV--KDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 151 LAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAFTLaSRVVAF 214
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARI-SDYVAF 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-218 |
1.07e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 108.61 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQ----IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---G 76
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFPHLTVLGNVllgrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:cd03266 82 FVSDSTGLYDRLTARENL---------EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-199 |
1.57e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.72 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GV 77
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRrqiGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFpHLTVLGNVLLGREfsGARyKAKLFGAARR-NAIEEARQLI----AEVGLAGSqdkypaQLSGGMQQRLALA 152
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGRP--DAT-DEEVEEAAKAaQAHEFIEALPdgydTVVGERGV------NLSGGQRQRIAIA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 153 QALIMKPKVLLLDEPFGALDPG----IRAEIHTLMKrlwhetQMTVVMVTH 199
Cdd:COG1132 489 RALLKDPPILILDEATSALDTEtealIQEALERLMK------GRTTIVIAH 533
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-212 |
2.17e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.39 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEY---------GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 72 GPDRG-------VVFQRY--SVFPHLTVlGNVLlgREfsGARYKAKLFGAARRnaiEEARQLIAEVGLAGSQ-DKYPAQL 141
Cdd:PRK10419 81 RAQRKafrrdiqMVFQDSisAVNPRKTV-REII--RE--PLRHLLSLDKAERL---ARASEMLRAVDLDDSVlDKRPPQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 142 SGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-200 |
2.27e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 113.67 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGK--------ILLDGEPLPPEPGPDRGVVFQRYSVFPHLT 89
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGREFSGARYKAKLfgaarrnaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRL---------LRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 170 ALDPGIRAEIHTLMKRLwHETQMTVVMVTHD 200
Cdd:PRK10535 174 ALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-274 |
3.66e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.51 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQ 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVLLgreFSgaRYkaklFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:PRK13537 88 FDNLDPDFTVRENLLV---FG--RY----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVVAFERRRDRPEEKERygATITKDIAiwpp 240
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH--ALIESEIG---- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499747244 241 rlAGQSSIFSPDrdgPVAslghSRDDLAS-------SGETL 274
Cdd:PRK13537 232 --CDVIEIYGPD---PVA----LRDELAPlaerteiSGETL 263
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-228 |
7.67e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.56 E-value: 7.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML-----LGQEQPTKGKI------LLDGEPLPPEP 71
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVtfhgknLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 72 GPDRGVVFQRYSVFPHlTVLGNVLLGREFSGarYKA---KLFGAARRNAI--EEARQLIAEVGLAgsqdkypaqLSGGMQ 146
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGARING--YKGdmdELVERSLRQAAlwDEVKDKLKQSGLS---------LSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 147 QRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAFTLASRVVAFERRRDrpEEKER 226
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFNVELT--EGGGR 233
|
..
gi 499747244 227 YG 228
Cdd:PRK14243 234 YG 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
1.40e-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: 104.05 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpdrgvvfqrys 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 vfphltvlgnvllGREFSGARYKaklfgaarrnaieEARQL-IAEVglagsqdkypAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03216 61 -------------GKEVSFASPR-------------DARRAgIAMV----------YQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVT 153
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-208 |
3.13e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD-------GEPLPPEPGPDRGVVFQRYSVFP 86
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgenipamSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HLTVLGNVLLG-REFSgaRYKAKLFGAARRNAIEearqliaEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:PRK11831 98 DMNVFDNVAYPlREHT--QLPAPLLHSTVMMKLE-------AVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLA 208
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIA 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-201 |
5.08e-27 |
|
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: 109.51 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY-----GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL----DGEPLPPEPGPD 74
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 RG-------VVFQRYSVFPHLTVLGNVL--LGREFSgarykaklFGAARRNAI----------EEARQLIaevglagsqD 135
Cdd:TIGR03269 360 RGrakryigILHQEYDLYPHRTVLDNLTeaIGLELP--------DELARMKAVitlkmvgfdeEKAEEIL---------D 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 136 KYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEI-HTLMKRLwHETQMTVVMVTHDM 201
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAR-EEMEQTFIIVSHDM 488
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-216 |
6.35e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.09 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML----------------LGQEQPTKGKILLDGEPL 67
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksagshielLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 68 PPEPgpdrGVVFQRYSVFPHLTVLGNVLLGREFSGARYKA--KLFGAARRnaiEEARQLIAEVGLAGSQDKYPAQLSGGM 145
Cdd:PRK09984 85 RANT----GYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfSWFTREQK---QRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-218 |
1.40e-26 |
|
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: 104.50 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 9 VWKEyGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL--------LDGEPLPPEPGpDRGVVFQ 80
Cdd:TIGR02769 18 FGAK-QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAFRR-DVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RY--SVFPHLTVlgnvllgREFSGA--RYKAKLFGAARRNAIEEarqLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQAL 155
Cdd:TIGR02769 96 DSpsAVNPRMTV-------RQIIGEplRHLTSLDESEQKARIAE---LLDMVGLRSEDaDKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
3.82e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.15 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSE--LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPE---PGPDR 75
Cdd:PRK11300 1 MSQplLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVV--FQRYSVFPHLTVLGNVLLGRE-------FSGArYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQ 146
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVAQHqqlktglFSGL-LKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 147 QRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPE 222
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTplanGTPE 239
|
.
gi 499747244 223 E 223
Cdd:PRK11300 240 E 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-214 |
4.59e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 4.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSE--LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRML--LGQEQPT---------KGKILLDGEPL 67
Cdd:PRK14239 1 MTEpiLQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivyNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 68 PPEPGPDRGVVFQRYSVFPhLTVLGNVLLGREFSGARYKAKLFGAARRNAI-----EEARQLIAEVGLAgsqdkypaqLS 142
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKgasiwDEVKDRLHDSALG---------LS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 143 GGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHetQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFF 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-200 |
1.17e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 100.19 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPgpdRGVVFQRYSVFphlTVLGN 93
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR---KGLLERRQRVG---LVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 ----VLLGREFSGARYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:TIGR01166 77 pddqLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 170 ALDPGIRAEIHTLMKRLwHETQMTVVMVTHD 200
Cdd:TIGR01166 157 GLDPAGREQMLAILRRL-RAEGMTVVISTHD 186
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-201 |
1.31e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.12 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRG-------VVFQR-Y-SVFPHLT 89
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkiqIVFQNpYgSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 V---LGNVLLgrefsgarYKAKLFGAARRnaiEEARQLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:PRK11308 111 VgqiLEEPLL--------INTSLSAAERR---EKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-218 |
1.46e-25 |
|
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: 98.29 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpdrgvvfqrys 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 vfPHLTVLgnvllgrefsgarykaklfgaarrnaieearqliaevglagsqdkYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03221 61 --STVKIG---------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 164 LDEPFGALD-PGIRAEIHTLmkrlwHETQMTVVMVTHDmrEAF--TLASRVVAFERRR 218
Cdd:cd03221 94 LDEPTNHLDlESIEALEEAL-----KEYPGTVILVSHD--RYFldQVATKIIELEDGK 144
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-218 |
2.44e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.77 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGP---------- 73
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 74 ---DRGVVFQ--RYSVFPHLTVLGNV---LLGrefSGARYkaklFGAARrnaiEEARQLIAEVGLAGSQ-DKYPAQLSGG 144
Cdd:PRK11701 87 lrtEWGFVHQhpRDGLRMQVSAGGNIgerLMA---VGARH----YGDIR----ATAGDWLERVEIDAARiDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 145 MQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-212 |
3.87e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 104.00 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKT----TFLRMLLGQEQPTKGKILLDGEPLPPEPGPD----RG----VVFQR 81
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnriaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 --YSVFPHLTV---LGNVLlgrefsgaRYKAKLFGAARRnaiEEARQLIAEVGLAGSQ---DKYPAQLSGGMQQRLALAQ 153
Cdd:COG4172 101 pmTSLNPLHTIgkqIAEVL--------RLHRGLSGAAAR---ARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM---REaftLASRVV 212
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvvRR---FADRVA 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-212 |
3.97e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQ--IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GV 77
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvRrqvGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRY-SVFPHLTVLGNVLLGREFSGArykaklfgaARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFGLENIGV---------PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTlASRVV 212
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVI 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-214 |
4.19e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.45 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGD--QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GVV 78
Cdd:PRK13632 9 KVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEiRkkiGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRY-SVFPHLTVLGNVLLGREfsgarykaklfgaARRNAIEEARQLIAE----VGLAGSQDKYPAQLSGGMQQRLALAQ 153
Cdd:PRK13632 89 FQNPdNQFIGATVEDDIAFGLE-------------NKKVPPKKMKDIIDDlakkVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAfTLASRVVAF 214
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVF 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-200 |
4.54e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 103.98 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgepLPPEPGPDRGVVFQRYSVF---PHL-- 88
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD---GVPVSSLDQDEVRRRVSVCaqdAHLfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 89 -TVLGNVLLGREfsgarykaklfGAARrnaiEEARQLIAEVGLAGSQDKYP-----------AQLSGGMQQRLALAQALI 156
Cdd:TIGR02868 423 tTVRENLRLARP-----------DATD----EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMkrLWHETQMTVVMVTHD 200
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-213 |
5.14e-25 |
|
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: 103.52 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRYSVFPHlTVLGN 93
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWrdqiAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREFSGArykAKLFGAARRNAIEEARQLIAEvGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:TIGR02857 416 IRLARPDASD---AEIREALERAGLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 174 GIRAEIHTLMKRLwhETQMTVVMVTHDmREAFTLASRVVA 213
Cdd:TIGR02857 492 ETEAEVLEALRAL--AQGRTVLLVTHR-LALAALADRIVV 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-214 |
7.33e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---------------------- 75
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 ------GVVFQ--RYSVFPHlTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQ-DKYPAQLSGGMQ 146
Cdd:PRK13651 102 eirrrvGVVFQfaEYQLFEQ-TIEKDIIFG---------PVSMGVSKEEAKKRAAKYIELVGLDESYlQRSPFELSGGQK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 147 QRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-218 |
8.52e-25 |
|
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: 97.29 E-value: 8.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGvvfqrysvfPHL-TVLG 92
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---------DHVgYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLgreFSGArykaklfgaarrnaieearqlIAEvglagsqdkypAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03246 84 DDEL---FSGS---------------------IAE-----------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 173 PGIRAEIHTLMKRLwHETQMTVVMVTHDMrEAFTLASRVVAFERRR 218
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-212 |
1.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRY-SVFPHLT 89
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIrhkiGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGREFSGARYKAKlfgaarRNAIEEARQLiaeVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEM------KERVNEALEL---VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAfTLASRVV 212
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-204 |
1.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP---TKGKILLDGEPLPPEPGPD----RGVVFQRY-SVFPHLT 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDirekVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGREFSGArykaklfgaARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13640 102 VGDDVAFGLENRAV---------PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190
....*....|....*....|....*....|....*
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREA 204
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-210 |
1.42e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.43 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----- 75
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSgarykaKLFGAARRNaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIR------DDLSAEQRE--DRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASR 210
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCER 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
1.89e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.01 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKG-----KILLDGEPL-----PPEPGPDRGVVFQRY 82
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrdVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPhLTVLGNVLlgrefSGARyKAKLFGAARRNAIEEARqlIAEVGLAGS-QDKY---PAQLSGGMQQRLALAQALIMK 158
Cdd:PRK14271 111 NPFP-MSIMDNVL-----AGVR-AHKLVPRKEFRGVAQAR--LTEVGLWDAvKDRLsdsPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAFTLASRVVAF-----------ERRRDRPEEKE-- 225
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFfdgrlveegptEQLFSSPKHAEta 259
|
250
....*....|
gi 499747244 226 RYGATITKDI 235
Cdd:PRK14271 260 RYVAGLSGDV 269
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
2.13e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppepgpDRG--VVF-- 79
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGetVKIgy 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 --QRYSVF-PHLTVLGNVLlgrefsgarykaklfGAARRNAIEEARQLIAEVGLAGS-QDKYPAQLSGGMQQRLALAQAL 155
Cdd:COG0488 383 fdQHQEELdPDKTVLDELR---------------DGAPGGTEQEVRGYLGRFLFSGDdAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKrlwhETQMTVVMVTHDmREaF--TLASRVVAFE 215
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALD----DFPGTVLLVSHD-RY-FldRVATRILEFE 503
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-223 |
2.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------GVVFQrysvFPHLTV 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrkkvSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLgrefSGARYKAKLFGAARRNAIEEARQLIAEVGLAGS-QDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13641 99 FENTVL----KDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 170 ALDPGIRAEIHTLMKRlWHETQMTVVMVTHDMREAFTLASRVVAFER----RRDRPEE 223
Cdd:PRK13641 175 GLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHgkliKHASPKE 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-216 |
2.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------GVVFQrysvFPHLTV 90
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikpvrkkvGVVFQ----FPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLgrefSGARYKAKLFGAARRNAIEEARQLIAEVGLAGS-QDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13643 98 FEETVL----KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499747244 170 ALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:PRK13643 174 GLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-172 |
4.02e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 97.23 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRysvfPHL-- 88
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrsqiGLVSQE----PVLfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 89 -TVLGNVLLGRefsgarykaklFGAARRNAIEEARQ-----LIA--------EVGLAGSQdkypaqLSGGMQQRLALAQA 154
Cdd:cd03249 91 gTIAENIRYGK-----------PDATDEEVEEAAKKanihdFIMslpdgydtLVGERGSQ------LSGGQKQRIAIARA 153
|
170
....*....|....*...
gi 499747244 155 LIMKPKVLLLDEPFGALD 172
Cdd:cd03249 154 LLRNPKILLLDEATSALD 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-211 |
4.11e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------GVVFQRYSVFPHLT 89
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnqklGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNV----LLGrefsgarykaklfGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:PRK11629 104 ALENVamplLIG-------------KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMReaftLASRV 211
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ----LAKRM 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-204 |
6.71e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.13 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQR-YSVFPHLTVLGN 93
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrkhiGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREFSGARYKaklfgaarrNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK13648 105 VAFGLENHAVPYD---------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 174 GIRAEIHTLMKRLWHETQMTVVMVTHDMREA 204
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-218 |
1.09e-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: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPP--EPGPDR----------GVVFQRYSVF 85
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdlAQASPReilalrrrtiGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 PHLTVLGNV---LLGRefsgarykaklfGAARRNAIEEARQLIAEVGLAGS-QDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:COG4778 106 PRVSALDVVaepLLER------------GVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 162 LLLDEPFGALDPGIRAE----IHTLMKRlwhetQMTVVMVTHDM--REAftLASRVVAFERRR 218
Cdd:COG4778 174 LLLDEPTASLDAANRAVvvelIEEAKAR-----GTAIIGIFHDEevREA--VADRVVDVTPFS 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-199 |
1.25e-23 |
|
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: 95.76 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 2 SELKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----G 76
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrsmiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFPHlTVLGNVLLGREfsGARYKAKLFGAARRNAIEEARQLI----AEVGLAGSqdkypaQLSGGMQQRLALA 152
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRP--NATDEEVIEAAKEAGAHDFIMKLPngydTVLGENGG------NLSQGERQLLAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTH 199
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAH 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-223 |
2.61e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 12 EYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRG----VVFQRYSVFPH 87
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASrrvaSVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 LTVLGNVLLGREFSGARYKAklFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:PRK09536 92 FDVRQVVEMGRTPHRSRFDT--WTETDRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 168 FGALDpgIRAEIHTL-MKRLWHETQMTVVMVTHDMreafTLASR------VVAFERRRD--RPEE 223
Cdd:PRK09536 167 TASLD--INHQVRTLeLVRRLVDDGKTAVAAIHDL----DLAARycdelvLLADGRVRAagPPAD 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-214 |
3.58e-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: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQ 80
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrlAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVLLGReF--SGARYKAklfgaARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMK 158
Cdd:COG4604 83 ENHINSRLTVRELVAFGR-FpySKGRLTA-----EDREIIDEA---IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-199 |
4.31e-23 |
|
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: 93.58 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEpgpdRGVVFQRYSVFPHLTVLGN 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ----RDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREfsGARYKAKLFGAARRNaIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:TIGR01189 87 ELSALE--NLHFWAAIHGGAQRT-IEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 499747244 174 GIRAEIHTLMKRlwH-ETQMTVVMVTH 199
Cdd:TIGR01189 161 AGVALLAGLLRA--HlARGGIVLLTTH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-218 |
1.01e-22 |
|
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: 92.11 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVF-----QRYSVFPHLT 89
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGRefsgarykaklfgaarrnaieearqliaevglagsqdkypaQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:cd03215 95 VAENIALSS-----------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 170 ALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:cd03215 134 GVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-218 |
1.98e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVasRA--FVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---RGVVF-----QRYSVFPH 87
Cdd:COG1129 267 VVRDVSFSV--RAgeILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYvpedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 LTVLGNVLLGREFSGARykaklFGAARRNAIEE-ARQLIAEVGL-AGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:COG1129 345 LSIRENITLASLDRLSR-----GGLLDRRRERAlAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHEtQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-216 |
1.99e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI--------LLDGeplppepg 72
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvrgrvssLLGL-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 73 pdrGVVFQrysvfPHLTVLGNVllgrefsgaRYKAKLFGAARRnaieEARQLIAEV----GLAGSQDKYPAQLSGGMQQR 148
Cdd:cd03220 92 ---GGGFN-----PELTGRENI---------YLNGRLLGLSRK----EIDEKIDEIiefsELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 149 LALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWhETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-211 |
3.23e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPL----------PPEPGP 73
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 74 DRGVVFQRYSVFPHLTVLGNVLLGREFSGARYKAKLfgaarRNAIEEARQLIAEVGLAGSQDKYPA-QLSGGMQQRLALA 152
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREI-----KKIVEECLRKVGLWKEVYDRLNSPAsQLSGGQQQRLTIA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYV 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
4.86e-22 |
|
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: 91.11 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRYSVFpHLTVLGN 93
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLrrniGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREFSGaryKAKLFGAARRNAIEE-----ARQLIAEVGLAGsqdkypAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:cd03245 98 ITLGAPLAD---DERILRAAELAGVTDfvnkhPNGLDLQIGERG------RGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 169 GALDpgIRAEIHtLMKRL--WHETQmTVVMVTHDMReAFTLASRVVAFERRR 218
Cdd:cd03245 169 SAMD--MNSEER-LKERLrqLLGDK-TLIIITHRPS-LLDLVDRIIVMDSGR 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-216 |
6.23e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI------LLDGEPLPPEPGPDR--GVVFQRYSVFPHLTVLG 92
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPEKRriGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVllgrefsgaRYKAKLFGAARRNAIeearqliaeVGLAGSQ---DKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK11144 96 NL---------RYGMAKSMVAQFDKI---------VALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-201 |
8.92e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR------- 75
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflrrqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSGARykaklfGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGAS------GDDIRRRVSAA---LDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRlWHETQMTVVMVTHDM 201
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEE-FNRVGVTVLMATHDI 197
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-212 |
9.90e-22 |
|
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: 90.85 E-value: 9.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 11 KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL---LDGEPLPPEPGPDRGVVF-QRYSVFP 86
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvagLVPWKRRKKFLRRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HLTVLGNVLLGREFSG---ARYKAklfgaaRRNAIEEARQLIAEVglagsqDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03267 109 DLPVIDSFYLLAAIYDlppARFKK------RLDELSELLDLEELL------DTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-218 |
1.10e-21 |
|
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: 91.05 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPE------------- 70
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlseaerrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 71 PGPDRGVVFQRYSVFPHLTVLGNVLLGREF--SGARYkaklFGAARrnaiEEARQLIAEVGL-AGSQDKYPAQLSGGMQQ 147
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLmaIGARH----YGNIR----ATAQDWLEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 148 RLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-218 |
1.15e-21 |
|
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: 94.70 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 8 KVWKEYGDQIVlEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL---DGEPLPPEPGPDRGVVFQRYSV 84
Cdd:TIGR01257 936 KIFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggkDIETNLDAVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 85 FPHLTVLGNVLlgrefsgarYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:TIGR01257 1015 FHHLTVAEHIL---------FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 165 DEPFGALDPGIRAEIHTLMkrLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-212 |
1.62e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTT----FLRMLlgqeqPTKGKILLDGEPLPPEPGPDR-------GVVFQ-- 80
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvrhriQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLGNVLlgrefSGARYKAKLFGAARRNaiEEARQLIAEVGL-AGSQDKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:PRK15134 372 NSSLNPRLNVLQIIE-----EGLRVHQPTLSAAQRE--QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVI 497
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-212 |
5.04e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.84 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGpDR---------GVVFQrysvFPHlT 89
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTK-DKyirpvrkriGMVFQ----FPE-S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGREFSgarYKAKLFGAARRNAIEEARQLIAEVGLagSQD---KYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK13646 97 QLFEDTVEREII---FGPKNFKMNLDEVKNYAHRLLMDLGF--SRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 167 PFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVI 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-199 |
7.91e-21 |
|
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: 87.22 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYGDQIvLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQ--EQPTKGKILLDGEPLPPEPGPDR-GVVF 79
Cdd:cd03213 10 TVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKIiGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVlgnvllgREFsgARYKAKLFGaarrnaieearqliaevglagsqdkypaqLSGGMQQRLALAQALIMKP 159
Cdd:cd03213 89 QDDILHPTLTV-------RET--LMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWHeTQMTVVMVTH 199
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIH 169
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-199 |
9.59e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.71 E-value: 9.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpdrGVVFQRYS-VFPHLTVlgn 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD------------GVPLVQYDhHYLHRQV--- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGRE---FSGA-----------------RYKAKLFGAarRNAIEEARQLI-AEVGLAGSqdkypaQLSGGMQQRLALA 152
Cdd:TIGR00958 558 ALVGQEpvlFSGSvreniaygltdtpdeeiMAAAKAANA--HDFIMEFPNGYdTEVGEKGS------QLSGGQKQRIAIA 629
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRlwheTQMTVVMVTH 199
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAH 672
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-199 |
1.00e-20 |
|
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: 87.16 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 12 EYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpDRGVVFQRYSVFPHLTVL 91
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN----------GGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 92 GN------VLLGREfsGARYKAKLFGaarRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:cd03231 79 GHapgiktTLSVLE--NLRFWHADHS---DEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHETQMtVVMVTH 199
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGM-VVLTTH 183
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-201 |
1.15e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.77 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 20 EDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI------LLDGEPLP-PEPGPDRGVVFQR--YSVFPHLTV 90
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdLLGMKDDEwRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 lGNVLlgrefsgAR----YKAKLfgaARRNAIEEARQLIAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:PRK15079 118 -GEII-------AEplrtYHPKL---SRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-216 |
1.17e-20 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 87.14 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 10 WKEYGDQI--VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLdgeplppepgpdRGVVFqrY-SVFP 86
Cdd:cd03250 10 WDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV------------PGSIA--YvSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HL---TVLGNVLLGREFSGARYKAKLFGAARRNAIEE-ARQLIAEVGLAGSQdkypaqLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03250 76 WIqngTIRENILFGKPFDEERYEKVIKACALEPDLEIlPDGDLTEIGEKGIN------LSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 163 LLDEPFGALDPGIRAEI--HTLMKRLWHETqmTVVMVTHDMrEAFTLASRVVAFER 216
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIfeNCILGLLLNNK--TRILVTHQL-QLLPHADQIVVLDN 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-203 |
1.22e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.46 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-RGVV---F 79
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVsycA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHlTVLGNVLLGREFsgarykaklfgaaRRNAIEEARQL--IAEVGLAGSQ-DKYPAQLSGGMQQRLALAQALI 156
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQI-------------RNQQPDPAIFLddLERFALPDTIlTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMRE 203
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-199 |
6.10e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpDRGVVFQRYSVFPHLTVLGN 93
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ----------GEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 vLLG--REFSGA---RYKAKLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PRK13538 82 -QPGikTELTALenlRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|...
gi 499747244 169 GALDPGIRAEIHTLMKRlwHETQ--MtVVMVTH 199
Cdd:PRK13538 158 TAIDKQGVARLEALLAQ--HAEQggM-VILTTH 187
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-204 |
7.60e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 2 SELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGvvfQR 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFP--HLT-----VLGNVLLGRefsgARYKAkLFGaaRRNAIEEAR--QLIAEVGLAGSQDKYPAQLSGGMQQRLALA 152
Cdd:PRK11231 78 LALLPqhHLTpegitVRELVAYGR----SPWLS-LWG--RLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREA 204
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQA 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-242 |
7.82e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI-VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL---LDGEPLPPEPGPDR--GV 77
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKlvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQR-YSVFPHLTVLGNVLLGREfsgaryKAKLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPE------NLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREaFTLASRVVAFERRRDRPE-EKERYGATIT-KD 234
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEgEPENVLSDVSlQT 230
|
....*...
gi 499747244 235 IAIWPPRL 242
Cdd:PRK13644 231 LGLTPPSL 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-199 |
1.09e-19 |
|
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: 88.32 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQ--PTKGKILLDGEPLPPEPGPDR------ 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHVALCEKCGYVERpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 -------------------------------GVVFQR-YSVFPHLTVLGNVLlgREFSGARYKAKlfgaarrNAIEEARQ 123
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklrrrirkriAIMLQRtFALYGDDTVLDNVL--EALEEIGYEGK-------EAVGRAVD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 124 LIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTH 199
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-199 |
2.22e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.06 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD----GEPLPPEPGPDRGVVFQRYSVFPHlTV 90
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpiSQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLG-REFSGARYKAKLFGAARRNAIEEARQLI-AEVGLAGSQdkypaqLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:cd03248 105 QDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYdTEVGEKGSQ------LSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 169 GALDPGIRAEIHTLMkRLWHETQmTVVMVTH 199
Cdd:cd03248 179 SALDAESEQQVQQAL-YDWPERR-TVLVIAH 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-213 |
2.80e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPP--EPGPDRGVVF--QRYSVFPHLTV 90
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYlpQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLGR-EFSGARYKaklFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK10575 103 RELVAIGRyPWHGALGR---FGAADREKVEEA---ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVA 213
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVA 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-199 |
5.21e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 86.31 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEY-GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGE--PLPPEPGPDRGV-VFQR 81
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplSSLSHSVLRQGVaMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFPHLTVLGNVLLGREFSGARYKAKLfgaarrnaieEARQLIAEV-----GLAGSQDKYPAQLSGGMQQRLALAQALI 156
Cdd:PRK10790 423 DPVVLADTFLANVTLGRDISEEQVWQAL----------ETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTH 199
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-211 |
5.29e-19 |
|
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: 83.19 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP----TKGKILLDGEPLPPEPGPDR--GVVFQ--RYSVFPHLTVLg 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRhiATIMQnpRTAFNPLFTMG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 nvllgrefSGARYKAKLFGAARRNAIEEARQLIAEVGLAGSQ---DKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:TIGR02770 83 --------NHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRV 211
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEV 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
5.51e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.02 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI-LLDGEPLPPEPGPDR---GVVFQRY--SVFPhLTVLG 92
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRskvGLVFQDPddQVFS-STVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLGREFSGarykakLFGAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK13647 100 DVAFGPVNMG------LDKDEVERRVEEA---LKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 173 PGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK13647 171 PRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVI 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-212 |
6.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 11 KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEP-----GPDRGVVFQRysvf 85
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdiRNKAGMVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 PH-----LTVLGNVLLGREFSGARYKAKlfgaarRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:PRK13633 94 PDnqivaTIVEEDVAFGPENLGIPPEEI------RERVDES---LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTlASRVV 212
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRII 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
8.12e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.59 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD------GEPLPPEPGPDRGVVFQRY--SVFPHlT 89
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikyDKKSLLEVRKTVGIVFQNPddQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13639 96 VEEDVAFG---------PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499747244 170 ALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK13639 167 GLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKV 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-199 |
8.18e-19 |
|
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: 81.59 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQRysvfPHL--- 88
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSsliSVLNQR----PYLfdt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 89 TVLGNvlLGRefsgarykaklfgaarrnaieearqliaevglagsqdkypaQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:cd03247 90 TLRNN--LGR-----------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 169 GALDPGIRAEIHTLMkrLWHETQMTVVMVTH 199
Cdd:cd03247 127 VGLDPITERQLLSLI--FEVLKDKTLIWITH 155
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-199 |
8.46e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGeplppepgpDRGVVF--QR-YsvFPHLTvL 91
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA---------GARVLFlpQRpY--LPLGT-L 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 92 GNVLLgrefsgarYKAklfgAARRNAIEEARQLIAEVGLA------GSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:COG4178 443 REALL--------YPA----TAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|....
gi 499747244 166 EPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTH 199
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGT--TVISVGH 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
111-212 |
1.09e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 111 GAARRNAIEEARQLIAEVGLAGSQ---DKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLW 187
Cdd:PRK10261 136 GASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQ 215
|
90 100
....*....|....*....|....*
gi 499747244 188 HETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK10261 216 KEMSMGVIFITHDMGVVAEIADRVL 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-210 |
1.82e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.85 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGE-----PLPPEPGPDR 75
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVFQRYSVFPHLTVLGNVLLGREFSG-ARYKAKlfgaarrnaIEEARQLIAEvgLAGSQDKYPAQLSGGMQQRLALAQA 154
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAErDQFQER---------IKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASR 210
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADR 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-218 |
2.16e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD----RGVVFQRY--SVFPH 87
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfVGLVFQNPddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 lTVLGNVLLGREFSGarykakLFGAARRNAIEEARQLiaeVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:PRK13652 95 -TVEQDIAFGPINLG------LDEETVAHRVSSALHM---LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499747244 168 FGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-202 |
2.22e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 84.41 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGvvfqrysvfPHltvLG- 92
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG---------RH---IGy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 ---NVLLgreFSG------ARykaklFGAARRNAIEEARQLIA--------------EVGLAGsqdkypAQLSGGMQQRL 149
Cdd:COG4618 411 lpqDVEL---FDGtiaeniAR-----FGDADPEKVVAAAKLAGvhemilrlpdgydtRIGEGG------ARLSGGQRQRI 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDP-GIRAEIHTLmkRLWHETQMTVVMVTHDMR 202
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDeGEAALAAAI--RALKARGATVVVITHRPS 528
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-218 |
3.70e-18 |
|
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: 80.99 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD----GEPLPPEPGPDRGVVFQRYSVFpHLTVLGN 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlALADPAWLRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREfsgarykaklfGAARRNAIEEARqliaevgLAGSQD---KYP-----------AQLSGGMQQRLALAQALIMKP 159
Cdd:cd03252 96 IALADP-----------GMSMERVIEAAK-------LAGAHDfisELPegydtivgeqgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWheTQMTVVMVTHDMrEAFTLASRVVAFERRR 218
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRL-STVKNADRIIVMEKGR 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-214 |
4.07e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 2 SELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDrgvVFQR 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YSVFP-HLTVLGNVLLGREFSGARYKAK-LFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:PRK10253 83 IGLLAqNATTPGDITVQELVARGRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-203 |
6.93e-18 |
|
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: 80.35 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GVVFQRYSVFpHLTV 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRraiGVVPQDTVLF-NDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLGREFSGaryKAKLFGAARRNAIEEA--------RQLIAEVGLagsqdkypaQLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03253 92 GYNIRYGRPDAT---DEEVIEAAKAAQIHDKimrfpdgyDTIVGERGL---------KLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLwhETQMTVVMVTHDMRE 203
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-212 |
7.11e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 11 KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI--------LLDGeplppepgpdrGVVFQry 82
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsaLLEL-----------GAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 svfPHLTvlgnvllGREfsGARYKAKLFGAARRnAIEEARQLI---AEVGlagsqdKY---PAQ-LSGGMQQRLALAQAL 155
Cdd:COG1134 101 ---PELT-------GRE--NIYLNGRLLGLSRK-EIDEKFDEIvefAELG------DFidqPVKtYSSGMRARLAFAVAT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVV 212
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAI 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-201 |
7.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.05 E-value: 7.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI-VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPgpdRGVVFQRY 82
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR---KGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHLTVLGNVLlgreFSGARYKAKLFGAA-----RRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:PRK13636 83 SVGMVFQDPDNQL----FSASVYQDVSFGAVnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
8.96e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSEL-KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPpepgpdrGVVF 79
Cdd:PRK09544 1 MTSLvSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI-------GYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVLGNVLLgREFSGARyKAKLFGAARRnaiEEARQLIaevglagsqdKYPAQ-LSGGMQQRLALAQALIMK 158
Cdd:PRK09544 74 QKLYLDTTLPLTVNRFL-RLRPGTK-KEDILPALKR---VQAGHLI----------DAPMQkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-199 |
1.31e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGV-VFQRYSVFPHLTVLG 92
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLGREFSGarykaklfgaARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK13539 93 NLEFWAAFLG----------GEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*...
gi 499747244 173 PGIRAEIHTLMKRlwHETQ-MTVVMVTH 199
Cdd:PRK13539 160 AAAVALFAELIRA--HLAQgGIVIAATH 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-172 |
1.88e-17 |
|
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: 79.20 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQI--VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GV 77
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRrqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQRYSVFpHLTVLGNVLLGREfsgarykaklfGAARRNAIEEARQLIAEVGLAGSQDKYPA-------QLSGGMQQRLA 150
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP-----------GATREEVEEAARAANAHEFIMELPEGYDTvigergvKLSGGQRQRIA 148
|
170 180
....*....|....*....|..
gi 499747244 151 LAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03251 149 IARALLKDPPILILDEATSALD 170
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-199 |
1.89e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-RG---VVFQRYSVFPHlT 89
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaisVVSQRVHLFSA-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLgrefsgarykaklfgaARRNAIEEarQLIA---EVGLAGSQDKYPA----------QLSGGMQQRLALAQALI 156
Cdd:PRK11160 430 LRDNLLL----------------AAPNASDE--ALIEvlqQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRlwHETQMTVVMVTH 199
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITH 532
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-204 |
2.38e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.75 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRY-SVFPHLTVLGN 93
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkiGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREFSGArykaklfgaARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK13642 103 VAFGMENQGI---------PREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 174 GIRAEIHTLMKRLWHETQMTVVMVTHDMREA 204
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-182 |
3.01e-17 |
|
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: 81.13 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLdgeplppEPGPDRGVVFQ-RY 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-------GETVKLAYVDQsRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHLTVLgnvllgREFSGARYKAKLfGAARRNaieeARQLIAEVGLAGS-QDKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:TIGR03719 396 ALDPNKTVW------EEISGGLDIIKL-GKREIP----SRAYVGRFNFKGSdQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180
....*....|....*....|.
gi 499747244 162 LLLDEPFGALDpgiraeIHTL 182
Cdd:TIGR03719 465 LLLDEPTNDLD------VETL 479
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-212 |
5.00e-17 |
|
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: 77.70 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 11 KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP---TKGKILLDGEPLPPEPGPDR-GVVFQRYSVFP 86
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCvAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HLTV------LGNVLLGREFSGARYKAklfgaarrnaiEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03234 95 GLTVretltyTAILRLPRKSSDAIRKK-----------RVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 161 VLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMR-EAFTLASRVV 212
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHQPRsDLFRLFDRIL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-216 |
9.32e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPgpdRGVVFQRYS 83
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK---RGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VfphLTVLGN----VLLGREFSGARYKAKLFGAARRnaiEEARQLIAEVGLAGSQD--KYPAQ-LSGGMQQRLALAQALI 156
Cdd:PRK13638 79 V---ATVFQDpeqqIFYTDIDSDIAFSLRNLGVPEA---EITRRVDEALTLVDAQHfrHQPIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMtVVMVTHDMREAFTLASRVVAFER 216
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQ 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-199 |
9.71e-17 |
|
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: 79.78 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 2 SELKIEKVWKEYG-DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEpgpDRGVVFQ 80
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLgnvllgreFSGARYKAKLFGAARRNAIEEARQL--IAEV---------GLAGSQDKYPAQLSGGMQQRL 149
Cdd:TIGR01193 549 FINYLPQEPYI--------FSGSILENLLLGAKENVSQDEIWAAceIAEIkddienmplGYQTELSEEGSSISGGQKQRI 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDpgIRAEiHTLMKRLWHETQMTVVMVTH 199
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLD--TITE-KKIVNNLLNLQDKTIIFVAH 667
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
137-201 |
1.26e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.23 E-value: 1.26e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 137 YPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-198 |
1.53e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRG----VVFQRYSvfphltvlgNV 94
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrirMIFQDPS---------TS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 95 LLGREFSGA------RYKAKLFGAARRNAIEEA-RQliaeVGLAGSQ-DKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK15112 100 LNPRQRISQildfplRLNTDLEPEQREKQIIETlRQ----VGLLPDHaSYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190
....*....|....*....|....*....|..
gi 499747244 167 PFGALDPGIRAEIHTLMKRLWHETQMTVVMVT 198
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-202 |
1.58e-16 |
|
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: 76.22 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGVVfQRYSVF-----PHL---TV 90
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSR-NRYSVAyaaqkPWLlnaTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLGREFSGARYKAklfgaarrnaIEEARQLIAEVGLA--GSQDKYPAQ---LSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:cd03290 96 EENITFGSPFNKQRYKA----------VTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 166 EPFGALDpgIRAEIHTLMK---RLWHETQMTVVMVTHDMR 202
Cdd:cd03290 166 DPFSALD--IHLSDHLMQEgilKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-204 |
1.81e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 36 GPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVFQRYSVFPHLTVLGNVLLgrefsgaryKAKLFG- 111
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRrrvGYMSQAFSLYGELTVRQNLEL---------HARLFHl 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 112 --AARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHE 189
Cdd:NF033858 370 paAEIAARVAE---MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSRE 446
|
170
....*....|....*
gi 499747244 190 TQMTVVMVTHDMREA 204
Cdd:NF033858 447 DGVTIFISTHFMNEA 461
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
2.33e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-----GVV 78
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgiGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVLLGREFSgarykAKLFGAarrNAI------EEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALA 152
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLT-----KKVCGV---NIIdwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 153 QALIMKPKVLLLDEPFGALdpgIRAEIHTL---MKRLWHETQmTVVMVTHDMREAFTLASRV 211
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL---TNKEVDYLfliMNQLRKEGT-AIVYISHKLAEIRRICDRY 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
111-201 |
4.61e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 111 GAARRNAIEEARQLIAEVGL---AGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLW 187
Cdd:PRK11022 121 GGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQ 200
|
90
....*....|....
gi 499747244 188 HETQMTVVMVTHDM 201
Cdd:PRK11022 201 QKENMALVLITHDL 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-242 |
5.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL---------LDGEPLPPEPGPDRGVVFQ--RYSVFPH 87
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaipanLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 lTVLGNVLLGrefsgarykAKLFGAARRNAIEEARQLIAEVGLAGSQDKY-PAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK13645 107 -TIEKDIAFG---------PVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 167 PFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR----DRPEEKERYGATITKdIAIWPPRL 242
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKvisiGSPFEIFSNQELLTK-IEIDPPKL 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-212 |
6.04e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKT----TFLRML-------LGQEQPTKGKILLDGEPLPPepgpdRGV-------VF 79
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvyPSGDIRFHGESLLHASEQTL-----RGVrgnkiamIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QR--YSVFPHLTV---LGNVL-LGREFSGARYKAKLFGAARRNAIEEARQLIAEvglagsqdkYPAQLSGGMQQRLALAQ 153
Cdd:PRK15134 99 QEpmVSLNPLHTLekqLYEVLsLHRGMRREAARGEILNCLDRVGIRQAAKRLTD---------YPHQLSGGERQRVMIAM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVA 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-204 |
2.20e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.93 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI-LLDGeplppepgpDRGVVFQRYSVFPH---- 87
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGG---------DMADARHRRAVCPRiaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 88 -----------LTVLGNVllgrEFSGarykaKLFG---AARRNAIEEarqLIAEVGLAGSQDKyPA-QLSGGMQQRLALA 152
Cdd:NF033858 82 pqglgknlyptLSVFENL----DFFG-----RLFGqdaAERRRRIDE---LLRATGLAPFADR-PAgKLSGGMKQKLGLC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHET-QMTVVMVTHDMREA 204
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEA 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
2.20e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL---LDGEPLPPEPGPDRGVVF-QRYSVFPHLTVLGNV 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPFKRRKEFARRIGVVFgQRSQLWWDLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 95 LLGREF---SGARYKAKLfgaarrnaieeaRQLIAEVGLAGSQDKyPA-QLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:COG4586 118 RLLKAIyriPDAEYKKRL------------DELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499747244 171 LDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:COG4586 185 LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-218 |
1.26e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 13 YGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP----TKGKILLDGEPLPPEPGPDRGV--VFQR-YSVF 85
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIatIMQNpRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 PHLTVLGnvllgrefSGARYKAKLFGAARRNAIeeARQLIAEVGLAGSQ---DKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:PRK10418 93 NPLHTMH--------THARETCLALGKPADDAT--LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-199 |
1.29e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.88 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppEPGPDRGVVF--QRysvfPHLTvLG 92
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFlpQR----PYLP-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVllgREfsgarykaklfgaarrnaieearQLIaevglagsqdkYP--AQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:cd03223 79 TL---RE-----------------------QLI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*....
gi 499747244 171 LDPGIRAEIHTLMKRLwhetQMTVVMVTH 199
Cdd:cd03223 122 LDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-214 |
1.40e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVW-KEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILL---DGEPLPPEPGPDRGVVF 79
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdgeDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 -----QRYSVFPHLTVLGNVLLGReFSGARYKAKLFgaARRNAIEE-ARQLIAEVGLAGSQDKYPA-QLSGGMQQRLALA 152
Cdd:COG3845 338 ipedrLGRGLVPDMSVAENLILGR-YRRPPFSRGGF--LDRKAIRAfAEELIEEFDVRTPGPDTPArSLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVVAF 214
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-199 |
1.83e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQeQPTKGKILLDgeplppepgpdrGVVFQRYSV---------- 84
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKIN------------GIELRELDPeswrkhlswv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 85 -----FPHLTVLGNVLLGR-EFSGARYKAKLfgaARRNAIEEARQLiaEVGLA---GSQDkypAQLSGGMQQRLALAQAL 155
Cdd:PRK11174 429 gqnpqLPHGTLRDNVLLGNpDASDEQLQQAL---ENAWVSEFLPLL--PQGLDtpiGDQA---AGLSVGQAQRLALARAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499747244 156 IMKPKVLLLDEPFGALDpgIRAEiHTLMKRLWHETQ-MTVVMVTH 199
Cdd:PRK11174 501 LQPCQLLLLDEPTASLD--AHSE-QLVMQALNAASRrQTTLMVTH 542
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-199 |
2.27e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.87 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQE--QPTKGKILLDGEPLPPEPGPDR-----G 76
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaragiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFPHLTVLgNVLlgREFSGARYKAKLfgaARRNAIEEARQLIAEVGLAgsqDKYpAQ------LSGGMQQRLA 150
Cdd:COG0396 81 LAFQYPVEIPGVSVS-NFL--RTALNARRGEEL---SAREFLKLLKEKMKELGLD---EDF-LDryvnegFSGGEKKRNE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499747244 151 LAQALIMKPKVLLLDEPFGALD-PGIRAEIHTLMKRlwHETQMTVVMVTH 199
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDiDALRIVAEGVNKL--RSPDRGILIITH 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-214 |
5.70e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-----GVVFQRYSVFPHLTVLGN 93
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlaagvAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDp 173
Cdd:PRK11288 100 LYLG------QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 174 gIRaEIHTLMK---RLWHETQMtVVMVTHDMREAFTLASRVVAF 214
Cdd:PRK11288 173 -AR-EIEQLFRvirELRAEGRV-ILYVSHRMEEIFALCDAITVF 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-219 |
6.26e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR-----GVVFQRYSVFPHLTVLGN 93
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeagiGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREFSGArykaklFGAAR-RNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALd 172
Cdd:PRK10762 100 IFLGREFVNR------FGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499747244 173 pgIRAEIHTLMK--RLWHETQMTVVMVTHDMREAFTLASRVVAFerrRD 219
Cdd:PRK10762 173 --TDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVF---RD 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-215 |
7.07e-14 |
|
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: 69.36 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPlppepgpdrgVVFQRYSVFPHLTVLGNVLLgrefsgaRYKAKLFG 111
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----------VSYKPQYIKADYEGTVRDLL-------SSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 112 AARRNAIEEARQLiaevGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQ 191
Cdd:cd03237 91 THPYFKTEIAKPL----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|....
gi 499747244 192 MTVVMVTHDMREAFTLASRVVAFE 215
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-172 |
9.35e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.76 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLD----GEPLPPEPGPDRGVVFQRYSVFPHlTVLGNV 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdiRTVTRASLRRNIAVVFQDAGLFNR-SIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 95 LLGREfsGARyKAKLFGAARRNAIEE--ARQ---LIAEVGLAGSQdkypaqLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13657 430 RVGRP--DAT-DEEMRAAAERAQAHDfiERKpdgYDTVVGERGRQ------LSGGERQRLAIARALLKDPPILILDEATS 500
|
...
gi 499747244 170 ALD 172
Cdd:PRK13657 501 ALD 503
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-200 |
9.86e-14 |
|
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: 70.73 E-value: 9.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLppepgpdRGVVFQRYSVFPHLTVLGN 93
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK-------VGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGRefsgARYKAKLfgaARRNAI--------EEARQLIAEvgLAGSQDKYPAQ------------------------- 140
Cdd:TIGR03719 89 VEEGV----AEIKDAL---DRFNEIsakyaepdADFDKLAAE--QAELQEIIDAAdawdldsqleiamdalrcppwdadv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 141 --LSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgirAEIHTLMKRLWHETQMTVVMVTHD 200
Cdd:TIGR03719 160 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-211 |
1.34e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL-----LDGEPLPPEPGPDRGV--VFQR--YSVFPHLT 89
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGKLQALRRDIqfIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLlgrefSGARYKAKLFGAARRNAIEEarqLIAEVGLAGSQD-KYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PRK10261 420 VGDSIM-----EPLRVHGLLPGKAAAARVAW---LLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 169 GALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-172 |
2.02e-13 |
|
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: 69.75 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRYSVFPHlTVLGN 93
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLrrqvALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGR--EFSGARYKAKLFGAarrNAIEEARQLI----AEVGLAGSQdkypaqLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:TIGR02203 426 IAYGRteQADRAEIERALAAA---YAQDFVDKLPlgldTPIGENGVL------LSGGQRQRLAIARALLKDAPILILDEA 496
|
....*
gi 499747244 168 FGALD 172
Cdd:TIGR02203 497 TSALD 501
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-214 |
2.07e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---RGVVFQRYS-----VFPHLTVLG 92
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESrrdngFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVLLGREFSGARYKAK--LFGAARRNAIEEARQLIAEVGLAgSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:PRK09700 361 NMAISRSLKDGGYKGAmgLFHEVDEQRTAENQRELLALKCH-SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 171 LDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVVAF 214
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVF 482
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-226 |
2.61e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQE--QPTKGKilldgeplppepgpdrgVVFQRYSVFPHLTVLGNVl 95
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGC-----------------VDVPDNQFGREASLIDAI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 96 lgrefsgarykaklfgaARRNAIEEARQLIAEVGLAgsqDKY-----PAQLSGGMQQRLALAQALIMKPKVLLLDEpFGA 170
Cdd:COG2401 107 -----------------GRKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDE-FCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 171 -LDPGIRAEIHTLMKRLWHETQMTVVMVTH--DMREAftLASRVVAFERRRDRPEEKER 226
Cdd:COG2401 166 hLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDD--LQPDLLIFVGYGGVPEEKRR 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-211 |
2.77e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 33 ALVGPSGCGKTTFLRMLLGQEQPTKGkillDGEPLPPEPGPDRGVVFQRYSVFPHLTVLGNVLLGREFsgARYKAKLFGA 112
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSG----DATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREH--LYLYARLRGV 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 113 ARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQm 192
Cdd:TIGR01257 2043 PAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR- 2121
|
170
....*....|....*....
gi 499747244 193 TVVMVTHDMREAFTLASRV 211
Cdd:TIGR01257 2122 AVVLTSHSMEECEALCTRL 2140
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-212 |
2.95e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQ-EQPTKGKILLDGEPLPPEPGPD---RGVVF-----QRYSVFPHLT 89
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMvpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVLLG--REFSGaryKAKLFGAARRNAIEEArqlIAEVGLAGSQDKYP-AQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:TIGR02633 356 VGKNITLSvlKSFCF---KMRIDAAAELQIIGSA---IQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 167 PFGALDPGIRAEIHTLMKRLWHETqMTVVMVTHDMREAFTLASRVV 212
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVL 474
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
4.62e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR--------------------GV 77
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHElitnpyskkiknfkelrrrvSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 VFQ--RYSVFPHlTV-----LGNVLLGREFSGARYKAKLFgaarrnaieearqlIAEVGLAGS-QDKYPAQLSGGMQQRL 149
Cdd:PRK13631 121 VFQfpEYQLFKD-TIekdimFGPVALGVKKSEAKKLAKFY--------------LNKMGLDDSyLERSPFGLSGGQKRRV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVVAFER 216
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDK 251
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-183 |
7.10e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSE--LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQeQPT---KGKILLDGEPLPPEPGPD- 74
Cdd:PRK13549 1 MMEylLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 75 --RGVV--FQRYSVFPHLTVLGNVLLGREFSGarykaklFGAARRNAI-EEARQLIAEVGLAGSQDKYPAQLSGGMQQRL 149
Cdd:PRK13549 80 erAGIAiiHQELALVKELSVLENIFLGNEITP-------GGIMDYDAMyLRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190
....*....|....*....|....*....|....
gi 499747244 150 ALAQALIMKPKVLLLDEPFGALdpgIRAEIHTLM 183
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASL---TESETAVLL 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-211 |
1.12e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPP---EPGPDRGV--V 78
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpAKAHQLGIylV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 FQRYSVFPHLTVLGNVllgrefsgarykakLFGAARRNAIEE-ARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIM 157
Cdd:PRK15439 92 PQEPLLFPNLSVKENI--------------LFGLPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 158 KPKVLLLDEPFGALDPgirAEIHTLMKRLWHETQMTV--VMVTHDMREAFTLASRV 211
Cdd:PRK15439 158 DSRILILDEPTASLTP---AETERLFSRIRELLAQGVgiVFISHKLPEIRQLADRI 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-199 |
1.40e-12 |
|
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: 64.86 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQE--QPTKGKILLDGEPLPPEPGPDR-----G 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlgiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 77 VVFQRYSVFPHLTVLgnvllgrefsgarykaklfgaarrnaieearQLIAEVGlagsqdkypAQLSGGMQQRLALAQALI 156
Cdd:cd03217 81 LAFQYPPEIPGVKNA-------------------------------DFLRYVN---------EGFSGGEKKRNEILQLLL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 157 MKPKVLLLDEPFGALD-PGIRAEIHTLMKrlWHETQMTVVMVTH 199
Cdd:cd03217 121 LEPDLAILDEPDSGLDiDALRLVAEVINK--LREEGKSVLIITH 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-200 |
2.60e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 6 IEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIL----LDGEplppepgpdrgvVFQR 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtkLEVA------------YFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 Y--SVFPHLTVLGNVLLGR---EFSG-ARY-----KAKLFGAARrnaieeARQliaevglagsqdkyPAQ-LSGGMQQRL 149
Cdd:PRK11147 390 HraELDPEKTVMDNLAEGKqevMVNGrPRHvlgylQDFLFHPKR------AMT--------------PVKaLSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 150 ALAQaLIMKPKVLL-LDEPFGALDpgiraeIHT--LMKRLWHETQMTVVMVTHD 200
Cdd:PRK11147 450 LLAR-LFLKPSNLLiLDEPTNDLD------VETleLLEELLDSYQGTVLLVSHD 496
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-183 |
3.48e-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: 66.00 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLG--QEQPTKGKILLDGEPLPPEPGPD---RGVV 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDterAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 F--QRYSVFPHLTVLGNVLLGREFS--GARYKAKLFgaarrnaIEEARQLIAEVGLAGSQDKYP-AQLSGGMQQRLALAQ 153
Cdd:TIGR02633 82 IihQELTLVPELSVAENIFLGNEITlpGGRMAYNAM-------YLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190
....*....|....*....|....*....|
gi 499747244 154 ALIMKPKVLLLDEPFGALdpgIRAEIHTLM 183
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSL---TEKETEILL 181
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
113-218 |
3.98e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 113 ARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQm 192
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA- 195
|
90 100
....*....|....*....|....*.
gi 499747244 193 TVVMVTHDMREAFTLASRVVAFERRR 218
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGR 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-172 |
5.20e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 7 EKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPpepgpdrGVVFQ-RYSVF 85
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKL-------AYVDQsRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 PHLTV-------LGNVLLG-REFSgarykaklfgaarrnaieeARQLIAEVGLAGS-QDKYPAQLSGGMQQRLALAQALI 156
Cdd:PRK11819 401 PNKTVweeisggLDIIKVGnREIP-------------------SRAYVGRFNFKGGdQQKKVGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*.
gi 499747244 157 MKPKVLLLDEPFGALD 172
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD 477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-201 |
5.41e-12 |
|
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: 65.74 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLdgeplppepgpdRGVV--FQRYSVFPHLTVL 91
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVayVPQQAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 92 GNVLLGREFSGARYKAKLfgaarrnaieEARQLIAEVGLAGSQDKYP-----AQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:TIGR00957 717 ENILFGKALNEKYYQQVL----------EACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190
....*....|....*....|....*....|....*....
gi 499747244 167 PFGALDPGIRAEI--HTL--MKRLWHETQmtvVMVTHDM 201
Cdd:TIGR00957 787 PLSAVDAHVGKHIfeHVIgpEGVLKNKTR---ILVTHGI 822
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-172 |
5.69e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPT--KGKILLDGEPLPPEPGPDRGVVFQRY 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHLTVLGNVLLgreFSGARYKAKLfgaARRNAIEEARQLIAEVGLAGSQD-----KYPAQLSGGMQQRLALAQALIM 157
Cdd:PLN03211 150 ILYPHLTVRETLVF---CSLLRLPKSL---TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLI 223
|
170
....*....|....*
gi 499747244 158 KPKVLLLDEPFGALD 172
Cdd:PLN03211 224 NPSLLILDEPTSGLD 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
7.67e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---RGVVF-----QRYSVFPHLTV 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLG--REFSgaRYKAKLFGAARRNAIEEARQL--IAevglAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK10762 348 KENMSLTalRYFS--RAGGSLKHADEQQAVSDFIRLfnIK----TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499747244 167 PFGALDPGIRAEIHTLMKRLWHETqMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-215 |
9.16e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEplppepgpdrgVVF--QRYSVFPHLTV---LGNVllGREFSGARYK 106
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------ISYkpQYIKPDYDGTVedlLRSI--TDDLGSSYYK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 107 AKLfgaARRNAIEEarqLIaevglagsqDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRL 186
Cdd:PRK13409 435 SEI---IKPLQLER---LL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*....
gi 499747244 187 WHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-211 |
1.06e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 21 DVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR---GVVF-----QRYSVFPHLTVLG 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVllgrefSGARYKAKLFGA--ARRNAIEEarQLIAEVGLAGSQDKYPAQ-LSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK15439 361 NV------CALTHNRRGFWIkpARENAVLE--RYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499747244 170 ALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK15439 433 GVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRV 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-215 |
1.20e-11 |
|
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: 64.42 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEplppepgpdrgVVF--QRYSVFPHLTV---LGNVLlGREFSGARYK 106
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------ISYkpQYISPDYDGTVeefLRSAN-TDDFGSSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 107 AKLfgaARRNAIEEARqliaevglagsqDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRL 186
Cdd:COG1245 437 TEI---IKPLGLEKLL------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*....
gi 499747244 187 WHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:COG1245 502 AENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
110-211 |
1.30e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 110 FGAARRNAIEearqLIAEVGLAGSQD---KYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRL 186
Cdd:PRK15093 129 FGWRKRRAIE----LLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRL 204
|
90 100
....*....|....*....|....*
gi 499747244 187 WHETQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK15093 205 NQNNNTTILLISHDLQMLSQWADKI 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-179 |
1.30e-11 |
|
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: 64.46 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEplppepgpD---------R---GVVfqrysvf 85
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ--------DirdvtqaslRaaiGIV------- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 86 PHLTVL------GNVLLGREfsgarykaklfgAARRNAIEEARQLiAEVG--LAGSQDKYPAQ-------LSGGMQQRLA 150
Cdd:COG5265 438 PQDTVLfndtiaYNIAYGRP------------DASEEEVEAAARA-AQIHdfIESLPDGYDTRvgerglkLSGGEKQRVA 504
|
170 180
....*....|....*....|....*....
gi 499747244 151 LAQALIMKPKVLLLDEPFGALDPGIRAEI 179
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAI 533
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-194 |
1.31e-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: 64.55 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppepgPDRGvvfqRYSVFPHL------TVL 91
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KHSG----RISFSPQTswimpgTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 92 GNVLLGREFSGARYKaklfgaarrnAIEEARQLIAEVGLAGSQDKYP-----AQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:TIGR01271 505 DNIIFGLSYDEYRYT----------SVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190
....*....|....*....|....*....|
gi 499747244 167 PFGALDPGIRAEI--HTLMKRLWHETQMTV 194
Cdd:TIGR01271 575 PFTHLDVVTEKEIfeSCLCKLMSNKTRILV 604
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-199 |
1.36e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.30 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 7 EKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP---TKGKILLDGEPLPPEPGPDR-GVVFQRY 82
Cdd:TIGR00955 29 GCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIsAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHLTVLGNVLLGREFsgaRYKAKLFGAARRNAIEEarqLIAEVGLAGSQDK---YPAQ---LSGGMQQRLALAQALI 156
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHL---RMPRRVTKKEKRERVDE---VLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTH 199
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-212 |
1.60e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.96 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-RG---VVFQRYSVFPHlTV 90
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrlaVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLGREfsgarykaklfgAARRNAIEEARQLI--------------AEVGLAGsqdkypAQLSGGMQQRLALAQALI 156
Cdd:PRK10789 406 ANNIALGRP------------DATQQEIEHVARLAsvhddilrlpqgydTEVGERG------VMLSGGQKQRISIARALL 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499747244 157 MKPKVLLLDEPFGALDPGIRAEI-HTLmkRLWHEtQMTVVMVTHDMrEAFTLASRVV 212
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQIlHNL--RQWGE-GRTVIISAHRL-SALTEASEIL 520
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
139-211 |
1.82e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.82e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 139 AQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHEtQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRV 475
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-212 |
1.90e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 20 EDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD---RGVVF-----QRYSVFPHLTVL 91
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 92 GNVLLG--REFSgaryKAKLFGAARRNAiEEARQLIAEVGL-AGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PRK11288 350 DNINISarRHHL----RAGCLINNRWEA-ENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 169 GALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-201 |
3.65e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI-LLDGEPLPPEPGPDRGVVFQRYSV---FPHLtVLGNV 94
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRQALQKNLVAYVPQSEEVdwsFPVL-VEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 95 LLGRE-FSGARYKAKlfgAARRNAIEEArqlIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK15056 102 MMGRYgHMGWLRRAK---KRDRQIVTAA---LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*...
gi 499747244 174 GIRAEIHTLMKRLWHETQmTVVMVTHDM 201
Cdd:PRK15056 176 KTEARIISLLRELRDEGK-TMLVSTHNL 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-216 |
4.31e-11 |
|
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: 59.69 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 31 FVALVGPSGCGKTTFLRMLLGQEQPTKGKILLdgeplppepgpdrgvvfqrysvfphltvlgnvllgrefsgarykaklf 110
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 111 gaarrNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEI-----HTLMKR 185
Cdd:smart00382 36 -----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLL 110
|
170 180 190
....*....|....*....|....*....|.
gi 499747244 186 LWHETQMTVVMVTHDMREAFTLASRVVAFER 216
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-179 |
4.86e-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: 61.80 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppePGPDRGVVFQRYSVFPHLTVLGNVLLG 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHSGRISFSSQFSWIMPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 98 REFSGARYKaklfgaarrnAIEEARQLIAEVGLAGSQDKYP-----AQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03291 122 VSYDEYRYK----------SVVKACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
....*..
gi 499747244 173 PGIRAEI 179
Cdd:cd03291 192 VFTEKEI 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-199 |
6.86e-11 |
|
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: 60.59 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYGD--QIVLEDVSLTVASRAFVALVGPSGCGKTT----FLRMLlgqeQPTKGKILLDGEPLPPEPGPD-R 75
Cdd:cd03244 2 DIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 gvvfQRYSVFPHLTVLgnvllgreFSGA-RYKAKLFG----AARRNAIEEArQLIAEV-GLAGSQDKY----PAQLSGGM 145
Cdd:cd03244 78 ----SRISIIPQDPVL--------FSGTiRSNLDPFGeysdEELWQALERV-GLKEFVeSLPGGLDTVveegGENLSVGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499747244 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETqmTVVMVTH 199
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAH 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-215 |
9.09e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 36 GPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEpgpDRGVVFQRYSVFPHLTVLGNVLLGREFsgarykakLFGAARR 115
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLKADLSTLENLHF--------LCGLHGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 116 NAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP-GIRAEIHTLMKRLwhETQMTV 194
Cdd:PRK13543 113 RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLeGITLVNRMISAHL--RGGGAA 190
|
170 180
....*....|....*....|.
gi 499747244 195 VMVTHDMREAFTLASRVVAFE 215
Cdd:PRK13543 191 LVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-200 |
9.88e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 8 KVWKEYG-DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLppepgpdRGVVFQRYSVFP 86
Cdd:PRK11819 11 RVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIK-------VGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HLTVLGNVLLGRefsgARYKAKLfgaARRNAIEEA--------RQLIAEVG-LagsQDKYPAQ----------------- 140
Cdd:PRK11819 84 EKTVRENVEEGV----AEVKAAL---DRFNEIYAAyaepdadfDALAAEQGeL---QEIIDAAdawdldsqleiamdalr 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 141 ----------LSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgirAE-IHTLMKRLwHETQMTVVMVTHD 200
Cdd:PRK11819 154 cppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFL-HDYPGTVVAVTHD 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-201 |
1.06e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.07 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPT----------KGKILLDGEPLPPEPGPDR--GVVFQ--RYS 83
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKLSPRERRKIIGReiAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTV---LGNVLLGREFSGARYKakLFGAARRNAIEearqLIAEVGLAGSQD---KYPAQLSGGMQQRLALAQALIM 157
Cdd:COG4170 102 LDPSAKIgdqLIEAIPSWTFKGKWWQ--RFKWRKKRAIE----LLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDM 201
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDL 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-202 |
1.32e-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: 59.35 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKVWKEYGDQI--VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDrgvVFQ 80
Cdd:cd03369 6 EIEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVL--GNVLLGREFSGARYKAKLFGAARrnaieearqlIAEVGLagsqdkypaQLSGGMQQRLALAQALIMK 158
Cdd:cd03369 83 SLTIIPQDPTLfsGTIRSNLDPFDEYSDEEIYGALR----------VSEGGL---------NLSQGQRQLLCLARALLKR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWheTQMTVVMVTHDMR 202
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLR 185
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-215 |
1.73e-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: 58.74 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 5 KIEKVWKEYGDQIVLedVSLTVASRA-FVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEplppepgpdrgvvfqRYS 83
Cdd:cd03222 2 LYPDCVKRYGVFFLL--VELGVVKEGeVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI---------------TPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPhltvlgnvllgrefsgarykaklfgaarrnaieearQLIaevglagsqdkypaQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03222 65 YKP------------------------------------QYI--------------DLSGGELQRVAIAAALLRNATFYL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-211 |
1.96e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQeQPT---KGKILLDGEPLPPEPGPD---RGVVF--QRYSVFPHLTV 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDIRDseaLGIVIihQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 91 LGNVLLGREfsgaryKAKlFGAARRN-AIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:NF040905 96 AENIFLGNE------RAK-RGVIDWNeTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499747244 170 ALDPGIRAEIHTLMKRLWHETqMTVVMVTHDMREAFTLASRV 211
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQG-ITSIIISHKLNEIRRVADSI 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-200 |
2.61e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPlppepgpdRGVVFQRYSVfPHLTVLGNVLLgrefsgarYKAKLFG 111
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV--------RMAVFSQHHV-DGLDLSSNPLL--------YMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 112 AARRNAIeeaRQLIAEVGLAGS---QDKYpaQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD-PGIRAEIHTLMKrlw 187
Cdd:PLN03073 601 GVPEQKL---RAHLGSFGVTGNlalQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLVL--- 672
|
170
....*....|...
gi 499747244 188 heTQMTVVMVTHD 200
Cdd:PLN03073 673 --FQGGVLMVSHD 683
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-172 |
4.81e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 10 WKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLdgeplppepgpDRGVVF---QRYSVFp 86
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAyvpQVSWIF- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HLTVLGNVLLGREFSGARYKAklfgAARRNAIEEARQLIA-----EVGLAGsqdkypAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PLN03130 692 NATVRDNILFGSPFDPERYER----AIDVTALQHDLDLLPggdltEIGERG------VNISGGQKQRVSMARAVYSNSDV 761
|
170
....*....|.
gi 499747244 162 LLLDEPFGALD 172
Cdd:PLN03130 762 YIFDDPLSALD 772
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-216 |
6.07e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-----R 75
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDpprnvE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 76 GVVF--------------QRYSVFPHLtvlgnvlLGREFSG------ARYKAKLfgaARRNAIE-EAR--QLIAEVGLag 132
Cdd:PRK11147 81 GTVYdfvaegieeqaeylKRYHDISHL-------VETDPSEknlnelAKLQEQL---DHHNLWQlENRinEVLAQLGL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 133 SQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgiraeIHTLmkrLWHET-----QMTVVMVTHDmrEAF-- 205
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD------IETI---EWLEGflktfQGSIIFISHD--RSFir 217
|
250
....*....|.
gi 499747244 206 TLASRVVAFER 216
Cdd:PRK11147 218 NMATRIVDLDR 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-198 |
7.98e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 12 EYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplPPEPGPDRGV-------VFQRYSV 84
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE----RQSIKKDLCTyqkqlcfVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 85 FPHLTVLGNVLLGREFSGARYkaklfgaarrnaieEARQLIAEVGLAGSQDkYP-AQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAV--------------GITELCRLFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 499747244 164 LDEPFGALDpgiRAEIHTLMKRLW-HETQMTVVMVT 198
Cdd:PRK13540 151 LDEPLVALD---ELSLLTIITKIQeHRAKGGAVLLT 183
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-200 |
9.73e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRgVVFQRYS 83
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ-LEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFP--HLTVLgnvllgrefsgarykaklfgaARRNAIEEARQLIAEVGLAGSQDKYP-AQLSGGMQQRLALAQALIMKPK 160
Cdd:PRK10636 392 ESPlqHLARL---------------------APQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499747244 161 VLLLDEPFGALDPGIRaeiHTLMKRLWhETQMTVVMVTHD 200
Cdd:PRK10636 451 LLLLDEPTNHLDLDMR---QALTEALI-DFEGALVVVSHD 486
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-211 |
1.05e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.54 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGqEQPTKGKILLDgeplppepgpdrGVVFQRYSVfPHLtvlgnvllgr 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN------------GRPLSDWSA-AEL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 99 efsgARYKAKL-----------------FGAARRNAIEEARQLIAEV----GLAgsqDKYP---AQLSGGMQQRLALAQA 154
Cdd:COG4138 68 ----ARHRAYLsqqqsppfampvfqylaLHQPAGASSEAVEQLLAQLaealGLE---DKLSrplTQLSGGEWQRVRLAAV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 155 LIM-------KPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRV 211
Cdd:COG4138 141 LLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRV 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-200 |
1.67e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 34 LVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPpepgpdrGVVFQRYSVFPHLTVLGNVLLGREfsgARYKAKlfgaA 113
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERL-------GKLRQDQFAFEEFTVLDTVIMGHT---ELWEVK----Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 114 RRNAI----------------------------EEAR--QLIAEVGLAGSQDKYP-AQLSGGMQQRLALAQALIMKPKVL 162
Cdd:PRK15064 98 ERDRIyalpemseedgmkvadlevkfaemdgytAEARagELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 163 LLDEPFGALDpgiraeIHTLMkrlWHETQM-----TVVMVTHD 200
Cdd:PRK15064 178 LLDEPTNNLD------INTIR---WLEDVLnernsTMIIISHD 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-197 |
2.37e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 1 MSELKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGkilldgeplppepgpdrgvvfQ 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG---------------------E 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 RYSVFPHLTVLG----NVLLGREFSgaRYKAKL-------FGAARRNAIEE-----AR--QLIAEVGLAGSQDKYPAQLS 142
Cdd:PRK10938 60 RQSQFSHITRLSfeqlQKLVSDEWQ--RNNTDMlspgeddTGRTTAEIIQDevkdpARceQLAQQFGITALLDRRFKYLS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 143 GGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMV 197
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLV 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-201 |
3.10e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 10 WKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKgkilldgeplpPEPGPDRGVVF---QRYSVFp 86
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-----------TSSVVIRGSVAyvpQVSWIF- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 87 HLTVLGNVLLGREFSGARYKAKLFGAARRNAIE--EARQLiAEVGLAGsqdkypAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:PLN03232 692 NATVRENILFGSDFESERYWRAIDVTALQHDLDllPGRDL-TEIGERG------VNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190
....*....|....*....|....*....|....*....
gi 499747244 165 DEPFGALDPGIRAEI-HTLMKrlwHETQ-MTVVMVTHDM 201
Cdd:PLN03232 765 DDPLSALDAHVAHQVfDSCMK---DELKgKTRVLVTNQL 800
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-172 |
4.39e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDgeplppepgpdrGVVFQRY------------ 82
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD------------GHDLRDYtlaslrnqvalv 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 83 SVFPHL---TVLGNVLLGREfsgARYKaklfgaarRNAIEEARQL-----------------IAEVGlagsqdkypAQLS 142
Cdd:PRK11176 423 SQNVHLfndTIANNIAYART---EQYS--------REQIEEAARMayamdfinkmdngldtvIGENG---------VLLS 482
|
170 180 190
....*....|....*....|....*....|
gi 499747244 143 GGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-199 |
8.43e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLgQEQPTKGKILLDGEPLppepgpdRGVVFQR----YSVFPHLTVLgn 93
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSW-------NSVTLQTwrkaFGVIPQKVFI-- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 vllgreFSGArYKAKLFGAARRNAiEEARQLIAEVGLAGSQDKYPAQL-----------SGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR01271 1304 ------FSGT-FRKNLDPYEQWSD-EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190
....*....|....*....|....*....|....*..
gi 499747244 163 LLDEPFGALDPGIRAEIHTLMKRLWheTQMTVVMVTH 199
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEH 1410
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-207 |
8.75e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 9 VWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEP---LPPEPGPDRGV--VFQRYS 83
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGIsmVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPHLTVLGNVLLGrefsgaRYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK10982 84 LVLQRSVMDNMWLG------RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499747244 164 LDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTL 207
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQL 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-201 |
1.03e-08 |
|
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: 54.68 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTKGKiLLDGEPLPPEPGPDRGVVFQRYsvFPHLtVLGNV----------LLGREFS 101
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFRGSELQNY--FTKL-LEGDVkvivkpqyvdLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 102 GaRYKAKLFGAARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHT 181
Cdd:cd03236 105 G-KVGELLKKKDERGKLDE---LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180
....*....|....*....|
gi 499747244 182 LMKRLWHETQmTVVMVTHDM 201
Cdd:cd03236 181 LIRELAEDDN-YVLVVEHDL 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
1.06e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKI----------------------- 60
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydfendl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 61 -LLDGEPLPPEPGPD----RGVvfqrysvfphltvlgnvlLGRefsgarykaKLFGAarrnaiEEARqliaevglagsqd 135
Cdd:PRK15064 400 tLFDWMSQWRQEGDDeqavRGT------------------LGR---------LLFSQ------DDIK------------- 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499747244 136 KYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgiRAEIHTLMKRLwHETQMTVVMVTHDmREaF--TLASRVV 212
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD---MESIESLNMAL-EKYEGTLIFVSHD-RE-FvsSLATRII 506
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-173 |
1.06e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTT----FLRMLlgqeqPTKGKILLDgeplppepgpdrGVVFQRYSVFPHLT 89
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLL-----NTEGDIQID------------GVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 VLGNVllgrefsgaryKAKLF---GAARRN-------AIEEARQLIAEVGLAGSQDKYPAQL-----------SGGMQQR 148
Cdd:cd03289 78 AFGVI-----------PQKVFifsGTFRKNldpygkwSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180
....*....|....*....|....*
gi 499747244 149 LALAQALIMKPKVLLLDEPFGALDP 173
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDP 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-201 |
1.17e-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: 55.56 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppepgpDRGV----VFQRYS---VFPHLTVL--GNV-------- 94
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDY-------------DEEPswdeVLKRFRgteLQDYFKKLanGEIkvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 95 --LLGREFSGaRYKAKLFGAARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:COG1245 169 vdLIPKVFKG-TVRELLEKVDERGKLDE---LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*....
gi 499747244 173 PGIRAEIHTLMKRLwHETQMTVVMVTHDM 201
Cdd:COG1245 245 IYQRLNVARLIREL-AEEGKYVLVVEHDL 272
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-218 |
2.16e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 16 QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILldgeplppepgPDRGVVF--QRYSVFpHLTVLGN 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYvpQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 94 VLLGREFSGARykakLFGAARRNAIE-EARQLIA----EVGLAGsqdkypAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PTZ00243 741 ILFFDEEDAAR----LADAVRVSQLEaDLAQLGGgletEIGEKG------VNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499747244 169 GALDP--GIRAEIHTLMKRLWHETQmtvVMVTHDMrEAFTLASRVVAFERRR 218
Cdd:PTZ00243 811 SALDAhvGERVVEECFLGALAGKTR---VLATHQV-HVVPRADYVVALGDGR 858
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-199 |
3.14e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLL----------------------------GQEQPT------------- 56
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqGDEEQNvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 57 -------------KGKILLDGEPLPPEPGPDRGVVFQRYSVFP---HLTVLGNVLLGREfSGARYKAKLfgAARRNAIEE 120
Cdd:PTZ00265 1263 eggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPmlfNMSIYENIKFGKE-DATREDVKR--ACKFAAIDE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 121 -----ARQLIAEVGlagsqdKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVV 195
Cdd:PTZ00265 1340 fieslPNKYDTNVG------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
....
gi 499747244 196 MVTH 199
Cdd:PTZ00265 1414 TIAH 1417
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-212 |
5.10e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 17 IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQ--------EQPTKGKILLDGEPLPPEPGPD----RGVVFQRYS- 83
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprGARVTGDVTLNGEPLAAIDAPRlarlRAVLPQAAQp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 84 VFPhLTVLGNVLLGReFSGARYKaklfGAARRNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQAL-------- 155
Cdd:PRK13547 95 AFA-FSAREIVLLGR-YPHARRA----GALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 156 -IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQMTVVMVTHDMREAFTLASRVV 212
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIA 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-179 |
8.24e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-RGVVfqrySVFPHLTVLgnvll 96
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlRKVL----GIIPQAPVL----- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 97 greFSG-------------------ARYKAKLFGAARRNAieeaRQLIAEVGLAGSQdkypaqLSGGMQQRLALAQALIM 157
Cdd:PLN03130 1325 ---FSGtvrfnldpfnehndadlweSLERAHLKDVIRRNS----LGLDAEVSEAGEN------FSVGQRQLLSLARALLR 1391
|
170 180
....*....|....*....|..
gi 499747244 158 KPKVLLLDEPFGALDPGIRAEI 179
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALI 1413
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-200 |
8.94e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 8.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 31 FVALVGPSGCGKTTF---LRMLLGQEQPTKGKilldgeplppepgpdrGVVFQRySVFPHLTVLGNVLLG-REFSGARYK 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIieaLKYALTGELPPNSK----------------GGAHDP-KLIREGEVRAQVKLAfENANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 107 AKLFGAARRNAI----EEARQLIAEVglagsqdkyPAQLSGGmQQ-------RLALAQALIMKPKVLLLDEPFGALDPG- 174
Cdd:cd03240 87 ITRSLAILENVIfchqGESNWPLLDM---------RGRCSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEEn 156
|
170 180
....*....|....*....|....*.
gi 499747244 175 IRAEIHTLMKRLWHETQMTVVMVTHD 200
Cdd:cd03240 157 IEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-166 |
1.10e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDRGVVFQRYSVFPHLTVLGNV 94
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 95 LLGREFSgarykaklfgaarrNAIEEARQLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK13541 92 KFWSEIY--------------NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-215 |
1.13e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.49 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 34 LVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPD-R---GVVFQRYSVFPHltvlgnvllgrefsgarykakL 109
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRqlfSAVFSDFHLFDR---------------------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 110 FGAARRNAIEEARQLIAEVGLagsQDKYPAQ--------LSGGMQQRLALAQALIMKPKVLLLDEpFGA-LDPGIRA--- 177
Cdd:COG4615 422 LGLDGEADPARARELLERLEL---DHKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDE-WAAdQDPEFRRvfy 497
|
170 180 190
....*....|....*....|....*....|....*....
gi 499747244 178 -EIHTLMKRLWHetqmTVVMVTHDMReAFTLASRVVAFE 215
Cdd:COG4615 498 tELLPELKARGK----TVIAISHDDR-YFDLADRVLKMD 531
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-200 |
1.54e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 22 VSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDR----GVVFQRYSVFPHLtvLGNVllG 97
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYrklfSAVFTDFHLFDQL--LGPE--G 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 98 REFSGARYKAKLFGAARRNAIEEARQLIAEVglagsqdkypaQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRA 177
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLELEDGRISNL-----------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180
....*....|....*....|...
gi 499747244 178 EIHTLMKRLWHETQMTVVMVTHD 200
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-211 |
1.84e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQeQPTKGKILLDGEPLPPEPGPD----RGVVFQRYS------VFPHL 88
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarhRAYLSQQQTppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 89 TvlgnvllgrefsgarykakLFGAARRNAIEEARQLIAEVGLAGSQDKYP---AQLSGGMQQRLALAQALI-----MKP- 159
Cdd:PRK03695 91 T-------------------LHQPDKTRTEAVASALNEVAEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINPa 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499747244 160 -KVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMREAFTLASRV 211
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRV 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-200 |
3.13e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 2 SELKIEKvwkeyGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLlgqeqptKGKILLDGEPLPPEPGPDRGVVFQR 81
Cdd:PRK10636 5 SSLQIRR-----GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQLAWVNQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 82 YsvfPHLTV--LGNVLLG-REFSgaRYKAKLFGAARRN-------------AIE------EARQLIAEVGLAGSQDKYPA 139
Cdd:PRK10636 73 T---PALPQpaLEYVIDGdREYR--QLEAQLHDANERNdghaiatihgkldAIDawtirsRAASLLHGLGFSNEQLERPV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 140 Q-LSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgIRAEIhtLMKRLWHETQMTVVMVTHD 200
Cdd:PRK10636 148 SdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI--WLEKWLKSYQGTLILISHD 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-195 |
3.37e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 18 VLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDrgvVFQRYSVFPHLTVL--GNVL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQSPVLfsGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 96 LGREFSGARYKAKLFGAARRNAIEEARQ-----LIAEVGLAGSQdkypaqLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:PLN03232 1328 FNIDPFSEHNDADLWEALERAHIKDVIDrnpfgLDAEVSEGGEN------FSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180
....*....|....*....|....*
gi 499747244 171 LDPGIRAEIHTLMKRLWHETQMTVV 195
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVI 1426
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-172 |
4.09e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 15 DQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEP-----GPDRGVVFQ--------- 80
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInlkwwRSKIGVVSQdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 81 ----RYSVFP--HLTVLGNVLLGREFSG-------ARYKAKLFGA---------------ARRN--------AIEEARQL 124
Cdd:PTZ00265 477 knniKYSLYSlkDLEALSNYYNEDGNDSqenknkrNSCRAKCAGDlndmsnttdsnelieMRKNyqtikdseVVDVSKKV 556
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 125 IAEVGLAGSQDKY-------PAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PTZ00265 557 LIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-199 |
4.24e-07 |
|
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: 49.16 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP--TKGKILLDGEPLPPEPGPDRGVVFQRYSVFPHLTVlgnvll 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTV------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 97 gREfsgarykAKLFGAARRnaieearqliaevGLAGSQDKypaqlsggmqqRLALAQALIMKPKVLLLDEPFGALDPGIR 176
Cdd:cd03232 97 -RE-------ALRFSALLR-------------GLSVEQRK-----------RLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|...
gi 499747244 177 AEIHTLMKRLwHETQMTVVMVTH 199
Cdd:cd03232 145 YNIVRFLKKL-ADSGQAILCTIH 166
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-199 |
1.09e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 14 GDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLR--------------MLLGQEQPTKG------KILLDGEPLPPEPGP 73
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncQILHVEQEVVGddttalQCVLNTDIERTQLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 74 D--RGVVFQRYSVFPHLTVLGNVLLGREFSGARYKAKLFGAARR-NAIE----EARQLIAEVGLAGS---QDKYPAQLSG 143
Cdd:PLN03073 268 EeaQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRlELIDaytaEARAASILAGLSFTpemQVKATKTFSG 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499747244 144 GMQQRLALAQALIMKPKVLLLDEPFGALDpgiraeIHTLmkrLWHETQM-----TVVMVTH 199
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLD------LHAV---LWLETYLlkwpkTFIVVSH 399
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-199 |
1.24e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 16 QIVLEDVSLTVASRAFVALVGPSGCGKTTFLRmLLGQEQPTKGKILldgeplppePGPDRGVVF---QRysvfPHLTvLG 92
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRL---------TKPAKGKLFyvpQR----PYMT-LG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 NVllgRE-----FSGARYKAKLFGAARRNAIEEARQLI----AEVGLAGSQDkYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:TIGR00954 530 TL---RDqiiypDSSEDMKRRGLSDKDLEQILDNVQLThileREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 499747244 164 LDEPFGALDPgiraEIHTLMKRLWHETQMTVVMVTH 199
Cdd:TIGR00954 606 LDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-173 |
1.78e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 12 EYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQ-------------EQPTKGKILLDGEPLPpepgpdrGVV 78
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGETIWDIKKHI-------GYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 79 fqrySVFPHL-----TVLGNVLLgrefSGARYKAKLFGAARRNAIEEARQLIAEVGLAGSQDKYPAQ-LSGGmQQRLAL- 151
Cdd:PRK10938 342 ----SSSLHLdyrvsTSVRNVIL----SGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWG-QQRLALi 412
|
170 180
....*....|....*....|..
gi 499747244 152 AQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-212 |
2.63e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 2.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499747244 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMREAFTLASRVV 212
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRIL 462
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-196 |
3.67e-06 |
|
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: 46.49 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPT---KGKILLDGEPLPPEPGPDRG-VVF--QRYSVFPHLTVlg 92
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGeIIYvsEEDVHFPTLTV-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 93 nvllgrefsgarykaklfgaarRNAIEEARQLIAevglagsqDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03233 101 ----------------------RETLDFALRCKG--------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|....
gi 499747244 173 PGIRAEIHTLMKRLWHETQMTVVM 196
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFV 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-172 |
7.72e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 47.25 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 17 IVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKILLDGEPLPPEPGPDrgVVFQrYSVFPHLTVLgnvll 96
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD--LRFK-ITIIPQDPVL----- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 97 greFSGA-RYKAKLFGAARRNAIEEARQLIAEVGLAGSQ-DKYPAQ-------LSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:TIGR00957 1372 ---FSGSlRMNLDPFSQYSDEEVWWALELAHLKTFVSALpDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
....*
gi 499747244 168 FGALD 172
Cdd:TIGR00957 1449 TAAVD 1453
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-203 |
2.11e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499747244 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHDMRE 203
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPE 466
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-186 |
9.25e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 3 ELKIEKvwkeyGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQP---TKGKILLDGEPLPPEPGPDRGVVF 79
Cdd:TIGR00956 768 EVKIKK-----EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 80 QRYSVFPHLTVlgnvllgRE---FSGA-RYKAKLFGAARRNAIEEARQLI-------AEVGLAGSqdkypaQLSGGMQQR 148
Cdd:TIGR00956 843 QQDLHLPTSTV-------REslrFSAYlRQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPGE------GLNVEQRKR 909
|
170 180 190
....*....|....*....|....*....|....*....
gi 499747244 149 LALAQALIMKPKVLL-LDEPFGALDPGIRAEIHTLMKRL 186
Cdd:TIGR00956 910 LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
138-200 |
1.15e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 1.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 138 PAQLSGGMQQRLALAQALI---MKPKVLLLDEPFGALDPGIRAEIHTLMKRLwHETQMTVVMVTHD 200
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKEL-SRNGAQLILTTHS 298
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-215 |
1.95e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 19 LEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQEQPTKGKIlldgeplppEPGPDRGVVFQRYSVFPHLTVLGNVllgr 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---------DRNGEVSVIAISAGLSGQLTGIENI---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 99 EFsgaryKAKLFGAARRNAIEEARQLI--AEVGLAGSQ--DKYpaqlSGGMQQRLALAQALIMKPKVLLLDEpfgALDPG 174
Cdd:PRK13546 107 EF-----KMLCMGFKRKEIKAMTPKIIefSELGEFIYQpvKKY----SSGMRAKLGFSINITVNPDILVIDE---ALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499747244 175 IRAEIHTLMKRLWH--ETQMTVVMVTHDMREAFTLASRVVAFE 215
Cdd:PRK13546 175 DQTFAQKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIE 217
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
32-57 |
2.07e-04 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 40.55 E-value: 2.07e-04
10 20
....*....|....*....|....*.
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQEQPTK 57
Cdd:COG4917 4 IMLIGRSGAGKTTLTQALNGEELEYR 29
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-201 |
3.42e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 32 VALVGPSGCGKTTFLRMLLGQ---------EQPTKGKILldgeplppepGPDRGVVFQRYsvFPHLtVLGNV-------- 94
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVL----------KRFRGTELQNY--FKKL-YNGEIkvvhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 95 --LLGREFSGaRYKAKLFGAARRNAIEEarqLIAEVGLAGSQDKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK13409 169 vdLIPKVFKG-KVRELLKKVDERGKLDE---VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 499747244 173 PGIRAEIHTLMKRLWHETqmTVVMVTHDM 201
Cdd:PRK13409 245 IRQRLNVARLIRELAEGK--YVLVVEHDL 271
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
141-202 |
8.20e-04 |
|
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: 39.23 E-value: 8.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499747244 141 LSGGMQQRLALAQALIMKPK--VLLLDEPFGALDPGIRAEIHTLMKRLWHETQmTVVMVTHDMR 202
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD 150
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
29-52 |
9.82e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.77 E-value: 9.82e-04
10 20
....*....|....*....|....
gi 499747244 29 RAFVALVGPSGCGKTTFLRMLLGQ 52
Cdd:COG3267 43 GGFVVLTGEVGTGKTTLLRRLLER 66
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-201 |
3.27e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 3.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499747244 141 LSGGMQQRLALAQALIM---KPKVLLLDEPFGALDP-GIRAEIHTLMKrLWHETQmTVVMVTHDM 201
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHThDIKALIYVLQS-LTHQGH-TVVIIEHNM 872
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-200 |
3.44e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.34 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499747244 140 QLSGGMQQRLALAQALI---MKPKVL-LLDEPFGALDP-GIRAEIHTLMKRLWHETQMTVvmVTHD 200
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPrDGQALAEAILEHLVKGAQVIV--ITHL 140
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-202 |
4.22e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 37.70 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 4 LKIEKVWKEYGDQIVLEDVSLTVASRAFVALVGPSGCGKTTFLRMLLGQE--QPTKGKILLDGEPLPPEPGPDR---GV- 77
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 78 -VFQrYSV-FPHLTvlgnvllGREFSGARYKAKL--FGAARRNAIEEARQLIAEVGLAGSQDKYPAQ-----LSGGMQQR 148
Cdd:CHL00131 88 lAFQ-YPIeIPGVS-------NADFLRLAYNSKRkfQGLPELDPLEFLEIINEKLKLVGMDPSFLSRnvnegFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499747244 149 LALAQALIMKPKVLLLDEPFGALD----PGIRAEIHTLMKrlwheTQMTVVMVTHDMR 202
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMT-----SENSIILITHYQR 212
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-200 |
6.01e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.91 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 28 SRAFVALVGPSGCGKTTFL---RMLLGQEQPTKGKILLDGEPLPPEPGPDRgVVF----QRYSV---------FPHLT-- 89
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILeaiRYALYGKARSRSKLRSDLINVGSEEASVE-LEFehggKRYRIerrqgefaeFLEAKps 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499747244 90 ----VLGNVLLGREFSGARYKAKLFGAARRNAIEEARQLIA---EVGLAGSQDKYPAQLSGGMQQRLALAQALimkpkVL 162
Cdd:COG0419 101 erkeALKRLLGLEIYEELKERLKELEEALESALEELAELQKlkqEILAQLSGLDPIETLSGGERLRLALADLL-----SL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 499747244 163 LLDepFGALDPGIRAEIHTLMKRLwhetqmtvVMVTHD 200
Cdd:COG0419 176 ILD--FGSLDEERLERLLDALEEL--------AIITHV 203
|
|
| |
