|
Name |
Accession |
Description |
Interval |
E-value |
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-264 |
1.91e-165 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 458.40 E-value: 1.91e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPMRGTAADMQIVENLALAARRGESRGLSWGITRDERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLL 160
Cdd:COG1101 81 YIGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDEKRRLR 240
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKLT 240
|
250 260
....*....|....*....|....
gi 2506233547 241 VHDLLQKFEEASGGELANDRMLLS 264
Cdd:COG1101 241 VEDLLELFEEIRGEELADDRLLLG 264
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-228 |
4.52e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.05 E-value: 4.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRA- 79
Cdd:COG1136 4 LLELRNLTKSY-GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 ---TDLGRVFQD----PmrgtaaDMQIVENLALAARRGesrglswGITRDERasyRERLAEL--DLGLEERLTSKVGLLS 150
Cdd:COG1136 83 lrrRHIGFVFQFfnllP------ELTALENVALPLLLA-------GVSRKER---RERARELleRVGLGDRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 151 GGQRQ------AL----TLLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMnDAIRLGNRLI 220
Cdd:COG1136 147 GGQQQrvaiarALvnrpKLILA----------DEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVI 215
|
....*...
gi 2506233547 221 MMHEGNVI 228
Cdd:COG1136 216 RLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-227 |
6.01e-47 |
|
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: 155.73 E-value: 6.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHR---- 77
Cdd:cd03255 1 IELKNLSKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 RATDLGRVFQD----PmrgtaaDMQIVENLALAARrgesrglswgITRDERASYRERLAEL--DLGLEERLTSKVGLLSG 151
Cdd:cd03255 80 RRRHIGFVFQSfnllP------DLTALENVELPLL----------LAGVPKKERRERAEELleRVGLGDRLNHYPSELSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 152 GQRQ------ALT----LLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAiRLGNRLIM 221
Cdd:cd03255 144 GQQQrvaiarALAndpkIILA----------DEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIE 212
|
....*.
gi 2506233547 222 MHEGNV 227
Cdd:cd03255 213 LRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-238 |
8.53e-46 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 153.36 E-value: 8.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT- 80
Cdd:cd03219 1 LEVRGLTKRFGGLV-----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPmrGTAADMQIVENLALAARRGESRGLSWGITRDERASYRERLAEL--DLGLEERLTSKVGLLSGGQRQALT 158
Cdd:cd03219 76 GIGRTFQIP--RLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAEELleRVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDEKRR 238
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
3.43e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 152.13 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLP-----E 75
Cdd:COG3638 2 MLELRNLSKRYP----GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgralrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 76 HRRatDLGRVFQDPmrgtaadmQIVENL-----ALAARRGES---RGLSWGITRDERASYRERLAELdlGLEERLTSKVG 147
Cdd:COG3638 78 LRR--RIGMIFQQF--------NLVPRLsvltnVLAGRLGRTstwRSLLGLFPPEDRERALEALERV--GLADKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 148 LLSGGQRQ------AL----TLLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGN 217
Cdd:COG3638 146 QLSGGQQQrvaiarALvqepKLILA----------DEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYAD 215
|
250
....*....|...
gi 2506233547 218 RLIMMHEGNVIFD 230
Cdd:COG3638 216 RIIGLRDGRVVFD 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-228 |
3.49e-45 |
|
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: 151.13 E-value: 3.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatD 81
Cdd:cd03259 1 LELKGLSKTYG-----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrgtaA---DMQIVENLALAARRGesrglswGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALT 158
Cdd:cd03259 74 IGMVFQDY-----AlfpHLTVAENIAFGLKLR-------GVPKAEIRARVRELLEL-VGLEGLLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
3.76e-41 |
|
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: 141.72 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG1120 1 MLEAENLSVGYGGRPV-----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPmrGTAADMQiVENLALAARRGESRGLSWGITRDERASyRERLAELDL-GLEERLtskVGLLSGGQRQ---- 155
Cdd:COG1120 76 RIAYVPQEP--PAPFGLT-VRELVALGRYPHLGLFGRPSAEDREAV-EEALERTGLeHLADRP---VDELSGGERQrvli 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 --ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:COG1120 149 arALAqepplLLL-----------DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
..
gi 2506233547 229 FD 230
Cdd:COG1120 218 AQ 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
9.31e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.00 E-value: 9.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRlPEHRRAT 80
Cdd:COG1116 7 ALELRGVSKRFPTGG-GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 dlgrVFQDPM----RgTAADmqiveNLALAARRGesrglswGITRDERasyRERLAE-LDL-GLEERLTSKVGLLSGGQR 154
Cdd:COG1116 85 ----VFQEPAllpwL-TVLD-----NVALGLELR-------GVPKAER---RERARElLELvGLAGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 155 Q------ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMM 222
Cdd:COG1116 145 QrvaiarALAndpevLLM-----------DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-230 |
1.11e-40 |
|
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: 139.78 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:COG1122 1 IELENLSFSYP----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrgtaaDMQIV-----ENLALAARRgesrglsWGITRDERasyRERLAEL--DLGLEERLTSKVGLLSGGQR 154
Cdd:COG1122 77 VGLVFQNP------DDQLFaptveEDVAFGPEN-------LGLPREEI---RERVEEAleLVGLEHLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 Q--AL---------TLLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMH 223
Cdd:COG1122 141 QrvAIagvlamepeVLVL-----------DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLD 208
|
....*..
gi 2506233547 224 EGNVIFD 230
Cdd:COG1122 209 DGRIVAD 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-228 |
1.48e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.93 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRat 80
Cdd:COG3842 5 ALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQD----PMrgtaadMQIVENLALAARRgesRGLSwgitRDERasyRERLAE-LDL-GLEERLTSKVGLLSGGQR 154
Cdd:COG3842 78 NVGMVFQDyalfPH------LTVAENVAFGLRM---RGVP----KAEI---RARVAElLELvGLEGLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 Q------ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMH 223
Cdd:COG3842 142 QrvalarALApeprvLLL-----------DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMN 210
|
....*
gi 2506233547 224 EGNVI 228
Cdd:COG3842 211 DGRIE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-235 |
1.99e-40 |
|
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: 145.82 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG---GQVILDGRDVSRLPEHR 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDV---PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 RATDLGRVFQDPMrgTAADMQIVEN-LALAARRGesrglswGITRDERasyRERLAEL--DLGLEERLTSKVGLLSGGQR 154
Cdd:COG1123 81 RGRRIGMVFQDPM--TQLNPVTVGDqIAEALENL-------GLSRAEA---RARVLELleAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDD 234
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
.
gi 2506233547 235 E 235
Cdd:COG1123 229 E 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
6.71e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.27 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAtD 81
Cdd:COG1131 1 IEVRGLTKRYGD-----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrGTAADMQIVENLALAARrgesrglSWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:COG1131 75 IGYVPQEP--ALYPDLTVRENLRFFAR-------LYGLPRKEARERIDELLEL-FGLTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-235 |
4.57e-39 |
|
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: 142.35 E-value: 4.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRR-- 78
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 -ATDLGRVFQDPMRGTAADMQIVENLALAARRgesRGLswgITRDERasyRERLAEL--DLGLEERLTSK-VGLLSGGQR 154
Cdd:COG1123 340 lRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRL---HGL---LSRAER---RERVAELleRVGLPPDLADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 Q------ALT----LLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHE 224
Cdd:COG1123 411 QrvaiarALAlepkLLIL----------DEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250
....*....|.
gi 2506233547 225 GNVIFDARDDE 235
Cdd:COG1123 481 GRIVEDGPTEE 491
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
1.98e-38 |
|
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: 134.78 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG0411 4 LLEVRGLTKRFGGLV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 D-LGRVFQDPmrGTAADMQIVENLALAARRGESRGL------SWGITRDERASYRERLAELD-LGLEERLTSKVGLLSGG 152
Cdd:COG0411 79 LgIARTFQNP--RLFPELTVLENVLVAAHARLGRGLlaallrLPRARREEREARERAEELLErVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 153 QRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMnDAI-RLGNRLIMMHEGNVIFD 230
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM-DLVmGLADRIVVLDFGRVIAE 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-225 |
4.75e-38 |
|
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: 132.59 E-value: 4.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 3 VLKGVTKTFNKStvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDL 82
Cdd:cd03225 1 ELKNLSFSYPDG---ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQDPmrgtaaDMQIV-----ENLALAARRgesrglsWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQAL 157
Cdd:cd03225 78 GLVFQNP------DDQFFgptveEEVAFGLEN-------LGLPEEEIEERVEEALEL-VGLEGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-235 |
1.75e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 131.40 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD-LGRVFQDpmRGTAADMQ 98
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEG--RRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 99 IVENLALAARRGESRGLSWGItrderasyrERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAA 178
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARL---------ERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 179 LDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:cd03224 163 LAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-232 |
6.41e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-----PE 75
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreiPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 76 HRRatDLGRVFQD----PmrgtaaDMQIVENLALAARrgesrglswgITRDERASYRERLAE-LDL-GLEERLTSKVGLL 149
Cdd:COG2884 77 LRR--RIGVVFQDfrllP------DRTVYENVALPLR----------VTGKSRKEIRRRVREvLDLvGLSDKAKALPHEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 150 SGGQRQ------AL----TLLMAilkkpkllllDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRL 219
Cdd:COG2884 139 SGGEQQrvaiarALvnrpELLLA----------DEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRV 207
|
250
....*....|...
gi 2506233547 220 IMMHEGNVIFDAR 232
Cdd:COG2884 208 LELEDGRLVRDEA 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-235 |
1.11e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.49 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNekpaltgVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLR-------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLgrVFQD----PmrgtaaDMQIVENLALaarrgesrGLSWG--ITRDERASYRERLAEldLGLEERLTSKVGLLSGGQR 154
Cdd:COG3840 74 SM--LFQEnnlfP------HLTVAQNIGL--------GLRPGlkLTAEQRAQVEQALER--VGLAGLLDRLPGQLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDD 234
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
.
gi 2506233547 235 E 235
Cdd:COG3840 216 A 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-230 |
1.63e-36 |
|
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: 129.61 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDV-----SRLPEH 76
Cdd:cd03256 1 IEVENLSKTYP----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRatDLGRVFQDPmrgtaadmQIVENL--------ALAARRGESRGLSWGITRDERASYRERLAelDLGLEERLTSKVGL 148
Cdd:cd03256 77 RR--QIGMIFQQF--------NLIERLsvlenvlsGRLGRRSTWRSLFGLFPKEEKQRALAALE--RVGLLDKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 149 LSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
..
gi 2506233547 229 FD 230
Cdd:cd03256 225 FD 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
2.48e-36 |
|
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: 128.94 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRA- 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 --TDLGRVFQDpmrgtAA---DMQIVENLALAARrgESRGLSWGITRdERAsyRERLAELDL-GLEERLTSKvglLSGGQ 153
Cdd:COG1127 80 lrRRIGMLFQG-----GAlfdSLTVFENVAFPLR--EHTDLSEAEIR-ELV--LEKLELVGLpGAADKMPSE---LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 154 RQ------ALTL----LMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMH 223
Cdd:COG1127 147 RKrvalarALALdpeiLLY----------DEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
....*..
gi 2506233547 224 EGNVIFD 230
Cdd:COG1127 217 DGKIIAE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-228 |
2.80e-36 |
|
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: 128.39 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHR--- 77
Cdd:cd03257 1 LLEVKNLSVSF-PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 RATDLGRVFQDPM-----RGTAADmQIVENLalaarrgesrgLSWGITRDERAsYRERLAELDLGL---EERLTSKVGLL 149
Cdd:cd03257 80 RRKEIQMVFQDPMsslnpRMTIGE-QIAEPL-----------RIHGKLSKKEA-RKEAVLLLLVGVglpEEVLNRYPHEL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-228 |
6.47e-36 |
|
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: 126.01 E-value: 6.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 16 VNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQdpmrgtaa 95
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 dmqivenlALAArrgesrglswgitrderasyrerlaeldLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:cd03214 81 --------ALEL----------------------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 176 TAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-222 |
1.34e-35 |
|
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: 126.43 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRratd 81
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 lGRVFQD----PMRgtaadmQIVENLALAARRGesrglswGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQAL 157
Cdd:cd03293 76 -GYVFQQdallPWL------TVLDNVALGLELQ-------GVPKAEARERAEELLEL-VGLSGFENAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMM 222
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
1.34e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.81 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRat 80
Cdd:COG3839 3 SLELENVSKSYGG-----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDP-----MrgTAAdmqivENLALAAR-RGESRGlswgiTRDERAsyrERLAELdLGLEERLTSKVGLLSGGQR 154
Cdd:COG3839 76 NIAMVFQSYalyphM--TVY-----ENIAFPLKlRKVPKA-----EIDRRV---REAAEL-LGLEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 Q------ALT-----LLMailkkpkllllDEHTAALDPKtaSKVLALTE--RLVGEHGLTTLMVTHNMNDAIRLGNRLIM 221
Cdd:COG3839 140 QrvalgrALVrepkvFLL-----------DEPLSNLDAK--LRVEMRAEikRLHRRLGTTTIYVTHDQVEAMTLADRIAV 206
|
....*.
gi 2506233547 222 MHEGNV 227
Cdd:COG3839 207 MNDGRI 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-254 |
7.79e-35 |
|
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: 125.30 E-value: 7.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG1124 1 MLEVRNLSVSY-GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPMrgTAAD--MQIVENLALAARrgesrglswgITRdeRASYRERLAEL--DLGLEER-LTSKVGLLSGGQRQ 155
Cdd:COG1124 80 RVQMVFQDPY--ASLHprHTVDRILAEPLR----------IHG--LPDREERIAELleQVGLPPSfLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
250
....*....|....*....
gi 2506233547 236 KRRLRVHDLLQKFEEASGG 254
Cdd:COG1124 226 LLAGPKHPYTRELLAASLA 244
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-225 |
1.03e-34 |
|
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: 123.07 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL----PEHR 77
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 RatDLGRVFQDPmrGTAADMQIVENLALAarrgesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQAL 157
Cdd:cd03229 76 R--RIGMVFQDF--ALFPHLTVLENIALG------------------------------------------LSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
1.70e-34 |
|
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: 123.85 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPE----H 76
Cdd:cd03258 1 MIELKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRAtDLGRVFQDpmRGTAADMQIVENLALAARrgesrglSWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQA 156
Cdd:cd03258 80 ARR-RIGMIFQH--FNLLSSRTVFENVALPLE-------IAGVPKAEIEERVLELLEL-VGLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 157 LTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-227 |
1.95e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.00 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 15 TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL--PEHRRatDLGRVFQDP--M 90
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMppPEWRR--QVAYVPQEPalW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 91 RGTAADmqiveNLALAARRgesRGLSWGITRDERAsyrerLAELDLGlEERLTSKVGLLSGGQRQALTLLMAILKKPKLL 170
Cdd:COG4619 87 GGTVRD-----NLPFPFQL---RERKFDRERALEL-----LERLGLP-PDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 171 LLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-235 |
7.68e-34 |
|
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: 122.23 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRR---AT 80
Cdd:cd03261 3 LRGLTKSFGGRTV-----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDpmrgtAA---DMQIVENLALAARRGesrglswgiTRDERASYRERLAE-LDL-GLEERLTSKVGLLSGGQRQ 155
Cdd:cd03261 78 RMGMLFQS-----GAlfdSLTVFENVAFPLREH---------TRLSEEEIREIVLEkLEAvGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-239 |
1.24e-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: 121.63 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKStvnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAt 80
Cdd:COG0410 3 MLEVENLHAGYGGI-----HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLG--------RVFqdpmrgtaADMQIVENLALAARrgesrglswgiTRDERASYRERLAE-LDL--GLEERLTSKVGLL 149
Cdd:COG0410 77 RLGigyvpegrRIF--------PSLTVEENLLLGAY-----------ARRDRAEVRADLERvYELfpRLKERRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 150 SGGQRQALT----------LLMailkkpklllLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRL 219
Cdd:COG0410 138 SGGEQQMLAigralmsrpkLLL----------LDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRA 206
|
250 260
....*....|....*....|....*.
gi 2506233547 220 IMMHEGNVIFD------ARDDEKRRL 239
Cdd:COG0410 207 YVLERGRIVLEgtaaelLADPEVREA 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-231 |
1.72e-33 |
|
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: 121.64 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR-----LPE 75
Cdd:TIGR02315 1 MLEVENLSKVYP----NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 76 HRRATdlGRVFQDpmrgtaadMQIVENLA-----LAARRGESRGLSWGITRDERASYRERLAELD-LGLEERLTSKVGLL 149
Cdd:TIGR02315 77 LRRRI--GMIFQH--------YNLIERLTvlenvLHGRLGYKPTWRSLLGRFSEEDKERALSALErVGLADKAYQRADQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIF 229
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
..
gi 2506233547 230 DA 231
Cdd:TIGR02315 227 DG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-247 |
3.79e-33 |
|
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: 120.73 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAt 80
Cdd:COG4555 1 MIEVENLSKKYGK-----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDpmRGTAADMQIVENLALAARrgesrglSWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTLL 160
Cdd:COG4555 75 QIGVLPDE--RGLYDRLTVRENIRYFAE-------LYGLFDEELKKRIEELIEL-LGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDEKRRLR 240
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
....*..
gi 2506233547 241 VHDLLQK 247
Cdd:COG4555 224 GEENLED 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-230 |
1.58e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 119.84 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDG---RDVSRLPEHRRAtdLGRVFQDPmrgt 93
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtLDEENLWEIRKK--VGMVFQNP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 aaDMQIV------------ENLalaarrgesrglswGITRDErasYRERLAE-LDL-GLEERLTSKVGLLSGGQRQ--AL 157
Cdd:TIGR04520 87 --DNQFVgatveddvafglENL--------------GVPREE---MRKRVDEaLKLvGMEDFRDREPHLLSGGQKQrvAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 158 TLLMA------ILkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIrLGNRLIMMHEGNVIFD 230
Cdd:TIGR04520 148 AGVLAmrpdiiIL--------DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAE 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-228 |
5.58e-32 |
|
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: 117.44 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatDLGRVFQD----PmrgtaaDM 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVPQNyalfP------HM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAARrgesrglswgITRDERASYRERLAEL--DLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:cd03299 87 TVYKNIAYGLK----------KRKVDKKEIERKVLEIaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 176 TAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-231 |
6.31e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRA- 79
Cdd:COG1126 1 MIEIENLHKSFGDLEV-----LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 -TDLGRVFQD----PmrgtaaDMQIVENLALAARRgeSRGLSwgitrdeRASYRER-LAELD-LGLEERLTSKVGLLSGG 152
Cdd:COG1126 76 rRKVGMVFQQfnlfP------HLTVLENVTLAPIK--VKKMS-------KAEAEERaMELLErVGLADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 153 QRQ------ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIM 221
Cdd:COG1126 141 QQQrvaiarALAmepkvMLF-----------DEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVF 208
|
250
....*....|
gi 2506233547 222 MHEGNVIFDA 231
Cdd:COG1126 209 MDGGRIVEEG 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-228 |
8.59e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.41 E-value: 8.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGvfaL---DGGQVILDGRDVSRLPEH- 76
Cdd:COG1135 1 MIELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LerpTSGSVLVDGVDLTALSERe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 ----RRatDLGRVFQDP---MRGTAAdmqivENLALAARRgesrglsWGITRDERasyRERLAEL-DL-GLEERLTSKVG 147
Cdd:COG1135 77 lraaRR--KIGMIFQHFnllSSRTVA-----ENVALPLEI-------AGVPKAEI---RKRVAELlELvGLSDKADAYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 148 LLSGGQRQ------AL----TLLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMnDAIR-LG 216
Cdd:COG1135 140 QLSGGQKQrvgiarALannpKVLLC----------DEATSALDPETTRSILDLLKDINRELGLTIVLITHEM-DVVRrIC 208
|
250
....*....|..
gi 2506233547 217 NRLIMMHEGNVI 228
Cdd:COG1135 209 DRVAVLENGRIV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-246 |
2.06e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDV--SRLPEHRR 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV-----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 ATDLGRVFQD----PmrgtaaDMQIVENLALAARRgeSRGLSwgiTRDERASYRERLAELdlGLEERLTSKVGLLSGGQR 154
Cdd:PRK09493 76 RQEAGMVFQQfylfP------HLTALENVMFGPLR--VRGAS---KEEAEKQARELLAKV--GLAERAHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDD 234
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
250
....*....|....*...
gi 2506233547 235 E------KRRLRvhDLLQ 246
Cdd:PRK09493 222 VliknppSQRLQ--EFLQ 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
2.16e-31 |
|
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: 115.80 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatD 81
Cdd:cd03300 1 IELENVSKFYGGFV-----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQD----PmrgtaaDMQIVENLALAARRgesRGLSwgitrdeRASYRERLAE-LDL-GLEERLTSKVGLLSGGQRQ 155
Cdd:cd03300 74 VNTVFQNyalfP------HLTVFENIAFGLRL---KKLP-------KAEIKERVAEaLDLvQLEGYANRKPSQLSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-227 |
2.54e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 115.04 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatD 81
Cdd:cd03301 1 VELENVTKRFGN-----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR--D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQD----PmrgtaaDMQIVENLALAARrgeSRGLSwgitRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQAL 157
Cdd:cd03301 74 IAMVFQNyalyP------HMTVYDNIAFGLK---LRKVP----KDEIDERVREVAEL-LQIEHLLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
2.59e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH---- 76
Cdd:COG1121 6 AIELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 --RRATDLGrvFqdPMRgtaadmqiVENLALAARRGEsRGLSWGITRDERASYRERLAEldLGLEERLTSKVGLLSGGQR 154
Cdd:COG1121 81 pqRAEVDWD--F--PIT--------VRDVVLMGRYGR-RGLFRRPSRADREAVDEALER--VGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 Q------ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMH 223
Cdd:COG1121 146 QrvllarALAqdpdlLLL-----------DEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLN 213
|
250
....*....|.
gi 2506233547 224 EGNVIFDARDD 234
Cdd:COG1121 214 RGLVAHGPPEE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-225 |
1.34e-29 |
|
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: 108.87 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLG 83
Cdd:cd00267 2 IENLSFRYGG-----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQdpmrgtaadmqivenlalaarrgesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQALTLLMAI 163
Cdd:cd00267 77 YVPQ-------------------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 164 LKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-230 |
1.45e-29 |
|
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: 112.16 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-----RLPEHRR 78
Cdd:TIGR04521 3 LKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 atDLGRVFQDPmrgtaaDMQIVE------------NLalaarrgesrGLSwgitrDERAsyRERLAE-LDL-GLEERLTS 144
Cdd:TIGR04521 83 --KVGLVFQFP------EHQLFEetvykdiafgpkNL----------GLS-----EEEA--EERVKEaLELvGLDEEYLE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 145 KVGL-LSGGQ--RQAL---------TLLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDA 212
Cdd:TIGR04521 138 RSPFeLSGGQmrRVAIagvlamepeVLIL-----------DEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDV 206
|
250
....*....|....*...
gi 2506233547 213 IRLGNRLIMMHEGNVIFD 230
Cdd:TIGR04521 207 AEYADRVIVMHKGKIVLD 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-228 |
3.50e-29 |
|
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: 109.96 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFAL-----DGGQVILDGRDVSRLP----EHRRAtdLGRVFQ 87
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvdvlELRRR--VGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 88 DPmrgTAADMQIVENLALAARrgeSRGLSWGITRDERAsyRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKP 167
Cdd:cd03260 89 KP---NPFPGSIYDNVAYGLR---LHGIKLKEELDERV--EEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 168 KLLLLDEHTAALDPKTASKVlaltERLVGE--HGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKI----EELIAElkKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-227 |
1.84e-28 |
|
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: 106.33 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAtD 81
Cdd:cd03230 1 IEVRNLSKRYGK-----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPMrgTAADMQIVENLalaarrgesrglswgitrderasyrerlaeldlgleerltskvgLLSGGQRQALTLLM 161
Cdd:cd03230 75 IGYLPEEPS--LYENLTVRENL--------------------------------------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-228 |
2.08e-28 |
|
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: 108.20 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKStvnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatD 81
Cdd:cd03296 3 IEVRNVSKRFGDF-----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDpmRGTAADMQIVENLA--LAARRGESRGLSWGItrDERASYRERLAELDlGLEERLTSKvglLSGGQRQALTL 159
Cdd:cd03296 76 VGFVFQH--YALFRHMTVFDNVAfgLRVKPRSERPPEAEI--RAKVHELLKLVQLD-WLADRYPAQ---LSGGQRQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-230 |
2.71e-28 |
|
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: 107.28 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVtVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATd 81
Cdd:cd03264 1 LQLENLTKRYGK-----KRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrGTAADMQIVENLALAARRGesrglswGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:cd03264 74 IGYLPQEF--GVYPNFTVREFLDYIAWLK-------GIPSKEVKARVDEVLEL-VNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHglTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
4.42e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnkSTVnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PehRRA 79
Cdd:COG1129 4 LLEMRGISKSF--GGV---KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsP--RDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 TDLG--RVFQDPMrgTAADMQIVENLALAARRGESRGLSWgitRDERASYRERLAEldLGLEERLTSKVGLLSGGQRQ-- 155
Cdd:COG1129 77 QAAGiaIIHQELN--LVPNLSVAENIFLGREPRRGGLIDW---RAMRRRARELLAR--LGLDIDPDTPVGDLSVAQQQlv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ----ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGN 226
Cdd:COG1129 150 eiarALSrdarvLIL-----------DEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGR 217
|
..
gi 2506233547 227 VI 228
Cdd:COG1129 218 LV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-225 |
4.54e-28 |
|
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: 106.85 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS----RLPEHRRa 79
Cdd:cd03262 3 IKNLHKSFGDFHV-----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 tDLGRVFQD----PmrgtaaDMQIVENLALAARRgesrglSWGITRDE-RASYRERLAELdlGLEERLTSKVGLLSGGQR 154
Cdd:cd03262 77 -KVGMVFQQfnlfP------HLTVLENITLAPIK------VKGMSKAEaEERALELLEKV--GLADKADAYPAQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-235 |
1.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS----RLPEHRRa 79
Cdd:PRK13637 5 IENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 tDLGRVFQDPmrgtaaDMQIVE-----NLALAARRgesRGLSwgitrDERASYRERLAELDLGLE-ERLTSKVGL-LSGG 152
Cdd:PRK13637 84 -KVGLVFQYP------EYQLFEetiekDIAFGPIN---LGLS-----EEEIENRVKRAMNIVGLDyEDYKDKSPFeLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 153 QRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDAR 232
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
...
gi 2506233547 233 DDE 235
Cdd:PRK13637 229 PRE 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-235 |
1.07e-27 |
|
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: 111.46 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRAt 80
Cdd:COG2274 474 IELENVSFRYPG---DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdPASLRR- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDP--MRGTaadmqIVENLALAARrgesrglswGITRDE--RASyreRLAELD-------LGLEERLTSKVGLL 149
Cdd:COG2274 550 QIGVVLQDVflFSGT-----IRENITLGDP---------DATDEEiiEAA---RLAGLHdfiealpMGYDTVVGEGGSNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMnDAIRLGNRLIMMHEGNVIF 229
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRL-STIRLADRIIVLDKGRIVE 689
|
....*.
gi 2506233547 230 DARDDE 235
Cdd:COG2274 690 DGTHEE 695
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-228 |
1.50e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.31 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDV-SRLPEHRRAT 80
Cdd:COG1118 3 IEVRNISKRFGS-----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 dlGRVFQDP--MRgtaaDMQIVENLALAAR-RGESRglswgitRDERASYRERLAELDL-GLEERLTSKvglLSGGQRQ- 155
Cdd:COG1118 78 --GFVFQHYalFP----HMTVAENIAFGLRvRPPSK-------AEIRARVEELLELVQLeGLADRYPSQ---LSGGQRQr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 -----ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:COG1118 142 valarALAvepevLLL-----------DEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
...
gi 2506233547 226 NVI 228
Cdd:COG1118 211 RIE 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
1.89e-27 |
|
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: 105.28 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAtD 81
Cdd:cd03263 1 LQIRNLTKTYKKGT---KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQ-S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDpmRGTAADMQIVENLALAARrgeSRGLSWGITRDERASYRErlaelDLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:cd03263 77 LGYCPQF--DALFDELTVREHLRFYAR---LKGLPKSEIKEEVELLLR-----VLGLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-228 |
3.67e-27 |
|
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: 104.61 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDP--MRGTa 94
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTflFSGT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 admqIVENLALAARrgesrglswgITRDERASYRERLAELDL-------GLEERLTSKVGLLSGGQRQALTLLMAILKKP 167
Cdd:cd03254 93 ----IMENIRLGRP----------NATDEEVIEAAKEAGAHDfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKII 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-230 |
3.67e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.53 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQvILDGRdvSRLPEHRRATD 81
Cdd:PRK11247 13 LLLNAVSKRYGERTV-----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT--APLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LgrVFQD----PMRgtaadmQIVENLALaarrgesrglswGITRDERASYRERLAELdlGLEERLTSKVGLLSGGQRQAL 157
Cdd:PRK11247 85 L--MFQDarllPWK------KVIDNVGL------------GLKGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-235 |
4.29e-27 |
|
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: 109.46 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:COG4988 337 IELEDVSFSYP----GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDP--MRGTaadmqIVENLALAARrgesrglswGITRDE------RASYRERLAELDLGLEERLTSKVGLLSGGQ 153
Cdd:COG4988 413 IAWVPQNPylFAGT-----IRENLRLGRP---------DASDEEleaaleAAGLDEFVAALPDGLDTPLGEGGRGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMnDAIRLGNRLIMMHEGNVIFDARD 233
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTH 555
|
..
gi 2506233547 234 DE 235
Cdd:COG4988 556 EE 557
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-228 |
5.34e-27 |
|
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: 104.69 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKStvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:cd03295 1 IEFENVTKRYGGG----KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrGTAADMQIVENLALAARRgesrgLSWgitrdERASYRERLAEL--DLGLE-----ERLTSKvglLSGGQR 154
Cdd:cd03295 77 IGYVIQQI--GLFPHMTVEENIALVPKL-----LKW-----PKEKIRERADELlaLVGLDpaefaDRYPHE---LSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-222 |
6.25e-27 |
|
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: 103.77 E-value: 6.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR-------LPEHRratDLGRVFqdP 89
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkrigyVPQRR---SIDRDF--P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 90 MRgtaadmqiVENLALAARRGESRGLSWgITRDERASYRERLAEldLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKL 169
Cdd:cd03235 85 IS--------VRDVVLMGLYGHKGLFRR-LSKADKAKVDEALER--VGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 170 LLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMM 222
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-228 |
6.42e-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: 102.12 E-value: 6.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKStvnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRAT 80
Cdd:cd03216 1 LELRGITKRFGGV-----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQdpmrgtaadmqivenlalaarrgesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQALTLL 160
Cdd:cd03216 76 GIAMVYQ-------------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-224 |
2.56e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.17 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTktfnkSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG----VFALDGgQVILDGRDVSRLPEH 76
Cdd:COG4136 1 MLSLENLT-----ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlspAFSASG-EVLLNGRRLTALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRAtdLGRVFQDPMrgTAADMQIVENLALAARRGESRGLswgitRDERASyrERLAELDL-GLEERLtskVGLLSGGQRQ 155
Cdd:COG4136 75 QRR--IGILFQDDL--LFPHLSVGENLAFALPPTIGRAQ-----RRARVE--QALEEAGLaGFADRD---PATLSGGQRA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAiRLGNRLIMMHE 224
Cdd:COG4136 141 RVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDLGN 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-230 |
2.61e-26 |
|
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: 102.19 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 26 DLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLgrVFQDpmRGTAADMQIVENLAL 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSM--LFQE--NNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 106 aarrGESRGLSwgITRDERASYRERLAELdlGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTAS 185
Cdd:cd03298 94 ----GLSPGLK--LTAEDRQAIEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2506233547 186 KVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-235 |
8.04e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 26 DLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLgrVFQDpmRGTAADMQIVENLAL 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSM--LFQE--NNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 106 aarrgesrGLSWGITRDerASYRERLAEL--DLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKT 183
Cdd:PRK10771 95 --------GLNPGLKLN--AAQREKLHAIarQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 184 ASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-225 |
8.49e-26 |
|
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: 99.38 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:cd03228 1 IEFKNVSFSYPG---RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDP--MRGTaadmqIVENLalaarrgesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQALTL 159
Cdd:cd03228 78 IAYVPQDPflFSGT-----IRENI---------------------------------------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvgEHGLTTLMVTHNMNdAIRLGNRLIMMHEG 225
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVLDDG 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-228 |
1.33e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.25 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLP--EHRRAtdLGRVFQDPMR--G 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTleSLRRQ--IGVVPQDTFLfsG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TAAdmqivENLALAARrgesrglswGITRDE------RASYRERLAELDLGLEERLTSKVGLLSGGQRQALT-------- 158
Cdd:COG1132 429 TIR-----ENIRYGRP---------DATDEEveeaakAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAiarallkd 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 159 ---LLMailkkpkllllDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:COG1132 495 ppiLIL-----------DEATSALDTETEALIQEALERLM--KGRTTIVIAHRLS-TIRNADRILVLDDGRIV 553
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-225 |
2.17e-25 |
|
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: 100.23 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAtdlgrVFQD----PMrgtaadM 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNysllPW------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAARRgesrglswgITRDERASYRERLAE--LDL-GLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDE 174
Cdd:TIGR01184 70 TVRENIALAVDR---------VLPDLSKSERRAIVEehIALvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 175 HTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-235 |
2.55e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.54 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVV-----LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDP---MRGTaadmqiVENLALAARRGESRGlswGITRDERASYRERLAELDLG-LEER-LTSkvglLSGGQRQ 155
Cdd:COG4604 76 RLAILRQENhinSRLT------VRELVAFGRFPYSKG---RLTAEDREIIDEAIAYLDLEdLADRyLDE----LSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
3.19e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKStVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRlPEHRRAT 80
Cdd:COG4525 3 MLTVRHVSVRYPGG-GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 dlgrVFQD----PMRgtaadmQIVENLALAAR-RGESRglswgITRDERAsyRERLAELdlGLEERLTSKVGLLSGGQRQ 155
Cdd:COG4525 81 ----VFQKdallPWL------NVLDNVAFGLRlRGVPK-----AERRARA--EELLALV--GLADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 156 ------ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMM 222
Cdd:COG4525 142 rvgiarALAadprfLLM-----------DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-230 |
3.28e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 99.71 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRD-VSRLPEHRRatDL 82
Cdd:cd03267 19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLR--RI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQDpmRGTAA-DMQIVENLALAARrgesrglswgITRDERASYRERLAELD--LGLEERLTSKVGLLSGGQRQALTL 159
Cdd:cd03267 97 GVVFGQ--KTQLWwDLPVIDSFYLLAA----------IYDLPPARFKKRLDELSelLDLEELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-235 |
3.67e-25 |
|
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: 99.43 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG4181 8 IIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGR----VFQD-PMRGTaadMQIVENLALAArrgESRGlswgiTRDERASYRERLAEldLGLEERLTSKVGLLSGG--Q 153
Cdd:COG4181 87 LRARhvgfVFQSfQLLPT---LTALENVMLPL---ELAG-----RRDARARARALLER--VGLGHRLDHYPAQLSGGeqQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 154 RQAL--------TLLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGnRLIMMHEG 225
Cdd:COG4181 154 RVALarafatepAILFA----------DEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAG 222
|
250
....*....|
gi 2506233547 226 NVIFDARDDE 235
Cdd:COG4181 223 RLVEDTAATA 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-207 |
1.68e-24 |
|
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: 97.16 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAt 80
Cdd:COG4133 2 MLEAENLSCRRG-----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPmrGTAADMQIVENLALAARrgesrglSWGITRDeRASYRERLAEldLGLEERLTSKVGLLSGGQRQALTLL 160
Cdd:COG4133 76 RLAYLGHAD--GLKPELTVRENLRFWAA-------LYGLRAD-REAIDEALEA--VGLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTH 207
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHL-ARGGAVLLTTH 189
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
1.72e-24 |
|
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: 99.74 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTF--NKSTVnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV---FALDGGQVILDGRDVSRLPE 75
Cdd:COG0444 1 LLEVRNLKVYFptRRGVV---KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 76 HR----RATDLGRVFQDPM-----RGTAADmQIVEnlALAARRGESRglswgitrderASYRERLAELdlgLEerltsKV 146
Cdd:COG0444 78 KElrkiRGREIQMIFQDPMtslnpVMTVGD-QIAE--PLRIHGGLSK-----------AEARERAIEL---LE-----RV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 147 GL-------------LSGGQRQ------AL----TLLMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTL 203
Cdd:COG0444 136 GLpdperrldrypheLSGGMRQrvmiarALalepKLLIA----------DEPTTALDVTIQAQILNLLKDLQRELGLAIL 205
|
250 260
....*....|....*....|....*
gi 2506233547 204 MVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:COG0444 206 FITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-228 |
3.18e-24 |
|
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: 97.71 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHR----RATDLGRVFQDpmRGTAA 95
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKISMVFQS--FALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 DMQIVENLALaarrgesrGLS-WGITRDERasyRERLAE-LDL-GLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:cd03294 116 HRTVLENVAF--------GLEvQGVPRAER---EERAAEaLELvGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 173 DEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-228 |
4.62e-24 |
|
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: 96.28 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATd 81
Cdd:cd03265 1 IEVENLVKKYGDFE-----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrgtAADMQIV--ENLALAARrgesrglSWGITRDERasyRERLAEL--DLGLEERLTSKVGLLSGGQRQAL 157
Cdd:cd03265 75 IGIVFQDL----SVDDELTgwENLYIHAR-------LYGVPGAER---RERIDELldFVGLLEAADRLVKTYSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-208 |
5.02e-24 |
|
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: 100.51 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMrgtAADMQI 99
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAH---LFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLALAARRGESRGLSWGItrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAAL 179
Cdd:TIGR02868 426 RENLRLARPDATDEELWAAL---ERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*....
gi 2506233547 180 DPKTASKVLALTerLVGEHGLTTLMVTHN 208
Cdd:TIGR02868 503 DAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-230 |
5.25e-24 |
|
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: 96.06 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLpehrratDLG 83
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-------GLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQDPMRGtaadmqiVENLALaarrgesRGLSWGITRDERASYRERLAELDlGLEERLTSKVGLLSGGQRQALTLLMAI 163
Cdd:cd03220 93 GGFNPELTG-------RENIYL-------NGRLLGLSRKEIDEKIDEIIEFS-ELGDFIDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 164 LKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-231 |
7.41e-24 |
|
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: 95.44 E-value: 7.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 31 PGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR--DVSR----LPEHRRAtdLGRVFQDpmrgtAA---DMQIVE 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRkkinLPPQQRK--IGLVFQQ-----YAlfpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 NLALAARRGESRglswgitrDERASYRERLAELdlGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDP 181
Cdd:cd03297 95 NLAFGLKRKRNR--------EDRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2506233547 182 KTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDA 231
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-230 |
9.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS---RLPEHRRATdlGRVFQDPmrgt 93
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeeNLWDIRNKA--GMVFQNP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 aaDMQIV-----ENLALAARrgesrglSWGITRDErasYRERLAEL--DLGLEERLTSKVGLLSGGQRQALTLLMAILKK 166
Cdd:PRK13633 95 --DNQIVativeEDVAFGPE-------NLGIPPEE---IRERVDESlkKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 167 PKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRlGNRLIMMHEGNVIFD 230
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-235 |
2.28e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.71 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:COG1137 3 TLEAENLVKSYGKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 D-LGRVFQDP--MRGtaadMQIVENLALAArrgESRGLSwgitRDERasyRERLAEL--DLGLEERLTSKVGLLSGGQRQ 155
Cdd:COG1137 78 LgIGYLPQEAsiFRK----LTVEDNILAVL---ELRKLS----KKER---EERLEELleEFGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ------ALT------LLmailkkpkllllDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMH 223
Cdd:COG1137 144 rveiarALAtnpkfiLL------------DEPFAGVDPIAVADIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIIS 210
|
250
....*....|..
gi 2506233547 224 EGNVIFDARDDE 235
Cdd:COG1137 211 EGKVLAEGTPEE 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-230 |
2.93e-23 |
|
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: 93.97 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEKpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAt 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQ-AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDpmRGTAADMQIVENLALAARRgesrglsWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTLL 160
Cdd:cd03266 79 RLGFVSDS--TGLYDRLTARENLEYFAGL-------YGLKGDELTARLEELADR-LGMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 161 MAILKKPKLLLLDEHTAALDpKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-219 |
3.44e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.08 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT----DLGRVFQDPMrgTAADM 97
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFVFQSFM--LIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAAR-RGESrglswgiTRDERASYRERLAELdlGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHT 176
Cdd:PRK10584 104 NALENVELPALlRGES-------SRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2506233547 177 AALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRL 219
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-235 |
5.00e-23 |
|
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: 93.76 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:cd03218 1 LRAENLSKRYGKRKV-----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 -LGRVFQDP--MRgtaaDMQIVENLALAArrgESRGLSwgitRDERasyRERLAEL--DLGLEERLTSKVGLLSGGQRQA 156
Cdd:cd03218 76 gIGYLPQEAsiFR----KLTVEENILAVL---EIRGLS----KKER---EEKLEELleEFHITHLRKSKASSLSGGERRR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 157 LTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-228 |
5.39e-23 |
|
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: 95.94 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 25 VDLHLePGDFVTVI-GGNGAGKSTLLNSIAGVFALDGGQVILDGR---DVSR---LPEHRRAtdLGRVFQDPM------- 90
Cdd:COG4148 18 VDFTL-PGRGVTALfGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPHRRR--IGYVFQEARlfphlsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 91 RGtaadmqiveNLALAARRgesrglswgITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLL 170
Cdd:COG4148 95 RG---------NLLYGRKR---------APRAERRISFDEVVEL-LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 171 LLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-228 |
6.66e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.64 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH---- 76
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 -RRatDLGRVFQD---PMRGTAADmqiveNLALAARrgesrglswgITRDERASYRERLAEL-DL-GLEERLTSKVGLLS 150
Cdd:PRK11153 80 aRR--QIGMIFQHfnlLSSRTVFD-----NVALPLE----------LAGTPKAEIKARVTELlELvGLSDKADRYPAQLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 151 GGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-228 |
7.17e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR--LPEHRRatDLGRVFQDPmrgta 94
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRR--QVGMVFQNP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 aDMQIV-----ENLALAArrgESRGlswgITRDERAsyrERLAE-LDL-GLEERLTSKVGLLSGGQRQALTLLMAILKKP 167
Cdd:PRK13635 91 -DNQFVgatvqDDVAFGL---ENIG----VPREEMV---ERVDQaLRQvGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRlGNRLIMMHEGNVI 228
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-228 |
8.86e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.30 E-value: 8.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDG----RDVSRLPEHR 77
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 R-ATDLGRVFQDPmrgtaaDMQIVENLAlaarrgeSRGLSWG---ITRDERASYRERLAELDL-GLEERLTSKVGL-LSG 151
Cdd:PRK13645 87 RlRKEIGLVFQFP------EYQLFQETI-------EKDIAFGpvnLGENKQEAYKKVPELLKLvQLPEDYVKRSPFeLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 152 GQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
8.94e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.32 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSrlpEHRRATD 81
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT---AGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 L-------GRVFQDPmrgtaaDMQIVENLALaarRGESRG-LSWGITRDE-RASYRERLAELdlGLEERLTSKVGL-LSG 151
Cdd:PRK13634 80 LkplrkkvGIVFQFP------EHQLFEETVE---KDICFGpMNFGVSEEDaKQKAREMIELV--GLPEELLARSPFeLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 152 GQ--RQALTLLMAILKKPKLLllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13634 149 GQmrRVAIAGVLAMEPEVLVL--DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-228 |
1.47e-22 |
|
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: 91.96 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRratd 81
Cdd:cd03269 1 LEVENVTKRFG-----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDpmRGTAADMQIVENLA-LAARRGESRglswgitRDERASYRERLAEldLGLEERLTSKVGLLSGGQRQALTLL 160
Cdd:cd03269 72 IGYLPEE--RGLYPKMKVIDQLVyLAQLKGLKK-------EEARRRIDEWLER--LELSEYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-227 |
2.01e-22 |
|
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: 91.70 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTvnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLpeHRRAT- 80
Cdd:cd03292 1 IEFINVTKTYPNGT----AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL--RGRAIp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 ----DLGRVFQDPMrgTAADMQIVENLALAARrgesrglswgITRDERASYRERLAE-LDL-GLEERLTSKVGLLSGGQR 154
Cdd:cd03292 75 ylrrKIGVVFQDFR--LLPDRNVYENVAFALE----------VTGVPPREIRKRVPAaLELvGLSHKHRALPAELSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERlVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-230 |
4.38e-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: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKStvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLG 83
Cdd:cd03245 5 FRNVSFSYPNQ---EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQDPM--RGTaadmqIVENLALAARRGESRGLswgITRDERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:cd03245 82 YVPQDVTlfYGT-----LRDNITLGAPLADDERI---LRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGehGLTTLMVTHNMNdAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
4.41e-22 |
|
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: 94.83 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKStvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:COG4987 334 LELEDVSFRYPGA---GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDP--MRGTaadmqIVENLALAARrgesrglswGITRDE------RASYRERLAELDLGLEERLTSKVGLLSGGQ 153
Cdd:COG4987 411 IAVVPQRPhlFDTT-----LRENLRLARP---------DATDEElwaaleRVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHglTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLA-GLERMDRILVLEDGRIV 548
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-229 |
4.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.54 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 7 VTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVsrlpeHRRATD----- 81
Cdd:PRK13646 8 VSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-----THKTKDkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 ----LGRVFQDPmrgtaaDMQIVENLAlaARRGESRGLSWGITRDERASYRERLAeLDLGLEERLTSKVGL-LSGGQRQA 156
Cdd:PRK13646 83 vrkrIGMVFQFP------ESQLFEDTV--EREIIFGPKNFKMNLDEVKNYAHRLL-MDLGFSRDVMSQSPFqMSGGQMRK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 157 LTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIF 229
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-235 |
4.57e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.72 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 15 TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATdlgrvfqdpMRG-- 92
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR---------RRAvl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 ----------TAAdmQIVEnLALAARRGESRglswgitRDERASyRERLAELDL-GLEERLTSKvglLSGGQRQ------ 155
Cdd:COG4559 81 pqhsslafpfTVE--EVVA-LGRAPHGSSAA-------QDRQIV-REALALVGLaHLAGRSYQT---LSGGEQQrvqlar 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ALT------------LLMailkkpkllllDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMH 223
Cdd:COG4559 147 VLAqlwepvdggprwLFL-----------DEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLH 214
|
250
....*....|..
gi 2506233547 224 EGNVIFDARDDE 235
Cdd:COG4559 215 QGRLVAQGTPEE 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-227 |
5.04e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.47 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLP-EHRratDL 82
Cdd:PRK09452 17 LRGISKSFD-----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPaENR---HV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQD----PmrgtaaDMQIVENLALAARrgesrglswgITRDERASYRERLAE-LDL-GLEERLTSKVGLLSGGQRQA 156
Cdd:PRK09452 89 NTVFQSyalfP------HMTVFENVAFGLR----------MQKTPAAEITPRVMEaLRMvQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 157 LTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-228 |
5.59e-22 |
|
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: 94.78 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS--RLPEHRRATDLgrVFQDPMrgtAA 95
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQVAL--VSQDVV---LF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 DMQIVENLALAARRGESRGlswGITRDERASY-RERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDE 174
Cdd:TIGR02203 419 NDTIANNIAYGRTEQADRA---EIERALAAAYaQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 175 HTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLM--QGRTTLVIAHRLS-TIEKADRIVVMDDGRIV 546
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-208 |
6.24e-22 |
|
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: 89.79 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR--DVSR--LPEHRRAtdLGRVFQDPmrg 92
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRkgLLERRQR--VGLVFQDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 taaDMQIvenlaLAARRGESRG---LSWGITRDE-RASYRERLAELDL-GLEERLTSkvgLLSGGQRQALTLLMAILKKP 167
Cdd:TIGR01166 78 ---DDQL-----FAADVDQDVAfgpLNLGLSEAEvERRVREALTAVGAsGLRERPTH---CLSGGEKKRVAIAGAVAMRP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHN 208
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRLR-AEGMTVVISTHD 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-237 |
1.02e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.82 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRA-TDLGRVFQDpMRgTAADMQI 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArMGVVRTFQH-VR-LFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLALAARRGESRGLSWGI--TRDERASYRERLAE----LD-LGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:PRK11300 98 IENLLVAQHQQLKTGLFSGLlkTPAFRRAESEALDRaatwLErVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 173 DEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDEKR 237
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-228 |
1.12e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.60 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPmrGTAADMQ 98
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS--SLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 99 IVENLALaarrgesrGLS-WGITRDE-RASYRERLAELDL-GLEERLTSKvglLSGGQRQ------ALTLLMAILKKPKL 169
Cdd:PRK13548 93 VEEVVAM--------GRApHGLSRAEdDALVAAALAQVDLaHLAGRDYPQ---LSGGEQQrvqlarVLAQLWEPDGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 170 LLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-242 |
1.24e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR-------- 72
Cdd:COG4152 1 MLELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 73 LPEHrratdlgrvfqdpmRGTAADMQIVENLALAARRgesRGLSwgitrdeRASYRERLAEL--DLGLEERLTSKVGLLS 150
Cdd:COG4152 76 LPEE--------------RGLYPKMKVGEQLVYLARL---KGLS-------KAEAKRRADEWleRLGLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 151 GGQRQALTLLMAILKKPKLLLLDEHTAALDP------KTAskVLALTERlvgehGLTTLMVTHNMNDAIRLGNRLIMMHE 224
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPvnvellKDV--IRELAAK-----GTTVIFSSHQMELVEELCDRIVIINK 204
|
250 260
....*....|....*....|....
gi 2506233547 225 GNVIFDARDDE------KRRLRVH 242
Cdd:COG4152 205 GRKVLSGSVDEirrqfgRNTLRLE 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-228 |
1.47e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.09 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatD 81
Cdd:PRK11432 7 VVLKNITKRFGSNTV-----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR--D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQD----PmrgtaaDMQIVENLALaarrgesrGLSW-GITRDERAS-YRERLAELDL-GLEERLtskVGLLSGGQR 154
Cdd:PRK11432 80 ICMVFQSyalfP------HMSLGENVGY--------GLKMlGVPKEERKQrVKEALELVDLaGFEDRY---VDQISGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPK----TASKVLALTERLvgehGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANlrrsMREKIRELQQQF----NITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-218 |
2.11e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-RLPEHRRA 79
Cdd:COG3845 5 ALELRGITKRFGGVV-----ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 TDLGRVFQDPMrgTAADMQIVENLALAARRGESRGLSWgitrderASYRERLAEL--DLGLEERLTSKVGLLSGGQRQ-- 155
Cdd:COG3845 80 LGIGMVHQHFM--LVPNLTVAENIVLGLEPTKGGRLDR-------KAARARIRELseRYGLDVDPDAKVEDLSVGEQQrv 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 156 ----AL-----TLLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNR 218
Cdd:COG3845 151 eilkALyrgarILIL-----------DEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADR 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-214 |
2.24e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQV-ILDGRDVSRLPEHrraTDLGRVFQDPMRGTAAdmq 98
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAYVPQR---SEVPDSLPLTVRDLVA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 99 ivenLALAARRGESRGLswgiTRDERASYRERLAELDL-GLEERltsKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTA 177
Cdd:NF040873 80 ----MGRWARRGLWRRL----TRDDRAAVDDALERVGLaDLAGR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 2506233547 178 ALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIR 214
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-163 |
2.26e-21 |
|
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: 87.32 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPmrGTAADMQIVE 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 102 NLALAARrgeSRGLSWGITRDERASYRERLAELDLgLEERLTSKVGLLSGGQRQALTLLMAI 163
Cdd:pfam00005 79 NLRLGLL---LKGLSKREKDARAEEALEKLGLGDL-ADRPVGERPGTLSGGQRQRVAIARAL 136
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKStvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR--LPEHRr 78
Cdd:PRK13632 7 MIKVENVSFSYPNS---ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 aTDLGRVFQDPmrgtaaDMQIV-----ENLA--LAARRgesrglswgITRDERASYRERLAElDLGLEERLTSKVGLLSG 151
Cdd:PRK13632 83 -KKIGIIFQNP------DNQFIgatveDDIAfgLENKK---------VPPKKMKDIIDDLAK-KVGMEDYLDKEPQNLSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 152 GQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIrLGNRLIMMHEGNVI 228
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-222 |
5.36e-21 |
|
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: 91.58 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:TIGR02857 322 LEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDP--MRGTaadmqIVENLALaARRGESRGLSwgitrdERASYRERLAELDLGLEERLTSKVG----LLSGGQRQ 155
Cdd:TIGR02857 398 IAWVPQHPflFAGT-----IAENIRL-ARPDASDAEI------REALERAGLDEFVAALPQGLDTPIGeggaGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGehGLTTLMVTHNMNDAIRLgNRLIMM 222
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-245 |
6.39e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 87.97 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRA-TDLGRVFQDpmRGTAADMQI 99
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERArAGIAYVPQG--REIFPRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENL--ALAARRGESRGLSwgitrderasyrERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTA 177
Cdd:TIGR03410 93 EENLltGLAALPRRSRKIP------------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 178 ALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDEKRRLRVHDLL 245
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-228 |
6.78e-21 |
|
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: 88.71 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEK----PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PE 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAkqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 76 HRRA--TDLGRVFQDPMRGTAADMQIVENLALAARRGESRGLSwgiTRDERASYRERLAELDLGLEERLTSKvglLSGGQ 153
Cdd:TIGR02769 82 QRRAfrRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDES---EQKARIAELLDMVGLRSEDADKLPRQ---LSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-230 |
6.87e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.40 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ-----ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPMRgTAADMQIVENLALaarrgesrglswGITRDERASYRERLA---ELDLGLEERLTSKVGLLSGGQRQAL 157
Cdd:PRK11614 80 EAVAIVPEGRR-VFSRMTVEENLAM------------GGFFAERDQFQERIKwvyELFPRLHERRIQRAGTMSGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-228 |
9.34e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.44 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR-----DVSRLPE 75
Cdd:PRK11701 6 LLSVRGLTKLYG-----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 76 HRRA----TDLGRVFQDPMRG----TAADMQIVENL-ALAARRgesrglsWGITRDERASYRERLaELDLgleERLTSKV 146
Cdd:PRK11701 81 AERRrllrTEWGFVHQHPRDGlrmqVSAGGNIGERLmAVGARH-------YGDIRATAGDWLERV-EIDA---ARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 147 GLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGN 226
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
..
gi 2506233547 227 VI 228
Cdd:PRK11701 230 VV 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-230 |
1.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDV---SRLPEHR 77
Cdd:PRK13644 1 MIRLENVSYSYPDGT----PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 RAtdLGRVFQDPM-----RGTAADMQI-VENLALAARrgESRglswgiTRDERAsyrerLAELDLGLEERLTSKVglLSG 151
Cdd:PRK13644 77 KL--VGIVFQNPEtqfvgRTVEEDLAFgPENLCLPPI--EIR------KRVDRA-----LAEIGLEKYRHRSPKT--LSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 152 GQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDaIRLGNRLIMMHEGNVIFD 230
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-225 |
2.77e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRratdlGRVFQD----PMRgta 94
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNegllPWR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 admQIVENLALAARRGesrglswGITRDER-ASYRERLAELDL-GLEERltsKVGLLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:PRK11248 86 ---NVQDNVAFGLQLA-------GVEKMQRlEIAHQMLKKVGLeGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 173 DEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-228 |
3.17e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:PRK11607 19 LLEIRNLTKSFDG-----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLgrVFQDpmRGTAADMQIVENLAlaarrgesrglsWGITRDE--RASYRERLAELdLGL---EERLTSKVGLLSGGQRQ 155
Cdd:PRK11607 94 NM--MFQS--YALFPHMTVEQNIA------------FGLKQDKlpKAEIASRVNEM-LGLvhmQEFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASK----VLALTERLvgehGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
3.20e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQV------ILDGRDVSRLP 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV-----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 75 EHRRA--TDLGRVFQD----PMRgTAADmQIVENLALAarRGESRGlswgitrDERASYRERLAELdlGLEERLTSKVGL 148
Cdd:PRK11264 78 GLIRQlrQHVGFVFQNfnlfPHR-TVLE-NIIEGPVIV--KGEPKE-------EATARARELLAKV--GLAGKETSYPRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 149 LSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLAlTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN-TIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-230 |
4.26e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTF-----------------NKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQV 63
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 64 ILDGRDVSRLpehrratDLGRVFQDPMRGtaadmqiVENLALaarrgesRGLSWGITRDErasYRERLAE-LDL-GLEER 141
Cdd:COG1134 84 EVNGRVSALL-------ELGAGFHPELTG-------RENIYL-------NGRLLGLSRKE---IDEKFDEiVEFaELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 142 LTSKVGLLSGGQRQAL-----------TLLMailkkpkllllDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMN 210
Cdd:COG1134 140 IDQPVKTYSSGMRARLafavatavdpdILLV-----------DEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMG 207
|
250 260
....*....|....*....|
gi 2506233547 211 DAIRLGNRLIMMHEGNVIFD 230
Cdd:COG1134 208 AVRRLCDRAIWLEKGRLVMD 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-227 |
8.15e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVsrlpEHRRAT 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTV-----LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV----EALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPMRGTAADM-----QIVEnlalaARRGESRGLSWGITRDERASYRERLAELDLG--LEERLTSkvglLSGGQ 153
Cdd:PRK09536 74 AASRRVASVPQDTSLSFefdvrQVVE-----MGRTPHRSRFDTWTETDRAAVERAMERTGVAqfADRPVTS----LSGGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-248 |
1.53e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.96 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLL---NSIAGVF--ALDGGQVILDGRDVSRLP-- 74
Cdd:PRK14247 4 IEIRDLKVSFGQVEV-----LDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYpeARVSGEVYLDGQDIFKMDvi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 75 EHRRATDLgrVFQDPmrGTAADMQIVENLALaarrgesrGLSWGITRDERASYRERL------AELDLGLEERLTSKVGL 148
Cdd:PRK14247 79 ELRRRVQM--VFQIP--NPIPNLSIFENVAL--------GLKLNRLVKSKKELQERVrwalekAQLWDEVKDRLDAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 149 LSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhgLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
250 260
....*....|....*....|
gi 2506233547 229 FDARDDEKRRLRVHDLLQKF 248
Cdd:PRK14247 225 EWGPTREVFTNPRHELTEKY 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-230 |
2.31e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 15 TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALD---GGQVILDGRDVSRlpEHRRATDL-------GR 84
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQR--EGRLARDIrksrantGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 85 VFQDpmRGTAADMQIVENL---ALAARRGESRGLSWGITRDERASYRerlAELDLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:PRK09984 91 IFQQ--FNLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQ---ALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-228 |
2.35e-19 |
|
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: 83.70 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDP--MRGTa 94
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPvlFSGT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 admqIVENLALAARRGESRglSWGITrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDE 174
Cdd:cd03244 94 ----IRSNLDPFGEYSDEE--LWQAL--ERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 175 HTAALDPKTASKVlaltERLVGEH--GLTTLMVTHNMnDAIRLGNRLIMMHEGNVI 228
Cdd:cd03244 166 ATASVDPETDALI----QKTIREAfkDCTVLTIAHRL-DTIIDSDRILVLDKGRVV 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-227 |
2.76e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.91 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 6 GVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLpeHRRATDLGRV 85
Cdd:PRK10851 7 NIKKSFGRTQV-----LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 FQDpmRGTAADMQIVENLALaarrgesrGLSWgITRDER---ASYRERLAEL----DLG-LEERLTSKvglLSGGQRQAL 157
Cdd:PRK10851 80 FQH--YALFRHMTVFDNIAF--------GLTV-LPRRERpnaAAIKAKVTQLlemvQLAhLADRYPAQ---LSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-228 |
3.10e-19 |
|
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: 86.66 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKS----TLLNSIAGVFALDGGQVILDGRDVSRLPEHR----RATDLGRVFQD 88
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 89 PMrgTAAD------MQIVENLALaarrgeSRGLSwgitrdeRASYRERLAEL--DLGL---EERLTSKVGLLSGGQRQAL 157
Cdd:COG4172 101 PM--TSLNplhtigKQIAEVLRL------HRGLS-------GAAARARALELleRVGIpdpERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
4.50e-19 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 83.43 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS--RLPEHRRa 79
Cdd:cd03251 1 VEFKNVTFRYPG---DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 tDLGRVFQDPM--RGTaadmqIVENLALAARrgesrglswGITRDE-----RASY-RERLAELDLGLEERLTSKVGLLSG 151
Cdd:cd03251 77 -QIGLVSQDVFlfNDT-----VAENIAYGRP---------GATREEveeaaRAANaHEFIMELPEGYDTVIGERGVKLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 152 GQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLS-TIENADRIVVLEDGKIV 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-230 |
6.08e-19 |
|
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: 83.21 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG-VFALDGGQVILDGRDVSR--LPEHRR-----ATDLGRVFQD 88
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGedVWELRKriglvSPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 89 PMRgtaadmqiVENLALAARRGeSRGLSWGITRDERASYRERLAELdlGLEERLTSKVGLLSGGQRQaLTLLM-AILKKP 167
Cdd:COG1119 94 DET--------VLDVVLSGFFD-SIGLYREPTDEQRERARELLELL--GLAHLADRPFGTLSQGEQR-RVLIArALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-227 |
7.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 10 TFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS--RLPEHRRatDLGRVFQ 87
Cdd:PRK13650 11 TFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRH--KIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 88 DPmrgtaaDMQIV-----ENLALAArrgESRGLSwgitrdeRASYRERLAE-LDL-GLEERLTSKVGLLSGGQRQALTLL 160
Cdd:PRK13650 89 NP------DNQFVgatveDDVAFGL---ENKGIP-------HEEMKERVNEaLELvGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMnDAIRLGNRLIMMHEGNV 227
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL-DEVALSDRVLVMKNGQV 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-227 |
1.51e-18 |
|
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: 80.34 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRATdLGRVFQDPM--RGT 93
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDH-VGYLPQDDElfSGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 aadmqIVENLalaarrgesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQALTLLMAILKKPKLLLLD 173
Cdd:cd03246 92 -----IAENI---------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 174 EHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNdAIRLGNRLIMMHEGNV 227
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-231 |
1.60e-18 |
|
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: 81.11 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRatD 81
Cdd:cd03268 1 LKTNDLTKTYGK-----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrGTAADMQIVENLALAARrgesrglswgITRDERASYRERLAEldLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:cd03268 74 IGALIEAP--GFYPNLTARENLRLLAR----------LLGIRKKRIDEVLDV--VGLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDA 231
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-226 |
2.11e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 16 VNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMR--GT 93
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLfgDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 AADmqiveNLALAarrgesrglsWGITRD--ERASYRERLAELDLGlEERLTSKVGLLSGGQRQALTLLMAILKKPKLLL 171
Cdd:PRK10247 97 VYD-----NLIFP----------WQIRNQqpDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 172 LDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMN------DAIRLGNRLIMMHEGN 226
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDeinhadKVITLQPHAGEMQEAR 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-228 |
4.58e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 4.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNS-------IAGVFAldGGQVILDGRDVSR----LPEHRRatDLGRV 85
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EGEILLDGEDIYDpdvdVVELRR--RVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 FQDPmrgTAADMQIVENLALAARRGesrglswGITRderasyRERLAEL------DLGL-EE---RLTSKVGLLSGGQRQ 155
Cdd:COG1117 98 FQKP---NPFPKSIYDNVAYGLRLH-------GIKS------KSELDEIveeslrKAALwDEvkdRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ALT-----------LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHglTTLMVTHNMNDAIRLGNRLIMMHE 224
Cdd:COG1117 162 RLCiaralavepevLLM-----------DEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYL 228
|
....
gi 2506233547 225 GNVI 228
Cdd:COG1117 229 GELV 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-235 |
4.79e-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: 80.61 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRAtDLGRVFQDpmrGTAADMQI 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRR-QVGVVLQE---NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLALaARRGESRglswgitrdERASYRERLA-------ELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:cd03252 93 RDNIAL-ADPGMSM---------ERVIEAAKLAgahdfisELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 173 DEHTAALDPKTASKVLALTERLVGehGLTTLMVTHNMNdAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDE 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-228 |
9.90e-18 |
|
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: 82.04 E-value: 9.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 13 KSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTL----LNSIAGvfaldGGQVILDGRDVSRLPEH-----RRatDLG 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRalrplRR--RMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQDPM-----RGTAAdmQIV-ENLALAARrgesrglswGITRDERasyRERLAELdlgLEErltskVGL--------- 148
Cdd:COG4172 366 VVFQDPFgslspRMTVG--QIIaEGLRVHGP---------GLSAAER---RARVAEA---LEE-----VGLdpaarhryp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 149 --LSGGQRQ------ALTL----LMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMnDAIR-L 215
Cdd:COG4172 424 heFSGGQRQriaiarALILepklLVL----------DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL-AVVRaL 492
|
250
....*....|...
gi 2506233547 216 GNRLIMMHEGNVI 228
Cdd:COG4172 493 AHRVMVMKDGKVV 505
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-210 |
1.23e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.93 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTF---------NKSTVNekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVK---AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 73 LPEHRRAtDLGR----VFQDPM-----RGTAADMqIVENLALAarrgesrglswGI-TRDERasyRERLAELdlgLEerl 142
Cdd:COG4608 85 LSGRELR-PLRRrmqmVFQDPYaslnpRMTVGDI-IAEPLRIH-----------GLaSKAER---RERVAEL---LE--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 143 tsKVGL-----------LSGGQRQ------ALTL----LMAilkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLT 201
Cdd:COG4608 143 --LVGLrpehadrypheFSGGQRQrigiarALALnpklIVC----------DEPVSALDVSIQAQVLNLLEDLQDELGLT 210
|
....*....
gi 2506233547 202 TLMVTHNMN 210
Cdd:COG4608 211 YLFISHDLS 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-222 |
2.06e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 78.63 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEK--PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR----DVSRLP 74
Cdd:COG4778 4 LLEVENLSKTFTLHLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 75 EHR----RATDLGRVFQ----DPmRGTAADmqIVENLALAarRGESRglswgitrdERAsyRERLAEL--DLGLEERL-- 142
Cdd:COG4778 84 PREilalRRRTIGYVSQflrvIP-RVSALD--VVAEPLLE--RGVDR---------EEA--RARARELlaRLNLPERLwd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 143 ----TskvglLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNR 218
Cdd:COG4778 148 lppaT-----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADR 221
|
....
gi 2506233547 219 LIMM 222
Cdd:COG4778 222 VVDV 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-230 |
2.48e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR--DVSR--LPEHRRAtdLGRVFQDPmrgtaaD 96
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRkgLMKLRES--VGMVFQDP------D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 MQIvenLALAARRGESRG-LSWGITRDErASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK13636 93 NQL---FSASVYQDVSFGaVNLKLPEDE-VRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 176 TAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-228 |
3.61e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.87 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 7 VTKTFNKSTVNEKpaltgVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVF 86
Cdd:PRK10253 13 LTLGYGKYTVAEN-----LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 87 QDPMrgTAADMQIVENLALAARRGESRGLSWGiTRDERASYRERLAEldlGLEERLTSKVGLLSGGQRQALTLLMAILKK 166
Cdd:PRK10253 88 QNAT--TPGDITVQELVARGRYPHQPLFTRWR-KEDEEAVTKAMQAT---GITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 167 PKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-227 |
4.18e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.47 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSI-------AGVFALDGGQVIL----DGR----DVSRLPEHRraTDL 82
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLvrdkDGQlkvaDKNQLRLLR--TRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQDpmRGTAADMQIVENLALAARrgESRGLSWGITRDERASYRERLaeldlGLEERLTSKVGL-LSGGQRQALTLLM 161
Cdd:PRK10619 95 TMVFQH--FNLWSHMTVLENVMEAPI--QVLGLSKQEARERAVKYLAKV-----GIDERAQGKYPVhLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-230 |
6.04e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.98 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRD-VSRLPEHRRatDL 82
Cdd:COG4586 20 LKGALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFAR--RI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVF-QdpmRGT-AADMQIVENLALAARrgesrglswgITRDERASYRERLAELD--LGLEERLTSKVGLLSGGQRQALT 158
Cdd:COG4586 98 GVVFgQ---RSQlWWDLPAIDSFRLLKA----------IYRIPDAEYKKRLDELVelLDLGELLDTPVRQLSLGQRMRCE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-240 |
6.10e-17 |
|
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: 79.79 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEhrraTDLGRVF----QDP--MR 91
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR----EELGRHIgylpQDVelFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 92 GTaadmqIVENLA-----------LAARrgesrglswgitrdeRASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLL 160
Cdd:COG4618 420 GT-----IAENIArfgdadpekvvAAAK---------------LAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 161 MAILKKPKLLLLDEHTAALDPkTASKVLALTERLVGEHGLTTLMVTHNMNdAIRLGNRLIMMHEGNVI-FDARDDEKRRL 239
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDD-EGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQaFGPRDEVLARL 557
|
.
gi 2506233547 240 R 240
Cdd:COG4618 558 A 558
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-227 |
7.00e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 12 NKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-----PEHRRatDLGRVF 86
Cdd:PRK10908 8 SKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRR--QIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 87 QDpmRGTAADMQIVENLAL----AARRGEsrglswgitrDERasyRERLAELD-LGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:PRK10908 86 QD--HHLLMDRTVYDNVAIpliiAGASGD----------DIR---RRVSAALDkVGLLDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-248 |
7.12e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLpEHRRATDLG 83
Cdd:PRK09700 8 MAGIGKSFGPVH-----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 --RVFQDpmRGTAADMQIVENLALAarRGESRGLsWGITRDERASYRERLAE--LDLGLEERLTSKVGLLSGGQRQALTL 159
Cdd:PRK09700 82 igIIYQE--LSVIDELTVLENLYIG--RHLTKKV-CGVNIIDWREMRVRAAMmlLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGN-----VIFDARDD 234
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSND 235
|
250
....*....|....*
gi 2506233547 235 EKRRLRV-HDLLQKF 248
Cdd:PRK09700 236 DIVRLMVgRELQNRF 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
8.60e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR----DVSRLPEH 76
Cdd:PRK13639 1 ILETRDLKYSYPDGTE----ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRAtdLGRVFQDPmrgtaaDMQIV-----ENLALAArrgesrgLSWGITRDE-RASYRERLAELDL-GLEERLTSKvglL 149
Cdd:PRK13639 77 RKT--VGIVFQNP------DDQLFaptveEDVAFGP-------LNLGLSKEEvEKRVKEALKAVGMeGFENKPPHH---L 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13639 139 SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-228 |
1.41e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALD-----GGQVILDGRDVsrlpeHRRATD-------LGR 84
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI-----YSPRTDtvdlrkeIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 85 VFQDPmrgTAADMQIVENLALAARrgeSRGLSWGITRDERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAIL 164
Cdd:PRK14239 91 VFQQP---NPFPMSIYENVVYGLR---LKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 165 KKPKLLLLDEHTAALDPKTASKVlalTERLVG-EHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKI---EETLLGlKDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-235 |
1.47e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 79.01 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTAAdmqI 99
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGS---I 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLALAARRGESRGLSWGITrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAAL 179
Cdd:TIGR01193 565 LENLLLGAKENVSQDEIWAAC--EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 180 DPKTASKVLaltERLVGEHGLTTLMVTHNMNDAIRLgNRLIMMHEGNVIFDARDDE 235
Cdd:TIGR01193 643 DTITEKKIV---NNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDE 694
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-227 |
1.78e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 76.76 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSI-------AGVFALDGGQVIL-DGRDVSR 72
Cdd:COG4598 8 ALEVRDLHKSFGDLEV-----LKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRVGGEEIRLkPDRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 73 LPEHRRA-----TDLGRVFQDpmRGTAADMQIVENLALAARRgesrglSWGITRDERASYRERLAElDLGLEERLTSKVG 147
Cdd:COG4598 83 VPADRRQlqrirTRLGMVFQS--FNLWSHMTVLENVIEAPVH------VLGRPKAEAIERAEALLA-KVGLADKRDAYPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 148 LLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-235 |
1.91e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.46 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH--RRAtdLGRVFQDPMrgtA 94
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRN--IAVVFQDAG---L 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 ADMQIVENLALA---ARRGESRGLSwgitrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLL 171
Cdd:PRK13657 421 FNRSIEDNIRVGrpdATDEEMRAAA------ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 172 LDEHTAALDPKTASKVLALTERLVgeHGLTTLMVTHNMNdAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDE 555
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
2.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRD-------------- 69
Cdd:PRK13651 5 VKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 70 ---VSRLPEHRR---ATDL----GRVFQdpmrgtAADMQIVE-----NLALAARrgesrglSWGITRDE---RASYRERL 131
Cdd:PRK13651 85 eklVIQKTRFKKikkIKEIrrrvGVVFQ------FAEYQLFEqtiekDIIFGPV-------SMGVSKEEakkRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 132 AELDlglEERLTSKVGLLSGGQ--RQALTLLMAILKKPKLLllDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNM 209
Cdd:PRK13651 152 VGLD---ESYLQRSPFELSGGQkrRVALAGILAMEPDFLVF--DEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDL 225
|
250 260
....*....|....*....|..
gi 2506233547 210 NDAIRLGNRLIMMHEGNVIFDA 231
Cdd:PRK13651 226 DNVLEWTKRTIFFKDGKIIKDG 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-239 |
2.90e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSI-------AGVFALDGGQVI-LDGRDVSR 72
Cdd:PRK10535 4 LLELKDIRRSY-PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVAtLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 73 LpehrRATDLGRVFQdpmRG------TAAdmQIVENLALAArrgesrglswGITRDERasyRERLAEL--DLGLEERLTS 144
Cdd:PRK10535 83 L----RREHFGFIFQ---RYhllshlTAA--QNVEVPAVYA----------GLERKQR---LLRAQELlqRLGLEDRVEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 145 KVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRlGNRLIMMHE 224
Cdd:PRK10535 141 QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRD 218
|
250
....*....|....*
gi 2506233547 225 GNVIFDARDDEKRRL 239
Cdd:PRK10535 219 GEIVRNPPAQEKVNV 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-221 |
3.72e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT----DLGRVFQdpMRGTAADM 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQ--FHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAARRGESRglswgitrdeRASYRERLAEL--DLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK11629 103 TALENVAMPLLIGKKK----------PAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2506233547 176 TAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIM 221
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
4.49e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATd 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLV-----VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQ----DPmrgtaaDMQIVENLALAARRgesRGLSwgitrdeRASYRERLAEL--DLGLEERLTSKVGLLSGGQRQ 155
Cdd:PRK13537 82 VGVVPQfdnlDP------DFTVRENLLVFGRY---FGLS-------AAAARALVPPLleFAKLENKADAKVGELSGGMKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKtASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-228 |
6.04e-16 |
|
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: 74.22 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRlpeHRRATDLGRVFQDPmrgtaaDMQIVE 101
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDV------DYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 NLAlaarrGESRGLSWGITRDERASYRERLAELDL-GLEERLTSKvglLSGGQRQALTLLMAILKKPKLLLLDEHTAALD 180
Cdd:cd03226 87 DSV-----REELLLGLKELDAGNEQAETVLKDLDLyALKERHPLS---LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2506233547 181 PKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:cd03226 159 YKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
8.80e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRra 79
Cdd:PRK11650 3 GLKLQAVRKSYD----GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePADR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 tDLGRVFQD----PmrgtaaDMQIVENLALAARrgeSRGLSwgitRDERasyRERLAELD--LGLEERLTSKVGLLSGGQ 153
Cdd:PRK11650 77 -DIAMVFQNyalyP------HMSVRENMAYGLK---IRGMP----KAEI---EERVAEAAriLELEPLLDRKPRELSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-228 |
1.06e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 27 LHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVfqdPMRGTAADMQIVENLaLA 106
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL---PQQLPAAEGMTVREL-VA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 107 ARRGESRGLSWGITRDERASYRERLAELDLG-LEERLtskVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTAS 185
Cdd:PRK10575 108 IGRYPWHGALGRFGAADREKVEEAISLVGLKpLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2506233547 186 KVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-235 |
1.08e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMrgTAADM 97
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHL--TPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALaarrGESRGLS-WG-ITRDERASYRERLAelDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK11231 92 TVRELVAY----GRSPWLSlWGrLSAEDNARVNQAME--QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 176 TAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-235 |
1.12e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 7 VTKTFNKSTVNEkpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVF 86
Cdd:PRK13642 11 VFKYEKESDVNQ---LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 87 QDPmrgtaaDMQIV-----ENLALAARrgesrglSWGITRDERASyRERLAELDLGLEERLTSKVGLLSGGQRQALTLLM 161
Cdd:PRK13642 88 QNP------DNQFVgatveDDVAFGME-------NQGIPREEMIK-RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRlGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-229 |
1.75e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.72 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVfaLDG-GQVILDGRDVSRLPehrrATDLGRvfqdpMRG-------T 93
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL--LPGqGEILLNGRPLSDWS----AAELAR-----HRAylsqqqsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 AADMQIVENLALAARRGESrglswgitrdeRASYRERLAEL--DLGLEERLTSKVGLLSGGQRQ----ALTLLM---AIL 164
Cdd:COG4138 81 PFAMPVFQYLALHQPAGAS-----------SEAVEQLLAQLaeALGLEDKLSRPLTQLSGGEWQrvrlAAVLLQvwpTIN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 165 KKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIF 229
Cdd:COG4138 150 PEGQLLLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-228 |
2.16e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDL- 82
Cdd:PRK13649 5 LQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 ---GRVFQDPmRGTAADMQIVENLALAARrgesrglSWGITRDE-RASYRERLAEldLGLEERLTSKVGL-LSGGQRQAL 157
Cdd:PRK13649 85 kkvGLVFQFP-ESQLFEETVLKDVAFGPQ-------NFGVSQEEaEALAREKLAL--VGISESLFEKNPFeLSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-228 |
4.19e-15 |
|
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: 72.57 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 3 VLKGVTktFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDL 82
Cdd:cd03249 2 EFKNVS--FRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQDPmrgTAADMQIVENLALAARRGESrglswgiTRDERASyreRLAELD---LGLEERLTSKVG----LLSGGQRQ 155
Cdd:cd03249 80 GLVSQEP---VLFDGTIAENIRYGKPDATD-------EEVEEAA---KKANIHdfiMSLPDGYDTLVGergsQLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGehGLTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-228 |
5.98e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.91 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 5 KGVTKTFNKStvnEKPALTGVDLHLEPGDFVTVIGGNGAGKST---LLNSIAGVFALDGGQVILDGRDVSRLPEHRRATD 81
Cdd:PRK13640 9 KHVSFTYPDS---KKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmrgtaaDMQIV-----ENLALAArrgESRGLSwgitRDERASYRERLAElDLGLEERLTSKVGLLSGGQRQA 156
Cdd:PRK13640 86 VGIVFQNP------DNQFVgatvgDDVAFGL---ENRAVP----RPEMIKIVRDVLA-DVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 157 LTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIrLGNRLIMMHEGNVI 228
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-228 |
9.34e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 25 VDLHLePGDFVTVI-GGNGAGKSTLLNSIAGVFALDGGQVILDGR---DVSR---LPEHRRatDLGRVFQDpmrgtaadm 97
Cdd:PRK11144 17 VNLTL-PAQGITAIfGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKR--RIGYVFQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 qivenlalaAR-------RGEsrgLSWGITRDERASYrERLAELdLGLEERLTSKVGLLSGG--QRQA-----LT----L 159
Cdd:PRK11144 85 ---------ARlfphykvRGN---LRYGMAKSMVAQF-DKIVAL-LGIEPLLDRYPGSLSGGekQRVAigralLTapelL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 160 LMailkkpkllllDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11144 151 LM-----------DEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-248 |
1.06e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALT-GV---DLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHR-- 77
Cdd:PRK10070 22 FKYIEQGLSKEQILEKTGLSlGVkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 --RATDLGRVFQDpmRGTAADMQIVENLALAARRGesrglswGITRDERasyRERL--AELDLGLEERLTSKVGLLSGGQ 153
Cdd:PRK10070 102 evRRKKIAMVFQS--FALMPHMTVLDNTAFGMELA-------GINAEER---REKAldALRQVGLENYAHSYPDELSGGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARD 233
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
250
....*....|....*
gi 2506233547 234 DEKRRLRVHDLLQKF 248
Cdd:PRK10070 250 DEILNNPANDYVRTF 264
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-228 |
1.54e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT---DLGRVFQDPMRGTAADMQ 98
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 99 IVENLALAARRgesrglswgITRDERASYRERLAEL--DLGLEERLTSKV-GLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK10419 108 VREIIREPLRH---------LLSLDKAERLARASEMlrAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 176 TAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-228 |
1.72e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.69 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAT 80
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 ----DLGRVFQDPmRGTAADMQIVENLALAARrgesrglSWGITRDERASYRERLAELdLGLEERLTSKVGL-LSGGQRQ 155
Cdd:PRK13643 81 pvrkKVGVVFQFP-ESQLFEETVLKDVAFGPQ-------NFGIPKEKAEKIAAEKLEM-VGLADEFWEKSPFeLSGGQMR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERlVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-228 |
3.77e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.51 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVF-----------ALDGGQVILDGRDVSrlpEHRRAtdLGRVFQ 87
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyrysgdVLLGGRSIFNYRDVL---EFRRR--VGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 88 DPmrgTAADMQIVENLALAAR------RGESRGLSwgitrderasyRERLAELDL--GLEERLTSKVGLLSGGQRQALTL 159
Cdd:PRK14271 109 RP---NPFPMSIMDNVLAGVRahklvpRKEFRGVA-----------QARLTEVGLwdAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhgLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-228 |
4.23e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKStvnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNsiagVFAL----DGGQVILDGR--DVSRLPEHR 77
Cdd:COG4161 5 LKNINCFYGSH-----QALFDINLECPSGETLVLLGPSGAGKSSLLR----VLNLletpDSGQLNIAGHqfDFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 RATDL----GRVFQD----PmrgtaaDMQIVENLALAARRgeSRGLSWGITRDERASYRERLaeldlgleeRLTSKVG-- 147
Cdd:COG4161 76 AIRLLrqkvGMVFQQynlwP------HLTVMENLIEAPCK--VLGLSKEQAREKAMKLLARL---------RLTDKADrf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 148 --LLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:COG4161 139 plHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
...
gi 2506233547 226 NVI 228
Cdd:COG4161 218 RII 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-229 |
4.75e-14 |
|
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: 68.73 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVN-EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG--VFALDGGQVILDGRDVSRLPEHRR 78
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 atdLGRVFQDPMrgTAADMQIVENLALAAR-RGesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQAL 157
Cdd:cd03213 84 ---IGYVPQDDI--LHPTLTVRETLMFAAKlRG--------------------------------------LSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHN-MNDAIRLGNRLIMMHEGNVIF 229
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIY 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
7.58e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnkSTVnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRA 79
Cdd:PRK15439 11 LLCARSISKQY--SGV---EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 TDLGRVFQDPMrgTAADMQIVENLALaarrgesrglswGITRDERASyrERLAEL--DLGLEERLTSKVGLLSGGQRQAL 157
Cdd:PRK15439 86 LGIYLVPQEPL--LFPNLSVKENILF------------GLPKRQASM--QKMKQLlaALGCQLDLDSSAGSLEVADRQIV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 158 TLLMAILKKPKLLLLDEHTAALDPktaskvlALTERLVG------EHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIF 229
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTP-------AETERLFSrirellAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-235 |
7.81e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRAT--DLGRVFQDPM-----RG 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRAVrsDIQMIFQDPLaslnpRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TAADMqIVENLalaarrgesRGLSWGITRDErasYRERLAELDLgleerltsKVGLL-----------SGGQRQALTLLM 161
Cdd:PRK15079 116 TIGEI-IAEPL---------RTYHPKLSRQE---VKDRVKAMML--------KVGLLpnlinryphefSGGQCQRIGIAR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 248
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-227 |
8.23e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.91 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDP--MRGTaa 95
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPvlFSGS-- 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 dmqIVENLALaarrgesrGLSWGITRDERASYRERLA-----ELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLL 170
Cdd:TIGR00958 571 ---VRENIAY--------GLTDTPDEEIMAAAKAANAhdfimEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 171 LLDEHTAALDpktaskvlALTERLVGE----HGLTTLMVTHNMNdAIRLGNRLIMMHEGNV 227
Cdd:TIGR00958 640 ILDEATSALD--------AECEQLLQEsrsrASRTVLLIAHRLS-TVERADQILVLKKGSV 691
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-154 |
8.54e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKstvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR-DVSRLPEHRRATDL 82
Cdd:COG0488 1 LENLSKSFGG-----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlRIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQDPMRGTAADMQIVENLALAARRGESRGLSWgitrDERASYRERLAELD--------------LGLEER-LTSKVG 147
Cdd:COG0488 76 LTVLDTVLDGDAELRALEAELEELEAKLAEPDEDL----ERLAELQEEFEALGgweaearaeeilsgLGFPEEdLDRPVS 151
|
....*..
gi 2506233547 148 LLSGGQR 154
Cdd:COG0488 152 ELSGGWR 158
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-228 |
1.04e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 5 KGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS------RLPEHRR 78
Cdd:PRK13641 6 ENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 ATDLgrVFQDPmrgtaaDMQIVENLALaaRRGESRGLSWGITRDERasyRERLAEL--DLGLEERLTSKVGL-LSGGQ-- 153
Cdd:PRK13641 86 KVSL--VFQFP------EAQLFENTVL--KDVEFGPKNFGFSEDEA---KEKALKWlkKVGLSEDLISKSPFeLSGGQmr 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 154 RQALTLLMAIlkKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13641 153 RVAIAGVMAY--EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-207 |
1.23e-13 |
|
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: 67.77 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGtaaD 96
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKP---E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 MQIVENLALAARrgesrglswgITRDERASYRERLAELDL-GLEERLtskVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:TIGR01189 88 LSALENLHFWAA----------IHGGAQRTIEDALAAVGLtGFEDLP---AAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2506233547 176 TAALDPKTaskvLALTERLVGEH---GLTTLMVTH 207
Cdd:TIGR01189 155 TTALDKAG----VALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-228 |
1.84e-13 |
|
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: 68.03 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH--RRAtdLGRVFQDPM----- 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRA--IGVVPQDTVlfndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 91 --------RGTAADMQIVEnlalAARRGesrglswgitrderasyreRLAELDLGLEERLTSKVG----LLSGGQRQALT 158
Cdd:cd03253 91 igynirygRPDATDEEVIE----AAKAA-------------------QIHDKIMRFPDGYDTIVGerglKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGehGLTTLMVTHNMNDAIRlGNRLIMMHEGNVI 228
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-91 |
2.10e-13 |
|
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: 67.17 E-value: 2.10e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 16 VNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV--FALDGGQVILDGRDVSRLPEHRRA-TDLGRVFQDPMR 91
Cdd:cd03217 10 VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERArLGIFLAFQYPPE 88
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-235 |
2.98e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALD---GGQVILDGRDVSRLPEHRRAtdlGRVFQD----P 89
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS---AYVQQDdlfiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 90 MRGTAADMQIVENLALAARrgesrglswgITRDERasyRERLAEL--DLGLEERLTSKVGL------LSGGQRQALTLLM 161
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRR----------VTKKEK---RERVDEVlqALGLRKCANTRIGVpgrvkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAI-RLGNRLIMMHEGNVIFDARDDE 235
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQ 253
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-228 |
3.06e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR--DVSRLP------EHRRatDLGRVFQD---- 88
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsdkairELRR--NVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 89 PmrgtaaDMQIVENLALAARRgeSRGLSwgitrdeRASYRERLAELDLGLeeRLTSKVGL----LSGGQRQALTLLMAIL 164
Cdd:PRK11124 95 P------HLTVQQNLIEAPCR--VLGLS-------KDQALARAEKLLERL--RLKPYADRfplhLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 165 KKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-228 |
3.10e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 8 TKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQ 87
Cdd:PRK13652 6 TRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 88 DPmrgtaaDMQIVENLAlaarrgeSRGLSWGITR----DERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAI 163
Cdd:PRK13652 86 NP------DDQIFSPTV-------EQDIAFGPINlgldEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 164 LKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-228 |
4.09e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG-----GQVILDGRDVSRLP----EHRRatDLGRVFQDPmrG 92
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDvdpiEVRR--EVGMVFQYP--N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TAADMQIVENLALAARRGesrGLSWGITR-DERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLL 171
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLN---GLVKSKKElDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 172 LDEHTAALDPKTASKVLALTERLVGEhgLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-228 |
5.21e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMrgTAAD 96
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPV--VLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 mQIVENLALAarRGESRGLSWgitrdeRASYRERLAELDLGLEERLTSKVG----LLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:PRK10790 430 -TFLANVTLG--RDISEEQVW------QALETVQLAELARSLPDGLYTPLGeqgnNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 173 DEHTAALDPKTASKVL-ALteRLVGEHglTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10790 501 DEATANIDSGTEQAIQqAL--AAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-255 |
7.51e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKST----VNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH 76
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRATDLGRVFQDPMRGTAADMQIVENLALAARrgesrgLSWGITRDERA-SYRERLAELDLgLEERLTSKVGLLSGGQRQ 155
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLNPRQRISQILDFPLR------LNTDLEPEQREkQIIETLRQVGL-LPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 ALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250 260
....*....|....*....|
gi 2506233547 236 KRRLRVHDLLQKFEEASGGE 255
Cdd:PRK15112 237 VLASPLHELTKRLIAGHFGE 256
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-228 |
8.35e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.22 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 5 KGVTKTFNKST----VNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG------GQVILDGRDVSRLP 74
Cdd:PRK14246 5 KSAEDVFNISRlylyINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 75 EHRRATDLGRVFQDPmrGTAADMQIVENLALAARrgesrglSWGIT--RDERASYRERLAELDLGLE--ERLTSKVGLLS 150
Cdd:PRK14246 85 AIKLRKEVGMVFQQP--NPFPHLSIYDNIAYPLK-------SHGIKekREIKKIVEECLRKVGLWKEvyDRLNSPASQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 151 GGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhgLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-227 |
9.07e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATdLG 83
Cdd:TIGR01257 931 VKNLVKIFEPSG---RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS-LG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQDPMrgTAADMQIVENLALAArrgESRGLSWgitrDERASYRERLAElDLGLEERLTSKVGLLSGGQRQALTLLMAI 163
Cdd:TIGR01257 1007 MCPQHNI--LFHHLTVAEHILFYA---QLKGRSW----EEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 164 LKKPKLLLLDEHTAALDPKTASKVLALTerLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-228 |
1.20e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR--LPEHRRAtdLGRVFQDPM--RGTaa 95
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRV--LSIIPQSPVlfSGT-- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 dmqIVENLALAARRGESrGLsWGITrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PLN03232 1326 ---VRFNIDPFSEHNDA-DL-WEAL--ERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 176 TAALDPKTASkvlaLTERLVGEH--GLTTLMVTHNMNDAIRLgNRLIMMHEGNVI 228
Cdd:PLN03232 1399 TASVDVRTDS----LIQRTIREEfkSCTMLVIAHRLNTIIDC-DKILVLSSGQVL 1448
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-225 |
1.36e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG---GQVILDGRDVSRLPEHR----RATDLGRVFQDPMRGT 93
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKElnklRAEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 AADMQIVENLAlaarrgESRGLSWGITRDEraSYRERLAELD-LGLEE---RLTSKVGLLSGGQRQALTLLMAILKKPKL 169
Cdd:PRK09473 111 NPYMRVGEQLM------EVLMLHKGMSKAE--AFEESVRMLDaVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 170 LLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-211 |
1.45e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTG-VDLHLEPGDFVTVIGGNGAGKSTLLNSIAGvFALDGGQVILDGRDVSRL-PEHRRATdLGRVFQDPM--RGTaad 96
Cdd:PRK11174 364 TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELdPESWRKH-LSWVGQNPQlpHGT--- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 mqIVENLALAARRGESRGLSWGItrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHT 176
Cdd:PRK11174 439 --LRDNVLLGNPDASDEQLQQAL---ENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190
....*....|....*....|....*....|....*.
gi 2506233547 177 AALDPKTASKVL-ALTErlvGEHGLTTLMVTHNMND 211
Cdd:PRK11174 514 ASLDAHSEQLVMqALNA---ASRRQTTLMVTHQLED 546
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-227 |
1.74e-12 |
|
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: 64.80 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTK----TFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSrLPEHR-- 77
Cdd:cd03248 8 LKGIVKfqnvTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 78 ---------RATDLGRVFQDPMR---GTAADMQIVEnlalAARRGESRGLswgitrderasyrerLAELDLGLEERLTSK 145
Cdd:cd03248 87 hskvslvgqEPVLFARSLQDNIAyglQSCSFECVKE----AAQKAHAHSF---------------ISELASGYDTEVGEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 146 VGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKV-LALTErlvGEHGLTTLMVTHNMNdAIRLGNRLIMMHE 224
Cdd:cd03248 148 GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVqQALYD---WPERRTVLVIAHRLS-TVERADQILVLDG 223
|
...
gi 2506233547 225 GNV 227
Cdd:cd03248 224 GRI 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-235 |
2.00e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATdLG 83
Cdd:PRK13536 44 LAGVSKSYG-----DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQ----DPmrgtaaDMQIVENLALAARrgesrglSWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTL 159
Cdd:PRK13536 118 VVPQfdnlDL------EFTVRENLLVFGR-------YFGMSTREIEAVIPSLLEF-ARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKtASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-230 |
2.46e-12 |
|
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: 63.49 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATdLGRVFQDPMrgtAAD 96
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-ISVLNQRPY---LFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 MQIVENLAlaaRRgesrglswgitrderasyrerlaeldlgleerltskvglLSGGQRQALTLLMAILKKPKLLLLDEHT 176
Cdd:cd03247 89 TTLRNNLG---RR---------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 177 AALDPKTASKVLalteRLVGEH--GLTTLMVTHNMNdAIRLGNRLIMMHEGNVIFD 230
Cdd:cd03247 127 VGLDPITERQLL----SLIFEVlkDKTLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-228 |
3.35e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKS-TLLNSI----AGVFALdGGQVILDGRDVSrlPEHRRATDLGRVFQDPMRGt 93
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQT-AGRVLLDGKPVA--PCALRGRKIATIMQNPRSA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 aadMQIVENLALAARRgesRGLSWGITRDErASYRERLAELDLGLEERLTSKVGL-LSGGQRQALTLLMAILKKPKLLLL 172
Cdd:PRK10418 92 ---FNPLHTMHTHARE---TCLALGKPADD-ATLTAALEAVGLENAARVLKLYPFeMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 173 DEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-228 |
4.14e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDG-------RDVSRL 73
Cdd:PRK10261 12 VLAVENLNIAFMQEQ-QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 74 PE-------HRRATDLGRVFQDPMRGTAADMQIVENLAlaarrgESRGLSWGITRDERASYRERLAELDLGLEER--LTS 144
Cdd:PRK10261 91 SEqsaaqmrHVRGADMAMIFQEPMTSLNPVFTVGEQIA------ESIRLHQGASREEAMVEAKRMLDQVRIPEAQtiLSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 145 KVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHE 224
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
....
gi 2506233547 225 GNVI 228
Cdd:PRK10261 245 GEAV 248
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-239 |
4.25e-12 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 65.45 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDP--MRGTAA 95
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVelFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 dmqivENLAlaaRRGESrglswgiTRDERASYRERLA---ELDLGLEERLTSKVGL----LSGGQRQALTLLMAILKKPK 168
Cdd:TIGR01842 410 -----ENIA---RFGEN-------ADPEKIIEAAKLAgvhELILRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 169 LLLLDEHTAALDPK----TASKVLALTERlvgehGLTTLMVTHNMNdAIRLGNRLIMMHEGNV-IFDARDDEKRRL 239
Cdd:TIGR01842 475 LVVLDEPNSNLDEEgeqaLANAIKALKAR-----GITVVVITHRPS-LLGCVDKILVLQDGRIaRFGERDEVLAKL 544
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-228 |
4.41e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 25 VDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRA-TDLGRVFQDPmrGTAADMQIVENL 103
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEA--SIFRRLSVYDNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 104 -ALAARRGEsrglswgITRDERASYRERLAElDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPK 182
Cdd:PRK10895 100 mAVLQIRDD-------LSAEQREDRANELME-EFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2506233547 183 TASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10895 172 SVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-180 |
6.09e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS--RLPEHRRATDLG----RVFQDpmr 91
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVsqnvHLFND--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 92 gtaadmQIVENLALAARRGESRGlswGITRDERASY-RERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLL 170
Cdd:PRK11176 432 ------TIANNIAYARTEQYSRE---QIEEAARMAYaMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
170
....*....|
gi 2506233547 171 LLDEHTAALD 180
Cdd:PRK11176 503 ILDEATSALD 512
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-162 |
1.21e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILdGRDVSR--LPEHRR 78
Cdd:COG0488 315 VLELEGLSKSYG-----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 ATDLgrvfqdpmrgtaaDMQIVENLALAA---RRGESRGL--SWGITRDerasyrerlaeldlgleeRLTSKVGLLSGGQ 153
Cdd:COG0488 389 ELDP-------------DKTVLDELRDGApggTEQEVRGYlgRFLFSGD------------------DAFKPVGVLSGGE 437
|
170
....*....|.
gi 2506233547 154 RQ--ALTLLMA 162
Cdd:COG0488 438 KArlALAKLLL 448
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-208 |
1.24e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDvSRLPEHR-RATDLGRvfQDPMRGTaa 95
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAeACHYLGH--RNAMKPA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 dMQIVENLALAARrgesrglswgITRDERASYRERLAELDLGLEERLtsKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK13539 88 -LTVAENLEFWAA----------FLGGEELDIAAALEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2506233547 176 TAALDpkTASKvlALTERLVGEH---GLTTLMVTHN 208
Cdd:PRK13539 155 TAALD--AAAV--ALFAELIRAHlaqGGIVIAATHI 186
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-228 |
1.30e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH--RRATDL--GRV--FQDPM 90
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISVvsQRVhlFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 91 RgtaadmqivENLALAArrgesrglswgitrdERASyRERLAEL--DLGLEERLTSKVGL----------LSGGQRQALT 158
Cdd:PRK11160 431 R---------DNLLLAA---------------PNAS-DEALIEVlqQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTErlvgEH--GLTTLMVTHNMNdAIRLGNRLIMMHEGNVI 228
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLA----EHaqNKTVLMITHRLT-GLEQFDRICVMDNGQII 552
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-225 |
1.34e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG--GQVILDGRDVSrlPEHRR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLK--ASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 ATD---LGRVFQDPMrgTAADMQIVENLALaarrGESRGLSWGITRDERASYR--ERLAELDLGLEErLTSKVGLLSGGQ 153
Cdd:TIGR02633 74 DTEragIVIIHQELT--LVPELSVAENIFL----GNEITLPGGRMAYNAMYLRakNLLRELQLDADN-VTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-227 |
1.64e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKpaltgVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRAtdLG 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKD-----INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 84 RVFQD----PMRGTAADMQIveNLALAarrgesrglswGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQRQALTL 159
Cdd:PRK11000 79 MVFQSyalyPHLSVAENMSF--GLKLA-----------GAKKEEINQRVNQVAEV-LQLAHLLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDpkTASKVLALTE--RLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLD--AALRVQMRIEisRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-225 |
1.69e-11 |
|
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: 61.72 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRdvsrlpehrratd 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDP--MRGTaadmqIVENLALAARRGESRglswgitrderasYRE---------RLAELDLGLE----ERLTSkv 146
Cdd:cd03250 68 IAYVSQEPwiQNGT-----IRENILFGKPFDEER-------------YEKvikacalepDLEILPDGDLteigEKGIN-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 147 glLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKvlaLTERLVGEHGL---TTLMVTHNMnDAIRLGNRLIMMH 223
Cdd:cd03250 128 --LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH---IFENCILGLLLnnkTRILVTHQL-QLLPHADQIVVLD 201
|
..
gi 2506233547 224 EG 225
Cdd:cd03250 202 NG 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-225 |
1.88e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFnkstvnekP---ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVsRLPEHRR 78
Cdd:PRK11288 5 LSFDGIGKTF--------PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 ATDLGR--VFQD----PmrgtaaDMQIVENL---ALAARRGesrglsWGITRDERASYRERLAELDLGLEERltSKVGLL 149
Cdd:PRK11288 76 ALAAGVaiIYQElhlvP------EMTVAENLylgQLPHKGG------IVNRRLLNYEAREQLEHLGVDIDPD--TPLKYL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-229 |
1.91e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 6 GVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV---FALD-GGQVILDGRDVSRLPEHRRAtd 81
Cdd:TIGR00956 61 GFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgFHIGvEGVITYDGITPEEIKKHYRG-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 lgrvfqDPMRGTAAD-----MQIVENLALAAR-RG-ESRGLswGITRDERASYRERLAELDLGLEERLTSKVGL-----L 149
Cdd:TIGR00956 139 ------DVVYNAETDvhfphLTVGETLDFAARcKTpQNRPD--GVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMN-DAIRLGNRLIMMHEGNVI 228
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQI 290
|
.
gi 2506233547 229 F 229
Cdd:TIGR00956 291 Y 291
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.18e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.45 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTAAdMQIV 100
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVFS-STVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 101 ENLALAARrgesrglSWGITRDERASyRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALD 180
Cdd:PRK13647 99 DDVAFGPV-------NMGLDKDEVER-RVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2506233547 181 PKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13647 171 PRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-228 |
2.20e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVD---LHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG----GQVILDGRDVSRLPEHRR----ATDLGRV 85
Cdd:PRK11022 15 DESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERrnlvGAEVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 FQDPMRGT----AADMQIVEnlALAARRGESRGlswgiTRDERAsyrerlaeLDL----GL---EERLTSKVGLLSGGQR 154
Cdd:PRK11022 95 FQDPMTSLnpcyTVGFQIME--AIKVHQGGNKK-----TRRQRA--------IDLlnqvGIpdpASRLDVYPHQLSGGMS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-228 |
2.47e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKST-------LLNSIAGVFAldGGQVILDGRDVSRLPEHR----RATDLGRV 85
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYP--SGDIRFHGESLLHASEQTlrgvRGNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 FQDPMRGT----AADMQIVENLALaarrgeSRGLSWGITRDERASYRERLaeldlGLEE---RLTSKVGLLSGGQRQALT 158
Cdd:PRK15134 98 FQEPMVSLnplhTLEKQLYEVLSL------HRGMRREAARGEILNCLDRV-----GIRQaakRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.56 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV------------------FALDGGQ 62
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyigdkKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 63 VILDGRDVSRLPEHRRAtdLGRVFQDP----MRGTAADMQIVENLALAARRGESRGLSwgitrderASYRERLAeLDLGL 138
Cdd:PRK13631 101 TNPYSKKIKNFKELRRR--VSMVFQFPeyqlFKDTIEKDIMFGPVALGVKKSEAKKLA--------KFYLNKMG-LDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 139 EERltSKVGlLSGGQ--RQALTLLMAIlkKPKLLLLDEHTAALDPKTASKVLALTERlVGEHGLTTLMVTHNMNDAIRLG 216
Cdd:PRK13631 170 LER--SPFG-LSGGQkrRVAIAGILAI--QPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVA 243
|
250
....*....|..
gi 2506233547 217 NRLIMMHEGNVI 228
Cdd:PRK13631 244 DEVIVMDKGKIL 255
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-228 |
3.23e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR--DVSRLPEHRRATDLGRVFQDPmrgtaa 95
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 DMQIV-----ENLALAARrgesrglSWGITRDERAsyRERLAELDLGLEERLTSK-VGLLSGGQRQALTLLMAILKKPKL 169
Cdd:PRK13638 87 EQQIFytdidSDIAFSLR-------NLGVPEAEIT--RRVDEALTLVDAQHFRHQpIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 170 LLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-214 |
3.39e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.72 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLL------NSIAGVFALDG-----GQVILDGrDVSRLPEHRRatdLGRVFQDP 89
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGkvtfhGKNLYAP-DVDPVEVRRR---IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 90 mrgTAADMQIVENLALAARRGESRGlswgiTRDERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKL 169
Cdd:PRK14243 101 ---NPFPKSIYDNIAYGARINGYKG-----DMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2506233547 170 LLLDEHTAALDPKTASKVLALTERLVGEHglTTLMVTHNMNDAIR 214
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAAR 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-228 |
4.34e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR--LPEHRRAtdLGRVFQDPM--RGTA- 94
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKV--LGIIPQAPVlfSGTVr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 ---------ADMQIVENLalaarrgesrglswgitrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILK 165
Cdd:PLN03130 1331 fnldpfnehNDADLWESL-------------------ERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 166 KPKLLLLDEHTAALDPKTAskvlALTERLVGEH--GLTTLMVTHNMNDAIRLgNRLIMMHEGNVI 228
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTD----ALIQKTIREEfkSCTMLIIAHRLNTIIDC-DRILVLDAGRVV 1451
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-227 |
6.49e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS--RLPEHRRatDLGRVFQDPmrgtaaDMQ 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRK--HIGIVFQNP------DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 99 IVENLAlaaRRGESRGL-SWGITRDErasYRERLAEL--DLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK13648 96 FVGSIV---KYDVAFGLeNHAVPYDE---MHRRVSEAlkQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 176 TAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRlGNRLIMMHEGNV 227
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-228 |
9.48e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTvnekpALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRlPEHRRAT--- 80
Cdd:NF033858 4 LEGVSHRYGKTV-----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 ------DLGR-------VFqdpmrgtaadmqivENLALAARrgesrgLsWGITRDERasyRERLAEL--DLGLEERLTSK 145
Cdd:NF033858 78 iaympqGLGKnlyptlsVF--------------ENLDFFGR------L-FGQDAAER---RRRIDELlrATGLAPFADRP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 146 VGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEH-GLTTLMVTHNMNDAIRLgNRLIMMHE 224
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDA 212
|
....
gi 2506233547 225 GNVI 228
Cdd:NF033858 213 GRVL 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-220 |
1.13e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRvfqdpMRGTAAD 96
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGH-----LPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 MQIVENL----ALAARRGESRGLSwgitrderasyrerlAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:PRK13543 97 LSTLENLhflcGLHGRRAKQMPGS---------------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 173 DEHTAALDPKTaskvLALTERLVGEH---GLTTLMVTHNMNDAIRLGNRLI 220
Cdd:PRK13543 162 DEPYANLDLEG----ITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRML 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-208 |
1.22e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 15 TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG--VFALDGGQVILDGRDVSRLPEHRRATD-LGRVFQDPMR 91
Cdd:COG0396 9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARAgIFLAFQYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 92 --GTAadmqiVENL---ALAARRGESRGLswgitRDERASYRERLAELdlGLEERLTSK---VGLlSGGQRQALTLLMAI 163
Cdd:COG0396 89 ipGVS-----VSNFlrtALNARRGEELSA-----REFLKLLKEKMKEL--GLDEDFLDRyvnEGF-SGGEKKRNEILQML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2506233547 164 LKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGlTTLMVTHN 208
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDR-GILIITHY 199
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-238 |
2.93e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG-----------GQVILDGR-DVSRLpehRRATDLgrVFQDP 89
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrvegrveffNQNIYERRvNLNRL---RRQVSM--VHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 90 mrgTAADMQIVENLALAARRgesrgLSW--GITRDERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKP 167
Cdd:PRK14258 98 ---NLFPMSVYDNVAYGVKI-----VGWrpKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLG----------NRLIMMHE---GNVIFDARDD 234
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSdftaffkgneNRIGQLVEfglTKKIFNSPHD 249
|
....
gi 2506233547 235 EKRR 238
Cdd:PRK14258 250 SRTR 253
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
16-235 |
5.59e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 16 VNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVfaLDG-GQVILDGRDVSRLPehrrATDLGRvfqdpMRG-- 92
Cdd:PRK03695 6 VAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQPLEAWS----AAELAR-----HRAyl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 -----TAADMQIVENLALAarrgesrgLSWGITRDERASYRERLAELdLGLEERLTSKVGLLSGGQ----RQALTLLM-- 161
Cdd:PRK03695 75 sqqqtPPFAMPVFQYLTLH--------QPDKTRTEAVASALNEVAEA-LGLDDKLGRSVNQLSGGEwqrvRLAAVVLQvw 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 162 -AILKKPKLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK03695 146 pDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-228 |
5.70e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 58.38 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTAAd 96
Cdd:cd03288 32 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 mqIVENLALAARRGESRglSWGITrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHT 176
Cdd:cd03288 111 --IRFNLDPECKCTDDR--LWEAL--EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 177 AALDPKTAS---KVL--ALTERLVgehgLTTLMVTHNMNDAirlgNRLIMMHEGNVI 228
Cdd:cd03288 185 ASIDMATENilqKVVmtAFADRTV----VTIAHRVSTILDA----DLVLVLSRGILV 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-228 |
5.97e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 11 FNKSTvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH-----RRatDLGRV 85
Cdd:PRK10261 330 LNRVT-REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalRR--DIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 FQDPM-----RGTAADmQIVENLALAarrgesrglswGITRDERAsyRERLAELdlgLEerltsKVGLL----------- 149
Cdd:PRK10261 407 FQDPYasldpRQTVGD-SIMEPLRVH-----------GLLPGKAA--AARVAWL---LE-----RVGLLpehawryphef 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-209 |
6.31e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDV---SRLPEHRRATDLGRVFQDPM-----RG 92
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPYgslnpRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TAADmQIVENLALAARrgesrglswgITRDERasyRERLAELdlgleerlTSKVGL-----------LSGGQRQALTLLM 161
Cdd:PRK11308 110 KVGQ-ILEEPLLINTS----------LSAAER---REKALAM--------MAKVGLrpehydryphmFSGGQRQRIAIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2506233547 162 AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNM 209
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-228 |
6.34e-10 |
|
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: 59.06 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEH--RRAtdLGRVFQDPM--RGT 93
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAA--IGIVPQDTVlfNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 aadmqIVENLALAArrgesrglsWGITRDE--RASyreRLAELD---LGLEERLTSKV---GL-LSGGQRQ----ALTLL 160
Cdd:COG5265 448 -----IAYNIAYGR---------PDASEEEveAAA---RAAQIHdfiESLPDGYDTRVgerGLkLSGGEKQrvaiARTLL 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 161 M--AIlkkpklLLLDEHTAALDPKTASKVLALTERLVGEHglTTLMVTHnmndaiRL-----GNRLIMMHEGNVI 228
Cdd:COG5265 511 KnpPI------LIFDEATSALDSRTERAIQAALREVARGR--TTLVIAH------RLstivdADEILVLEAGRIV 571
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-225 |
7.39e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.38 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFAlDGGQVI-----LDGRDVSRL-PEHRRA---TDLGRVFQDPMR 91
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTadrfrWNGIDLLKLsPRERRKiigREIAMIFQEPSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 92 GTAADMQIVENLALAARRGESRGLSWgitrdERASYRERLAEldlgleeRLTSKVGL-------------LSGGQRQALT 158
Cdd:COG4170 101 CLDPSAKIGDQLIEAIPSWTFKGKWW-----QRFKWRKKRAI-------ELLHRVGIkdhkdimnsypheLTEGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-68 |
7.62e-10 |
|
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: 55.92 E-value: 7.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 2 LVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGR 68
Cdd:cd03221 1 IELENLSKTYGGKLL-----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-152 |
1.13e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRL-PEHRRATDLGRVFQDPMR-GTAAD 96
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsPRERRRLGVAYIPEDRLGrGLVPD 350
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 97 MQIVENLALAARRGE--SRG--LSWGITRdERAsyRERLAELDLgleeRLTS---KVGLLSGG 152
Cdd:COG3845 351 MSVAENLILGRYRRPpfSRGgfLDRKAIR-AFA--EELIEEFDV----RTPGpdtPARSLSGG 406
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-255 |
1.26e-09 |
|
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: 58.28 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV--FALDGGQVILDgrdVSRLPEHRRATD 81
Cdd:TIGR03269 3 VKNLTKKFD-----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH---VALCEKCGYVER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQD-PMRGTAADMQIVE--NLALAARR-----------------GESRGLSWGITRDERASYR-----ERLAEL-- 134
Cdd:TIGR03269 75 PSKVGEPcPVCGGTLEPEEVDfwNLSDKLRRrirkriaimlqrtfalyGDDTVLDNVLEALEEIGYEgkeavGRAVDLie 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 135 DLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIR 214
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2506233547 215 LGNRLIMMHEGNVIFDARDDE--KRRLRVHDLLQKFEEASGGE 255
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEvvAVFMEGVSEVEKECEVEVGE 277
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-228 |
2.29e-09 |
|
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: 55.88 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPmrgTAADMQI 99
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDP---TLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLalaarrgesrglswgiTRDERASYRERLAELDLgleerltSKVGL-LSGGQRQALTLLMAILKKPKLLLLDEHTAA 178
Cdd:cd03369 99 RSNL----------------DPFDEYSDEEIYGALRV-------SEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 179 LDPKTAskvlALTERLVGEH--GLTTLMVTHNMNDAIRLgNRLIMMHEGNVI 228
Cdd:cd03369 156 IDYATD----ALIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
3.47e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnkSTVnekPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALD--GGQVILDGRDVSrlPEHRR 78
Cdd:PRK13549 5 LLEMKNITKTF--GGV---KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQ--ASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 79 ATD---LGRVFQDPMrgTAADMQIVENLALAARRGESrglswGITRDERASYR--ERLAELDLGLEERLtsKVGLLSGGQ 153
Cdd:PRK13549 78 DTEragIAIIHQELA--LVKELSVLENIFLGNEITPG-----GIMDYDAMYLRaqKLLAQLKLDINPAT--PVGNLGLGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 154 RQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMND 211
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNE 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-220 |
4.70e-09 |
|
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: 55.49 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 27 LHLEPGDF-----VTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVfqdpmrgtaadmqive 101
Cdd:cd03237 15 LEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTV---------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 nlalaarrgesRGLSWGITRD--ERASYRERLAElDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAAL 179
Cdd:cd03237 79 -----------RDLLSSITKDfyTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2506233547 180 DPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLI 220
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-262 |
5.49e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTllnsiaGVFALDggqviLDGRDVSRLP-------EH 76
Cdd:NF000106 16 VRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAH-----V*GPDAGRRPwrf*twcAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRATDLGRVFQDPMR-GTAADMQIVENLALAARRGE-SRglswgitRDERASYRERLAELDLglEERLTSKVGLLSGGQR 154
Cdd:NF000106 80 RRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDlSR-------KDARARADELLERFSL--TEAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 155 QALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDD 234
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
250 260
....*....|....*....|....*...
gi 2506233547 235 EkRRLRVHDLLQKFEEASGGELanDRML 262
Cdd:NF000106 230 E-LKTKVGGRTLQIRPAHAAEL--DRMV 254
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-222 |
6.77e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVsrlpehRRATD 81
Cdd:PRK15056 7 IVVNDVTVTWR----NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT------RQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 82 LGRVFQDPmRGTAADMQ---IVENLALAARRGESRGLSWGITRDeRASYRERLAELDLgLEERlTSKVGLLSGGQRQALT 158
Cdd:PRK15056 77 KNLVAYVP-QSEEVDWSfpvLVEDVVMMGRYGHMGWLRRAKKRD-RQIVTAALARVDM-VEFR-HRQIGELSGGQKKRVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 159 LLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMM 222
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-207 |
7.14e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 7 VTKTFNKS-TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGvfALDGGQViLDGRDVSRLPEHRRATDLGRV 85
Cdd:COG2401 30 VLEAFGVElRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPV-AGCVDVPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 fqdPMRGTAADmqIVENLALAarrgesrGLSwgitrdERASYRERLAEldlgleerltskvglLSGGQRQALTLLMAILK 165
Cdd:COG2401 107 ---GRKGDFKD--AVELLNAV-------GLS------DAVLWLRRFKE---------------LSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2506233547 166 KPKLLLLDEHTAALDPKTAsKVLALT-ERLVGEHGLTTLMVTH 207
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTA-KRVARNlQKLARRAGITLVVATH 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-228 |
9.95e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 13 KSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKST----LLNSIAGvfaldGGQVILDGRDVSR------LPEHRRatdL 82
Cdd:PRK15134 293 KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNlnrrqlLPVRHR---I 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 83 GRVFQDPmrgtaadmqiveNLALAARRGESRGLSWGITRDERA-SYRERLAELDLGLEErltskVGL-----------LS 150
Cdd:PRK15134 365 QVVFQDP------------NSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEE-----VGLdpetrhrypaeFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 151 GGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-72 |
1.01e-08 |
|
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: 55.57 E-value: 1.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 2 LVLKGVTKTFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR 72
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA 398
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-91 |
1.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDgRD--VSRLPehrratdlgrvfQDPMR 91
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARLQ------------QDPPR 77
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-63 |
1.24e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 2 LVLKGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQV 63
Cdd:PRK15064 320 LEVENLTKGFD-----NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-180 |
1.32e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 15 TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV--FALDGGQVILDGRDVSRL-PEHRRATDLGRVFQDPMR 91
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELsPEDRAGEGIFMAFQYPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 92 GTAADMQIVENLALAARRgESRGLSwGITRDERASYRERLAELDLGLEERLTSKVGL-LSGGQRQALTLLMAILKKPKLL 170
Cdd:PRK09580 90 IPGVSNQFFLQTALNAVR-SYRGQE-PLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELC 167
|
170
....*....|
gi 2506233547 171 LLDEHTAALD 180
Cdd:PRK09580 168 ILDESDSGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-228 |
2.03e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSrLPEHRRATDLGRVFQDPMRGTAADMQIV 100
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID-FKSSKEALENGISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 101 ENLALAarrgesRGLSWGITRDERASYRERLA---ELDLGLEERltSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTA 177
Cdd:PRK10982 92 DNMWLG------RYPTKGMFVDQDKMYRDTKAifdELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 178 ALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-207 |
2.15e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPE--HRRATDLGRVfqdpmRGTAA 95
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLLYLGHQ-----PGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 96 DMQIVENLALAARrgesrgLSWGITRDERASYRERlaeldLGLEERLTSKVGLLSGGQR------------QALTLLmai 163
Cdd:PRK13538 88 ELTALENLRFYQR------LHGPGDDEALWEALAQ-----VGLAGFEDVPVRQLSAGQQrrvalarlwltrAPLWIL--- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2506233547 164 lkkpkllllDEHTAALDpKTASKVLaltERLVGEH---GLTTLMVTH 207
Cdd:PRK13538 154 ---------DEPFTAID-KQGVARL---EALLAQHaeqGGMVILTTH 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-229 |
2.20e-08 |
|
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: 53.04 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG---GQVILDGRDVSRlpeHRRATDLGRVFQDPMrgT 93
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQKCVAYVRQDDI--L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 AADMQIVENLALAARRGESRGLSWGItRDERAsyrERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLD 173
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAI-RKKRV---EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2506233547 174 EHTAALDPKTASKVLALTERLvGEHGLTTLMVTHN-MNDAIRLGNRLIMMHEGNVIF 229
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQL-ARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVY 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-230 |
2.21e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG--------GQVILDGRDVSRLPEHRRATDLGRVFQDPMRGT 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 94 A--ADMQIVENLALAARRG-----ESRGLSWgitrdeRASYRERLAELDlgleerlTSKVGLLSGGQ------RQALTLL 160
Cdd:PRK13547 97 AfsAREIVLLGRYPHARRAgalthRDGEIAW------QALALAGATALV-------GRDVTTLSGGElarvqfARVLAQL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 161 M---AILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFD 230
Cdd:PRK13547 164 WpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-207 |
2.36e-08 |
|
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: 52.88 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTaadM 97
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTT---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAARRGesrglswgitrdERASYRERLAELDL-GLEERLtskVGLLSGGQRQALTLLMAILKKPKLLLLDEHT 176
Cdd:cd03231 89 SVLENLRFWHADH------------SDEQVEEALARVGLnGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|...
gi 2506233547 177 AALDpktASKVLALTERLVG--EHGLTTLMVTH 207
Cdd:cd03231 154 TALD---KAGVARFAEAMAGhcARGGMVVLTTH 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-225 |
3.36e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFNKSTvneKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVsrlpehrrAT 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTS---SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQD----PMRGTAADMQI-VENLALAAR-RGE-----SRGLSWGITRDERASYRERLAeldlgleerltskvGLL 149
Cdd:TIGR01257 2006 NISDVHQNmgycPQFDAIDDLLTgREHLYLYARlRGVpaeeiEKVANWSIQSLGLSLYADRLA--------------GTY 2071
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 150 SGGQRQALTLLMAILKKPKLLLLDEHTAALDPKtASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ-ARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-233 |
4.49e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR-------------LPEHRRATdlgrv 85
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVPEDRKGE----- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 86 fqdpmrGTAADMQIVENLALAARRGESRglsWGI--TRDERASYRERLAELDL---GLEErltsKVGLLSGGQRQ----- 155
Cdd:COG1129 340 ------GLVLDLSIRENITLASLDRLSR---GGLldRRRERALAEEYIKRLRIktpSPEQ----PVGNLSGGNQQkvvla 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 156 -ALT-----LLMailkkpkllllDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNV-- 227
Cdd:COG1129 407 kWLAtdpkvLIL-----------DEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIvg 474
|
....*.
gi 2506233547 228 IFDARD 233
Cdd:COG1129 475 ELDREE 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-185 |
5.46e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnkstvnekP---ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-RLPEH 76
Cdd:PRK10762 4 LLQLKGIDKAF--------PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 77 RRATDLGRVFQDpmRGTAADMQIVENLALaarrGESRGLSWGitrdeRASYRERLAELD-----LGLEERLTSKVGLLSG 151
Cdd:PRK10762 76 SQEAGIGIIHQE--LNLIPQLTIAENIFL----GREFVNRFG-----RIDWKKMYAEADkllarLNLRFSSDKLVGELSI 144
|
170 180 190
....*....|....*....|....*....|....*
gi 2506233547 152 GQRQALTLLMAILKKPKLLLLDEHTAAL-DPKTAS 185
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPTDALtDTETES 179
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-235 |
8.32e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 1 MLVLKGVTKTFnkstvnekP---ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFAlDG---GQVILDGrDVSRLP 74
Cdd:NF040905 1 ILEMRGITKTF--------PgvkALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDG-EVCRFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 75 EHRRATDLGRVF--QD----PMrgtaadMQIVENLALAARRGeSRGL-SWGITRdERAsyRERLAELdlGLEERLTSKVG 147
Cdd:NF040905 71 DIRDSEALGIVIihQElaliPY------LSIAENIFLGNERA-KRGViDWNETN-RRA--RELLAKV--GLDESPDTLVT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 148 LLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRT 217
|
250
....*....|
gi 2506233547 228 I--FDARDDE 235
Cdd:NF040905 218 IetLDCRADE 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-232 |
8.41e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 15 TVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDG--GQVILDGRDVSRlPEHRRAtdlGRVFQDPMrg 92
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-QILKRT---GFVTQDDI-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TAADMQIVENLALAARRGESRGLswgiTRDERASYRERLAElDLGLEERLTSKVGL-----LSGGQRQALTLLMAILKKP 167
Cdd:PLN03211 151 LYPHLTVRETLVFCSLLRLPKSL----TKQEKILVAESVIS-ELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 168 KLLLLDEHTAALDpKTASKVLALTERLVGEHGLTTLMVTHNMNDAI-RLGNRLIMMHEGNVIFDAR 232
Cdd:PLN03211 226 SLLILDEPTSGLD-ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGK 290
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-89 |
8.89e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 13 KSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG--VFALDGGQVILDGRDVSRL-PEHRRATDLGRVFQDP 89
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLePEERAHLGIFLAFQYP 93
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-234 |
1.16e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNKSTVNEKPALTGVD--------LHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-RLP 74
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSRDrkkvrdisFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 75 ------------EHRRATdlgrvfqdpmrGTAADMQIVENLALAARRGESR-GLSWGI--TRDERASYRERLAELDL--- 136
Cdd:PRK09700 333 ldavkkgmayitESRRDN-----------GFFPNFSIAQNMAISRSLKDGGyKGAMGLfhEVDEQRTAENQRELLALkch 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 137 GLEERLTSkvglLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLG 216
Cdd:PRK09700 402 SVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVC 476
|
250 260
....*....|....*....|
gi 2506233547 217 NRLIMMHEGNV--IFDARDD 234
Cdd:PRK09700 477 DRIAVFCEGRLtqILTNRDD 496
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-249 |
1.68e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 2 LVLKGVTKTFNKSTVNEKPaltgVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-RLPEHRRA- 79
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGP----INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 80 -----TDLgRVFQDPM--RGTAADMQIVEnlalaarrgesrglswgitrderaSYRERlaeldLGLEERLTSKVGL---- 148
Cdd:PRK10522 399 fsavfTDF-HLFDQLLgpEGKPANPALVE------------------------KWLER-----LKMAHKLELEDGRisnl 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 149 -LSGGQRQALTLLMAILKKPKLLLLDEHTAALDP---KTASKVLAlteRLVGEHGLTTLMVTHnmNDA-IRLGNRLIMMH 223
Cdd:PRK10522 449 kLSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrREFYQVLL---PLLQEMGKTIFAISH--DDHyFIHADRLLEMR 523
|
250 260
....*....|....*....|....*.
gi 2506233547 224 EGNVIfdARDDEKRRLRVHDLLQKFE 249
Cdd:PRK10522 524 NGQLS--ELTGEERDAASRDAVARTA 547
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-228 |
3.65e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTAAd 96
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 mqIVENLALaarrGESRGLSWGITRDER-ASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK10789 405 --VANNIAL----GRPDATQQEIEHVARlASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 176 TAALDPKTASKVLAlTERLVGEHglTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:PRK10789 479 LSAVDGRTEHQILH-NLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-227 |
6.15e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTAAdmqIVE 101
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGS---LRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 NLALAARRGESRgLSWGItrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDP 181
Cdd:TIGR00957 1379 NLDPFSQYSDEE-VWWAL---ELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2506233547 182 KTASKVLAlTERLVGEHgLTTLMVTHNMNdAIRLGNRLIMMHEGNV 227
Cdd:TIGR00957 1455 ETDNLIQS-TIRTQFED-CTVLTIAHRLN-TIMDYTRVIVLDKGEV 1497
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-239 |
6.46e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-RLPEHRRATDLGRVFQDPMR-GTAADM 97
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRKRdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAARRGESRGlsWGITRDERasyrERLAELDL---------GLEERltskVGLLSGGQRQALTLLMAILKKPK 168
Cdd:PRK10762 346 SVKENMSLTALRYFSRA--GGSLKHAD----EQQAVSDFirlfniktpSMEQA----IGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 169 LLLLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI--FDARDDEKRRL 239
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISgeFTREQATQEKL 487
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-207 |
1.24e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRlpehRRATdlgrvFQdpmrgtaad 96
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCT-----YQ--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 mqivENLALAarrGESRGLSWGITRDERASYRERLAELDLGLEERLT---------SKVGLLSGGQRQALTLLMAILKKP 167
Cdd:PRK13540 74 ----KQLCFV---GHRSGINPYLTLRENCLYDIHFSPGAVGITELCRlfslehlidYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTErlvgEH---GLTTLMVTH 207
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQ----EHrakGGAVLLTSH 185
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-235 |
3.23e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV----FALDGGQVILDGRDVSRL-PEHRR---ATDLGRVFQDPMRG 92
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLsPRERRklvGHNVSMIFQEPQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TAADMQIVENLALAARRGESRGLSWgitrdERASYRERLAeldlgLEerLTSKVGL-------------LSGGQRQALTL 159
Cdd:PRK15093 102 LDPSERVGRQLMQNIPGWTYKGRWW-----QRFGWRKRRA-----IE--LLHRVGIkdhkdamrsfpyeLTEGECQKVMI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 160 LMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDARDDE 235
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-181 |
4.56e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR--LPEHRRATDLgrVFQDPM--RGTAAdm 97
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSM--IPQDPVlfDGTVR-- 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 98 QIVENLALAARRGESRGLswgitrdERASYRERLAELDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKL-LLLDEHT 176
Cdd:PTZ00243 1402 QNVDPFLEASSAEVWAAL-------ELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGfILMDEAT 1474
|
....*
gi 2506233547 177 AALDP 181
Cdd:PTZ00243 1475 ANIDP 1479
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-210 |
6.03e-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: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGrDVSRLPEH--------RRATDLGRVFQD 88
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQawiqndslRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 89 PMRgtaadMQIVENLALaarrgesrglswgitrderasyrerLAELDL---GLEERLTSKVGLLSGGQRQALTLLMAILK 165
Cdd:TIGR00957 728 KYY-----QQVLEACAL-------------------------LPDLEIlpsGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2506233547 166 KPKLLLLDEHTAALDPKTASKVLaltERLVGEHGL----TTLMVTHNMN 210
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIF---EHVIGPEGVlknkTRILVTHGIS 823
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-225 |
8.52e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 11 FNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFA-LDGGQVILDGrDVSRLPEhrratdLGRVFQDP 89
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRG-SVAYVPQ------VSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 90 MRgtaadmqivENLALAARRGESRglsWGITRDERASYRerlaELDLgLEERLTSKVGL----LSGGQRQALTLLMAILK 165
Cdd:PLN03232 695 VR---------ENILFGSDFESER---YWRAIDVTALQH----DLDL-LPGRDLTEIGErgvnISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 166 KPKLLLLDEHTAALDPKTASKVL--ALTERLVGEhglTTLMVTHNMNdAIRLGNRLIMMHEG 225
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFdsCMKDELKGK---TRVLVTNQLH-FLPLMDRIILVSEG 815
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-229 |
8.52e-06 |
|
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: 46.83 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRdVSRLPEhrratdlgrvFQDPMRGTaadmqI 99
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQ----------TSWIMPGT-----I 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLAlaarrgesrglsWGITRDErasYRERLAELDLGLEERLT-----SKVGL------LSGGQRQALTLLMAILKKPK 168
Cdd:TIGR01271 504 KDNII------------FGLSYDE---YRYTSVIKACQLEEDIAlfpekDKTVLgeggitLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 169 LLLLDEHTAALDpktaskvlALTERLVGEHGLTTLM-------VTHNMnDAIRLGNRLIMMHEGNVIF 229
Cdd:TIGR01271 569 LYLLDSPFTHLD--------VVTEKEIFESCLCKLMsnktrilVTSKL-EHLKKADKILLLHEGVCYF 627
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-228 |
1.29e-05 |
|
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: 45.95 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQV-ILDGRD----VSRLPEHR-RATD-LGRVFQD----P 89
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdmTKPGPDGRgRAKRyIGILHQEydlyP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 90 MRgtaadmQIVENLAlaarrgESRGLSWgitRDERASYRERLAELDLGLEERLTSKV-----GLLSGGQRQALTLLMAIL 164
Cdd:TIGR03269 379 HR------TVLDNLT------EAIGLEL---PDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 165 KKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVI 228
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-65 |
1.35e-05 |
|
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: 46.08 E-value: 1.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 5 KGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVIL 65
Cdd:TIGR03719 326 ENLTKAFG-----DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-220 |
1.95e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 27 LHLEPGDF-----VTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRdVSRLPEHRRAtdlgrvfqdpmrgtAADMQIVE 101
Cdd:PRK13409 355 LEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISYKPQYIKP--------------DYDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 NLALAARRGESrglSWgitrderasYRERLAElDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDP 181
Cdd:PRK13409 420 LLRSITDDLGS---SY---------YKSEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2506233547 182 K---TASKVLaltERLVGEHGLTTLMVTHN--MNDAIrlGNRLI 220
Cdd:PRK13409 487 EqrlAVAKAI---RRIAEEREATALVVDHDiyMIDYI--SDRLM 525
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-227 |
2.19e-05 |
|
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: 45.20 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 25 VDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVF-ALDGGQVILDGRDVS-RLPEHRRATDLGRVFQDPMR-GTAADMQIVE 101
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKRhGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 NLALAARRGESrglswGITRDERAsyrerlAELDLGLEE--RLTSK-------VGLLSGGQRQALTLLMAILKKPKLLLL 172
Cdd:TIGR02633 359 NITLSVLKSFC-----FKMRIDAA------AELQIIGSAiqRLKVKtaspflpIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 173 DEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-207 |
2.61e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 22 LTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGvfALDGGqVILDGRDVSRLPEhrRATDLGRVF-----QDPMRGTAAd 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRLVNGRP--LDSSFQRSIgyvqqQDLHLPTST- 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 mqIVENLALAA--RRGESrglswgITRDERASYRERLAELdLGLEERLTSKVGL----LSGGQRQALTL---LMAilKKP 167
Cdd:TIGR00956 853 --VRESLRFSAylRQPKS------VSKSEKMEYVEEVIKL-LEMESYADAVVGVpgegLNVEQRKRLTIgveLVA--KPK 921
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2506233547 168 KLLLLDEHTAALDPKTASKVLALTERLVgEHGLTTLMVTH 207
Cdd:TIGR00956 922 LLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-240 |
3.37e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.99 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 18 EKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDV-----SRLPEHRRATDLgrVFQDPMRG 92
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSM--LFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 93 TaaDMQIVENLALAARrgESRGLSWGITrdeRASYRERLAELDL-GLEERLTSKvglLSGGQRQALTLLMAILKKPKLLL 171
Cdd:PRK11831 97 T--DMNVFDNVAYPLR--EHTQLPAPLL---HSTVMMKLEAVGLrGAAKLMPSE---LSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506233547 172 LDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNVIFDA-----RDDEKRRLR 240
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGsaqalQANPDPRVR 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-227 |
3.37e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 10 TFNKSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVF-ALDGGQVILDGRdVSRLPEhrratdLGRVFQD 88
Cdd:PLN03130 621 YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGT-VAYVPQ------VSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 89 PMRgtaadmqivENLALaarrgesrGLSWGITRDERASYRERLA-ELDLgLEERLTSKVGL----LSGGQRQALTLLMAI 163
Cdd:PLN03130 694 TVR---------DNILF--------GSPFDPERYERAIDVTALQhDLDL-LPGGDLTEIGErgvnISGGQKQRVSMARAV 755
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506233547 164 LKKPKLLLLDEHTAALDPKTASKVL--ALTERLVGEhglTTLMVTHNMNDAIRLgNRLIMMHEGNV 227
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFdkCIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-65 |
4.08e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 4.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506233547 5 KGVTKTFNkstvnEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVIL 65
Cdd:PRK11819 328 ENLSKSFG-----DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-63 |
6.61e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 6.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 1 MLVLKGVTKTFNKSTVnekpaLTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQV 63
Cdd:PRK09544 4 LVSLENVSVSFGQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI 61
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-54 |
1.52e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.87 E-value: 1.52e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG 54
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-67 |
1.95e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 1.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2506233547 21 ALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDG 67
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-229 |
1.96e-04 |
|
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: 41.77 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 20 PALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRdVSRLPEhrratdlgrvFQDPMRGTaadmqI 99
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQ----------FSWIMPGT-----I 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLAlaarrgesrglsWGITRDErasYRERLAELDLGLEERLTS----------KVGL-LSGGQRQALTLLMAILKKPK 168
Cdd:cd03291 115 KENII------------FGVSYDE---YRYKSVVKACQLEEDITKfpekdntvlgEGGItLSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 169 LLLLDEHTAALDpktaskvlALTERLVGEHGLTTLM-------VTHNMnDAIRLGNRLIMMHEGNVIF 229
Cdd:cd03291 180 LYLLDSPFGYLD--------VFTEKEIFESCVCKLManktrilVTSKM-EHLKKADKILILHEGSSYF 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-76 |
2.25e-04 |
|
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: 40.60 E-value: 2.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 26 DLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVIL-DGRDVSRLPEH 76
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQR 72
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-55 |
3.08e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 3.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2506233547 3 VLKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV 55
Cdd:PRK11819 8 TMNRVSKVVP----PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 56
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-54 |
3.30e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 3.30e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG 54
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-110 |
3.98e-04 |
|
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: 39.66 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 31 PGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSRLPEHRRATDLGRVFQDPMRGTAADMQIVENLALAARRG 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-207 |
4.15e-04 |
|
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: 41.46 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 4 LKGVTKTFNkstvNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGV---FalDGGQVILDGRDVSRLPEHRRAT 80
Cdd:TIGR03719 7 MNRVSKVVP----PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdF--NGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 81 DLGRVFQDPMRGTAADMQIVENL---------------ALAARRGESRGL-----SWGITRD-ERASYRERLAELDlgle 139
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFneisakyaepdadfdKLAAEQAELQEIidaadAWDLDSQlEIAMDALRCPPWD---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 140 erltSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDpktASKVLALtERLVGEHGLTTLMVTH 207
Cdd:TIGR03719 157 ----ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWL-ERHLQEYPGTVVAVTH 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-209 |
7.22e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 27 LHLEPGDF-----VTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRdVSRLPEhrratdlgRVFQDpmrgtaADMQIVE 101
Cdd:COG1245 356 LEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISYKPQ--------YISPD------YDGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 102 NLALAArrGESRGLSWgitrderasYRERLAElDLGLEERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDP 181
Cdd:COG1245 421 FLRSAN--TDDFGSSY---------YKTEIIK-PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190
....*....|....*....|....*....|.
gi 2506233547 182 K---TASKVLaltERLVGEHGLTTLMVTHNM 209
Cdd:COG1245 489 EqrlAVAKAI---RRFAENRGKTAMVVDHDI 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-227 |
9.75e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 25 VDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVS-RLPehRRATDLGRVFQDPMR---GTAADMQIV 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSP--RDAIRAGIMLCPEDRkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 101 ENLALAARRGESRGLSWGITRDERASYRERLAELDLGLEERLTsKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALD 180
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQ-LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2506233547 181 PKTASKVLALTERLvGEHGLTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK11288 429 VGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-68 |
1.00e-03 |
|
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: 39.15 E-value: 1.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 19 KPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG--VFALDGGQVILDGR 68
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGR 71
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-225 |
1.03e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 12 NKSTVNEKPALTGVDL----------HLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILDGRDVSR--------- 72
Cdd:PRK15439 259 RRQQAAGAPVLTVEDLtgegfrnislEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrlar 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 73 ----LPEHRRATDLgrvFQD-PMRGTAADMqIVENLALAARRGEsrglswgitrdERASYRERLAELDLGLEErLTSKVG 147
Cdd:PRK15439 339 glvyLPEDRQSSGL---YLDaPLAWNVCAL-THNRRGFWIKPAR-----------ENAVLERYRRALNIKFNH-AEQAAR 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506233547 148 LLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERlVGEHGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS-IAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
24-60 |
1.21e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2506233547 24 GVDLHLEPGdfVTVIGG-NGAGKSTLLNSIAgvFALDG 60
Cdd:pfam13476 11 DQTIDFSKG--LTLITGpNGSGKTTILDAIK--LALYG 44
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-57 |
1.23e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|....
gi 2506233547 25 VDLHLEPGDFVTVIGG-NGAGKSTLLNSIAGVFA 57
Cdd:COG3950 17 LEIDFDNPPRLTVLVGeNGSGKTTLLEAIALALS 50
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-54 |
1.52e-03 |
|
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: 38.78 E-value: 1.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2506233547 13 KSTVNEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAG 54
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN 55
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
20-53 |
1.66e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.98 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2506233547 20 PALTGVD-LHLEPGdfVTVI-GGNGAGKSTLLNSIA 53
Cdd:COG3910 25 PAVRNLEgLEFHPP--VTFFvGENGSGKSTLLEAIA 58
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
144-222 |
2.04e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 2.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506233547 144 SKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTASKVLALTERLVGEHGLTTLMVTHNMNdAIRLGNRLIMM 222
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-227 |
3.39e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 17 NEKPALTGVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQVILdgrdvsrlpehRRATDLGRVFQDPMRGTAAD 96
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIKLGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 97 MQIVENLALAARRGESRGLswgitRDERASYrerlaeldlGLE-ERLTSKVGLLSGGQRQALTLLMAILKKPKLLLLDEH 175
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKL-----RDYLGGF---------GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2506233547 176 TAALDPKTASkvlALTERLVGEHGlTTLMVTHNMNDAIRLGNRLIMMHEGNV 227
Cdd:PRK10636 458 TNHLDLDMRQ---ALTEALIDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
34-65 |
6.27e-03 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 36.86 E-value: 6.27e-03
10 20 30
....*....|....*....|....*....|..
gi 2506233547 34 FVTVIGGNGAGKSTLLNSIAGVFALDGGQVIL 65
Cdd:cd01672 2 FIVFEGIDGAGKTTLIELLAERLEARGYEVVL 33
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-194 |
6.87e-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: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 35 VTVIGG-NGAGKSTLLNSIAgvFALdGGQVILDGRDVSRLPehRRATDLGRV-------------------FQDPMRGTA 94
Cdd:COG0419 25 LNLIVGpNGAGKSTILEAIR--YAL-YGKARSRSKLRSDLI--NVGSEEASVelefehggkryrierrqgeFAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 95 AD-MQIVENLALAARRGESRGLswgiTRDERASYRERLAELD--LGLEERLTSK------VGLLSGGQRQALTLLMAILK 165
Cdd:COG0419 100 SErKEALKRLLGLEIYEELKER----LKELEEALESALEELAelQKLKQEILAQlsgldpIETLSGGERLRLALADLLSL 175
|
170 180
....*....|....*....|....*....
gi 2506233547 166 KPKlllldehTAALDPKTASKVLALTERL 194
Cdd:COG0419 176 ILD-------FGSLDEERLERLLDALEEL 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-225 |
7.15e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.60 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 25 VDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVFAldG---GQVILDGRDVS-RLPEHRRATDLGRVFQDPMR-GTAADMQI 99
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKiRNPQQAIAQGIAMVPEDRKRdGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 100 VENLALAARRGESRGlswGITRDErasyrerlAELDLGLEE--RLTSK-------VGLLSGGQRQALTLLMAILKKPKLL 170
Cdd:PRK13549 359 GKNITLAALDRFTGG---SRIDDA--------AELKTILESiqRLKVKtaspelaIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2506233547 171 LLDEHTAALDPKTASKVLALTERLVGEhGLTTLMVTHNMNDAIRLGNRLIMMHEG 225
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-209 |
7.18e-03 |
|
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: 36.96 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 30 EPGDFVTVIGGNGAGKSTLLNSIAGVFALDGGQvILDGRDVSRLPEHRRATDLGRVFQDPMRGTAADMQIVENLAL--AA 107
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLipKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506233547 108 RRGESRGLswgITR-DERASYRERLAELDL-GLEERltsKVGLLSGGQRQALTLLMAILKKPKLLLLDEHTAALDPKTAS 185
Cdd:cd03236 103 VKGKVGEL---LKKkDERGKLDELVDQLELrHVLDR---NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|....
gi 2506233547 186 KVLALTERLVgEHGLTTLMVTHNM 209
Cdd:cd03236 177 NAARLIRELA-EDDNYVLVVEHDL 199
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-56 |
7.63e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 7.63e-03
10 20 30
....*....|....*....|....*....|...
gi 2506233547 24 GVDLHLEPGDFVTVIGGNGAGKSTLLNSIAGVF 56
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
|