|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-335 |
4.92e-177 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 494.21 E-value: 4.92e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAM 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTPM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 241 NLIPGELVG-------------------LEPSVIWGARPEYLGYSAEAvDGGLHGVVSTVEHLGATSLVTVEADGFNLSV 301
Cdd:COG3839 240 NLLPGTVEGggvrlggvrlplpaalaaaAGGEVTLGIRPEHLRLADEG-DGGLEATVEVVEPLGSETLVHVRLGGQELVA 318
|
330 340 350
....*....|....*....|....*....|....
gi 2068383214 302 TVPEADEPSVGSDGWVIPQPGRVLLYDAESGRLL 335
Cdd:COG3839 319 RVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-329 |
1.89e-157 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 444.54 E-value: 1.89e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAM 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTpm 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEA-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 241 NLIPGELVGLEP----------------------SVIWGARPEYLGYSAEAVDGGLHGVVSTVEHLGATSLVTVE-ADGF 297
Cdd:COG3842 240 NLLPGTVLGDEGggvrtggrtlevpadaglaaggPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRlGDGQ 319
|
330 340 350
....*....|....*....|....*....|....
gi 2068383214 298 NLSVTVP--EADEPSVGSDGWVIPQPGRVLLYDA 329
Cdd:COG3842 320 ELVVRVPnrAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-333 |
6.10e-136 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 390.36 E-value: 6.10e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTPM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 241 NLIPGEL----VGLEPS------------------VIWGARPEYLGYSAEAvdGGLHGVVSTVEHLGATSLVTVEADGFN 298
Cdd:PRK11650 241 NLLDGRVsadgAAFELAggialplgggyrqyagrkLTLGIRPEHIALSSAE--GGVPLTVDTVELLGADNLAHGRWGGQP 318
|
330 340 350
....*....|....*....|....*....|....*
gi 2068383214 299 LSVTVPEADEPSVGSDGWVIPQPGRVLLYDAESGR 333
Cdd:PRK11650 319 LVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGR 353
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-326 |
5.05e-122 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 354.45 E-value: 5.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDV-TRLSPGRRDVAMVF 82
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 163 SNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTpmNL 242
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV--NV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 243 IPGELVG----------------LEPSVIWGARPEYLGYSAEAVD-GGLHGVVSTVEHLGATSLVTVEADGFN---LSVT 302
Cdd:COG1118 240 LRGRVIGgqleadgltlpvaeplPDGPAVAGVRPHDIEVSREPEGeNTFPATVARVSELGPEVRVELKLEDGEgqpLEAE 319
|
330 340
....*....|....*....|....*...
gi 2068383214 303 VPEAD----EPSVGSDGWVIPQPGRVLL 326
Cdd:COG1118 320 VTKEAwaelGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
2.13e-113 |
|
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: 328.43 E-value: 2.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
2.49e-113 |
|
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: 327.29 E-value: 2.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLD 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-215 |
6.37e-112 |
|
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: 323.70 E-value: 6.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQ 215
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-296 |
8.39e-110 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 323.53 E-value: 8.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGStpM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--V 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 241 NLIPGE-------LVG-----LEPSVIWGA-------RPEYLGYSAEAV-DGGLHGVVSTVEHLGATSLVTVEADG 296
Cdd:TIGR03265 239 NWLPGTrgggsraRVGgltlaCAPGLAQPGasvrlavRPEDIRVSPAGNaANLLLARVEDMEFLGAFYRLRLRLEG 314
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-237 |
5.01e-100 |
|
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: 294.63 E-value: 5.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQL----SLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGS 237
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-236 |
6.03e-100 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 299.17 E-value: 6.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVEL---TKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVF 82
Cdd:PRK09452 14 LVELrgiSKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 163 SNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIG 236
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-293 |
4.01e-98 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 294.21 E-value: 4.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR-----LSP 73
Cdd:NF040933 1 VTVRVENVTKIFKkgkKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 GRRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRP 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 154 KVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVAN 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 234 FIGStpMNLIPGELVG------------------LEPSVIWGARPE--YLGYSAEAVDGGL----HGVVSTVEHLGATSL 289
Cdd:NF040933 241 LIGD--INLLEGKVEEeglvdgndlkiplpnpklEAGEVIIGIRPEdiDISESDMRLPPGFvevgKGRVKVSSYAGGVFR 318
|
....
gi 2068383214 290 VTVE 293
Cdd:NF040933 319 VVVS 322
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-330 |
1.47e-96 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 290.08 E-value: 1.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVEL---TKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRD 77
Cdd:PRK11432 1 MTQKNFVVLkniTKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIAYPLKVRG---TDRRTRAAKATETGDqlsLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGvpkEERKQRVKEALELVD---LAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANF 234
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 235 IGSTpmNLIPGELVG--------------------LEPSVIWGARPEYLGYSAEAVDGGlHGVVSTVEHLGATSLVTVEA 294
Cdd:PRK11432 237 MGDA--NIFPATLSGdyvdiygyrlprpaafafnlPDGECTVGVRPEAITLSEQGEESQ-RCTIKHVAYMGPQYEVTVDW 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 2068383214 295 DGFNLSVTV-PEADEPSVGSDGWVIPQP-GRVLLYDAE 330
Cdd:PRK11432 314 HGQELLLQVnATQLQPDLGEHYYLEIHPyGMFLLADAA 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-312 |
1.36e-95 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 288.08 E-value: 1.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAM 80
Cdd:PRK11000 1 MASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTPM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 241 NLIPGELVGLEPS----------VIW----------------GARPEYLgYSAEAVDGGLHGVVSTVEHLGATSLVTVEA 294
Cdd:PRK11000 240 NFLPVKVTATAIEqvqvelpnrqQVWlpvegrgvqvganmslGIRPEHL-LPSDIADVTLEGEVQVVEQLGNETQIHIQI 318
|
330 340
....*....|....*....|....*.
gi 2068383214 295 DGF--------NLSVTVPEADEPSVG 312
Cdd:PRK11000 319 PAIrqnlvyrqNDVVLVEEGATFAIG 344
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-232 |
8.88e-95 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 281.98 E-value: 8.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPgrrD 77
Cdd:COG1116 5 APALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 158 FDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSD--GRIRQ-----LDTAREVFRRPADTF 230
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEeidvdLPRPRDRELRTSPEF 241
|
..
gi 2068383214 231 VA 232
Cdd:COG1116 242 AA 243
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-236 |
4.92e-93 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 276.68 E-value: 4.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:TIGR00968 1 IEIANISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:TIGR00968 80 HYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIG 236
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-295 |
2.62e-90 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 273.22 E-value: 2.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 35 LLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAK 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 115 ATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 195 QAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTPM-----------NLIPGELVGLEPSVIWGA----- 258
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVfeatvierkseQVVLAGVEGRRCDIYTDVpvekd 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2068383214 259 -------RPEYLGYSAEAVDGGLHGVVSTVEH---LGATSLVTVEAD 295
Cdd:TIGR01187 241 qplhvvlRPEKIVIEEEDEANSSNAIIGHVIDityLGMTLEVHVRLE 287
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-292 |
3.03e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 271.18 E-value: 3.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHMSVVDNIAY 99
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKK 179
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 180 LQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTpmNLIPGE--------LVGLE 251
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGVaekggegtILDTG 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 252 PSVIW-----------GARPEYLGYSAEAVDGG----LHGVVSTVEHLGATSLVTV 292
Cdd:NF040840 254 NIKIElpeekkgkvriGIRPEDITISTEKVKTSarneFKGKVEEIEDLGPLVKLTL 309
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-237 |
3.21e-89 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 269.65 E-value: 3.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYA 86
Cdd:COG1125 7 VTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelRRRIGYVIQQIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKVRGTDRRTRAAKATETgdqLSLQGL-----MARRPAELSGGQQQRVALARAMACRPKVFLFDEP 161
Cdd:COG1125 87 LFPHMTVAENIATVPRLLGWDKERIRARVDEL---LELVGLdpeeyRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 162 LSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGS 237
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
1.37e-88 |
|
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: 264.72 E-value: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGD---VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPgrrDVAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMS--DGRIRQ 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVA 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-236 |
1.43e-86 |
|
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: 260.35 E-value: 1.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHMSVVDNIAY 99
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKK 179
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 180 LQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIG 236
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-249 |
6.50e-86 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 262.71 E-value: 6.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAA----KATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRERPNAAaikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGStp 239
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE-- 239
|
250
....*....|
gi 2068383214 240 MNLIPGELVG 249
Cdd:PRK10851 240 VNRLQGTIRG 249
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-235 |
1.47e-82 |
|
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: 251.41 E-value: 1.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVAMVFQDYALF 88
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFI 235
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-237 |
1.15e-81 |
|
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: 247.98 E-value: 1.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYA 86
Cdd:cd03295 6 VTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSL--QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSN 164
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 165 LDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGS 237
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
15-235 |
5.61e-81 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 251.18 E-value: 5.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVAMVFQDYALF 88
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMVFQHFALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:COG4175 118 PHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFI 235
Cdd:COG4175 198 IRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
5.34e-80 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 243.03 E-value: 5.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------ 74
Cdd:COG1136 5 LELRNLTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 RRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQaEALALADRIAVMSDGRI 213
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
2.12e-79 |
|
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: 241.24 E-value: 2.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGD---VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRD--- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 ---VAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQaEALALADRIAVMSDGRI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
2.70e-79 |
|
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: 239.40 E-value: 2.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLS----PGRRDVA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDYALFPHMSVVDNIAYPlkvrgtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
1.57e-76 |
|
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: 243.66 E-value: 1.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP----GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG----- 74
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 RRDVAMVFQD--YALFPHMSVVDNIAYPLKVRGT-DRRTRAAKATETGDQLSLQ-GLMARRPAELSGGQQQRVALARAMA 150
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 151 CRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPAD 228
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-248 |
3.19e-76 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 237.28 E-value: 3.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----R 75
Cdd:COG1135 2 IELENLSKTFPtkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETgdqLSLQGLMARR---PAELSGGQQQRVALARAMACR 152
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAEL---LELVGLSDKAdayPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 153 PKVFLFDEPLSNLDAR-----LRLeartfLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:COG1135 159 PKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
250 260
....*....|....*....|.
gi 2068383214 228 DTFVANFIGSTPMNLIPGELV 248
Cdd:COG1135 234 SELTRRFLPTVLNDELPEELL 254
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
4.84e-75 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 231.04 E-value: 4.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIG-------EKDVTRLspgRR 76
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDgedltdsKKDINKL---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 77 DVAMVFQDYALFPHMSVVDNIAY-PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPAD 228
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-247 |
6.20e-75 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 235.50 E-value: 6.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDvTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKvrgTDRRTRAAKATETGDQLSL---QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLK---QDKLPKAEIASRVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDARLRleartflKKLQLE-------LGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVAN 233
Cdd:PRK11607 176 PMGALDKKLR-------DRMQLEvvdilerVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
|
250
....*....|....
gi 2068383214 234 FIGStpMNLIPGEL 247
Cdd:PRK11607 249 FIGS--VNVFEGVL 260
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-235 |
5.97e-73 |
|
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: 225.63 E-value: 5.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDV 78
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDYALFPHMSVVDNIAYPLKVRGT-DRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 158 FDEPLSNLDARLrleARTF---LKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPaDTFVANF 234
Cdd:COG1127 165 YDEPTAGLDPIT---SAVIdelIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240
|
.
gi 2068383214 235 I 235
Cdd:COG1127 241 L 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-239 |
1.97e-72 |
|
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: 224.68 E-value: 1.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDV 78
Cdd:COG1124 2 LEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDY--ALFPHMSVVDNIAYPLKVRG-TDRRTRAAKATEtgdQLSL-QGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGlPDREERIAELLE---QVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANF 234
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
....*
gi 2068383214 235 IGSTP 239
Cdd:COG1124 239 LAASL 243
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-226 |
7.36e-72 |
|
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: 222.59 E-value: 7.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQ--DYALFpHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
9.42e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 219.94 E-value: 9.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVF 82
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 163 SNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:COG1131 160 SGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
3.13e-70 |
|
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: 218.60 E-value: 3.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----R 75
Cdd:cd03258 2 IELKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-213 |
5.24e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 217.61 E-value: 5.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 10 TKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVFQD 84
Cdd:COG2884 8 SKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipylRRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 85 YALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSN 164
Cdd:COG2884 88 FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 165 LDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG2884 168 LDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-213 |
8.58e-70 |
|
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: 216.99 E-value: 8.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----R 75
Cdd:cd03257 2 LEVKNLSVSFPtggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQDY--ALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETgdqLSLQGL------MARRPAELSGGQQQRVALAR 147
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVL---LLLVGVglpeevLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 148 AMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-234 |
9.04e-70 |
|
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: 217.37 E-value: 9.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDV 78
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDYALFPHMSVVDNIAYPLKVRGT-DRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFL 157
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 158 FDEPLSNLD-------ARLrleartfLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREvFRRPADTF 230
Cdd:cd03261 160 YDEPTAGLDpiasgviDDL-------IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LRASDDPL 231
|
....
gi 2068383214 231 VANF 234
Cdd:cd03261 232 VRQF 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-215 |
3.74e-68 |
|
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: 212.54 E-value: 3.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQ---DGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-------GEKDVTrLSPGRRDVAMVFQDYALFP 89
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdSRKKIN-LPPQQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAYPLKVRgtDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:cd03297 89 HLNVRENLAFGLKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQ 215
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
3.71e-67 |
|
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: 209.69 E-value: 3.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG----RRDVA 79
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDYALFPHMSVVDNIAY-PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLF 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 159 DEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-236 |
4.61e-67 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 210.38 E-value: 4.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 24 TFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHMSVVDNIAY---P 100
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLglrP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 101 -LKVRGTDRRTRAAKAtetgDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKK 179
Cdd:COG3840 99 gLKLTAEQRAQVEQAL----ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 180 LQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIG 236
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-236 |
1.20e-66 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 213.56 E-value: 1.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP------GRRDVAMVFQDYALF 88
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIG 236
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-252 |
1.06e-65 |
|
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: 211.11 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 25 FTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDV------TRLSPGRRDVAMVFQDYALFPHMSVVDNIA 98
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRRIGYVFQEARLFPHLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 99 YPLK-VRGTDRRTRAAKATETgdqLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFL 177
Cdd:COG4148 100 YGRKrAPRAERRISFDEVVEL---LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 178 KKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPAdtFVANFIGSTPMNLIPGELVGLEP 252
Cdd:COG4148 177 ERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEAGSVLEATVAAHDP 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-228 |
2.00e-65 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.83 E-value: 2.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVFQ 83
Cdd:COG3638 8 LSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlRRRIGMIFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNI------AYPL------KVRGTDRRtRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMAC 151
Cdd:COG3638 88 QFNLVPRLSVLTNVlagrlgRTSTwrsllgLFPPEDRE-RALEALE---RVGLADKAYQRADQLSGGQQQRVAIARALVQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 152 RPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIrqldtareVFRRPAD 228
Cdd:COG3638 164 EPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGPPA 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-212 |
1.06e-63 |
|
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: 200.77 E-value: 1.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQ--DYALFpH 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFQnpDDQFF-G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:cd03225 91 PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068383214 171 LEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:cd03225 171 RELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.21e-62 |
|
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: 207.45 E-value: 1.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP-GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTG---GQIRIGEKDVTRLSPGRR--D 77
Cdd:COG1123 5 LEVRDLSVRYPgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQD--YALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-238 |
1.33e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 202.34 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPG---DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----R 75
Cdd:PRK11153 2 IELKNISKVFPQggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETgdqLSLQGLMARR---PAELSGGQQQRVALARAMACR 152
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTEL---LELVGLSDKAdryPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 153 PKVFLFDEPLSNLD-----ARLRLeartfLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:PRK11153 159 PKVLLCDEATSALDpattrSILEL-----LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|.
gi 2068383214 228 DTFVANFIGST 238
Cdd:PRK11153 234 HPLTREFIQST 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-227 |
2.62e-62 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 201.11 E-value: 2.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP----------GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP 73
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 G-----RRDVAMVFQD-YA-LFPHMSVVDNIAYPLKVRG-TDRRTRAAKATETgdqLSLQGL----MARRPAELSGGQQQ 141
Cdd:COG4608 88 RelrplRRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAEL---LELVGLrpehADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 142 RVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDqaeaLA----LADRIAVMSDGRIRQLD 217
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIA 240
|
250
....*....|
gi 2068383214 218 TAREVFRRPA 227
Cdd:COG4608 241 PRDELYARPL 250
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-221 |
4.90e-62 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 198.55 E-value: 4.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFPGD---VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTrlSPGRrD 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGA-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFL 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 158 FDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSD--GRIR---QLDTARE 221
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVerlELDFSRR 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-222 |
3.82e-60 |
|
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: 192.77 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVF 82
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 163 SNLDARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
7.40e-60 |
|
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: 194.50 E-value: 7.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP---TGGQIRIGEKDVTRLSPGR-- 75
Cdd:COG0444 2 LEVRNLKVYFPtrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 ----RDVAMVFQD-Y-ALFPHMSVVDNIAYPLKV-RGTDRRTRAAKATETgdqLSLQGL------MARRPAELSGGQQQR 142
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIEL---LERVGLpdperrLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 143 VALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 2068383214 223 FRRPA 227
Cdd:COG0444 239 FENPR 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-213 |
3.33e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 187.99 E-value: 3.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 10 TKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT------RLSpgRRDVAMVFQ 83
Cdd:PRK09493 8 SKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvdeRLI--RQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAY-PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK09493 85 QFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 163 SNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-223 |
8.97e-58 |
|
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: 187.17 E-value: 8.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGR--RDVAMVFQDYALFPHMS 92
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIA---YP-LKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:COG1120 92 VRELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVF 223
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
1.12e-57 |
|
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: 186.23 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTkVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-----ETPTGGQIRIGEKDVTRLSPG---- 74
Cdd:cd03260 1 IELRDLN-VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 RRDVAMVFQDYALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETGdqLSLQGL---MARR--PAELSGGQQQRVALARAM 149
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEA--LRKAALwdeVKDRlhALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 150 ACRPKVFLFDEPLSNLD--ARLRLEARtfLKKLQLElgVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:cd03260 157 ANEPEVLLLDEPTSALDpiSTAKIEEL--IAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-230 |
1.97e-56 |
|
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: 183.15 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDV 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDYALFPHMSVVDNI-----AYPLKVRGTDRR-TRAAK--ATETGDQLSLQGLMARRPAELSGGQQQRVALARAMA 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlGRRSTWRSLFGLfPKEEKqrALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 151 CRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIrqldtareVFRRPADTF 230
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGPPAEL 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-235 |
1.59e-55 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 180.98 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-----------GEKDVTRLspgRRDVAMV 81
Cdd:PRK11124 11 FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIREL---RRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDYALFPHMSVVDN-IAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK11124 88 FQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTArEVFRRPADTFVANFI 235
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAFKNYL 240
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-213 |
2.31e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 179.63 E-value: 2.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPhMSVVDNI 97
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewRRQVAYVPQEPALWG-GTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AYPLKVRgtDRRTRAAKATETGDQLSLQ-GLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTF 176
Cdd:COG4619 95 PFPFQLR--ERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 2068383214 177 LKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG4619 173 LREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
3.82e-55 |
|
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: 177.59 E-value: 3.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVF 82
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIayplkvrgtdrrtraakatetgdqlslqglmarrpaELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 163 SNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
6.82e-55 |
|
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: 179.17 E-value: 6.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP-GR---- 75
Cdd:COG4181 9 IELRGLTKTVGtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 -RDVAMVFQDYALFPHMSVVDNIAYPLKVRGtdRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQLDTARE 221
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
8.33e-55 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 178.21 E-value: 8.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVelTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLsPG------ 74
Cdd:TIGR02673 1 MIEFHNV--SKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRL-RGrqlpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 RRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:TIGR02673 78 RRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLeLGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-226 |
9.12e-54 |
|
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: 177.64 E-value: 9.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT-----RLSPGRRDVAMVFQ--DYA 86
Cdd:TIGR04521 15 PFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQfpEHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFpHMSVVDNIAY-P--LKVRGTDRRTRAAKAtetgdqLSLQGL----MARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:TIGR04521 95 LF-EETVYKDIAFgPknLGLSEEEAEERVKEA------LELVGLdeeyLERSPFELSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
1.39e-53 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 176.48 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFPGDvTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIG--EKDVTR-LSPG--- 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGdiTIDTARsLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 ----RRDVAMVFQDYALFPHMSVVDN-IAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAM 149
Cdd:PRK11264 80 irqlRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 150 ACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
18-306 |
1.53e-53 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 179.54 E-value: 1.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDgLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-------GEKDVTrLSPGRRDVAMVFQDYALFPH 90
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdSRKGIF-LPPEKRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLK-VRGTDRRTRAAKATETgdqLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:TIGR02142 90 LSVRGNLRYGMKrARPSERRISFERVIEL---LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPAdtfvanfigstpMNLIPGELVG 249
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD------------LPWLAREDQG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 250 -LEPSVIWGARPEYlGYSAEAVDGGLHGVVSTVEHLGATSLVTVEADGFNLSVTVPEA 306
Cdd:TIGR02142 235 sLIEGVVAEHDQHY-GLTALRLGGGHLWVPENLGPTGARLRLRVPARDVSLALQKPEA 291
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-213 |
1.62e-53 |
|
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: 174.99 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 7 VELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYA 86
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYP----LKVRGTDRRTRAAKATETGdqlsLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:cd03298 81 LFAHLTVEQNVGLGlspgLKLTAEDRQAIEVALARVG----LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 163 SNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-235 |
2.00e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 175.59 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIG-----------EKDVTRLspgRRDVAMV 81
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsqkpsEKAIRLL---RQKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDYALFPHMSVVDN-IAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:COG4161 88 FQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTArEVFRRPADTFVANFI 235
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYL 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-213 |
3.68e-53 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 175.64 E-value: 3.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEkdvTRLSPGRRDVAMVFQDYALF 88
Cdd:PRK11247 18 VSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAypLKVRGtDRRTRAAKATETgdqlslQGLMARR---PAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:PRK11247 94 PWKKVIDNVG--LGLKG-QWRDAALQALAA------VGLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068383214 166 DARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-225 |
3.82e-53 |
|
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: 174.79 E-value: 3.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRD 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNI-----AYPLKVRGTDRR-TRA--AKATETGDQLSLQGLMARRPAELSGGQQQRVALARAM 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLLGRfSEEdkERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 150 ACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI------RQLDTarEVF 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIvfdgapSELDD--EVL 238
|
..
gi 2068383214 224 RR 225
Cdd:TIGR02315 239 RH 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
4.22e-53 |
|
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: 173.75 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLsPG------RRD 77
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGraipylRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFL 157
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 158 FDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-228 |
6.93e-53 |
|
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: 173.81 E-value: 6.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRrdvAMVFQDYALFPHMSVVDNIAY 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR---MVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRGTDRRT--RAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFL 177
Cdd:TIGR01184 78 AVDRVLPDLSKseRRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 178 KKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV-FRRPAD 228
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-225 |
9.21e-52 |
|
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: 172.23 E-value: 9.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPG-DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIG---EKDVTRLSPGRRDVA 79
Cdd:TIGR04520 1 IEVENVSFSYPEsEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDyalfPH-----MSVVDNIAYPLKVRGTDR---RTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMAC 151
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPReemRKRVDEALK---LVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 152 RPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-205 |
1.05e-51 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 169.97 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP---TGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHM 91
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAY--PLKVRGTDRRTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:COG4136 92 SVGENLAFalPPTIGRAQRRARVEQALE---EAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEALAlADRI 205
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRV 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-213 |
1.13e-51 |
|
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: 171.37 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRD 77
Cdd:COG0411 2 DPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIA----------------YPLKVRGTDRRTRAaKATETGDQLSLQGLMARRPAELSGGQQQ 141
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLvaaharlgrgllaallRLPRARREEREARE-RAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 142 RVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
1.34e-51 |
|
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: 169.99 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFP-GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDV-TRLSPGRRDVAMV 81
Cdd:cd03263 1 LQIRNLTKTYKkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 162 LSNLDARLRleaRTFLKKLQLELGVTTV-FVTHDQAEALALADRIAVMSDGRIRQLDTARE 221
Cdd:cd03263 161 TSGLDPASR---RAIWDLILEVRKGRSIiLTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-216 |
1.56e-51 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 169.66 E-value: 1.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 26 TIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHMSVVDNIAYPLKVRG 105
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 106 TDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELG 185
Cdd:TIGR01277 100 KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQ 179
|
170 180 190
....*....|....*....|....*....|.
gi 2068383214 186 VTTVFVTHDQAEALALADRIAVMSDGRIRQL 216
Cdd:TIGR01277 180 RTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-227 |
1.62e-51 |
|
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: 170.31 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRDVAMVFQDY 85
Cdd:cd03219 6 LTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 86 ALFPHMSVVDNI-----------AYPLKVRGTDRRTRaAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:cd03219 85 RLFPELTVLENVmvaaqartgsgLLLARARREEREAR-ERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
19-213 |
6.89e-51 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 168.36 E-value: 6.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVAMVFQDYALFPHMS 92
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkiilrRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRGTDRRTRAAKATETgdqLSLQGLMARR---PAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARl 169
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQV---LNLFGIDNRRnhkPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSK- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068383214 170 rlEARTFLKKLQL--ELGVTTVFVTHDQaEALALADRIAVMSDGRI 213
Cdd:NF038007 176 --NARAVLQQLKYinQKGTTIIMVTHSD-EASTYGNRIINMKDGKL 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-226 |
1.24e-50 |
|
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: 176.03 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLEtPTGGQIRIGEKDVTRLS-----PGRRDVAMVFQD-YA- 86
Cdd:COG4172 296 VGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpFGs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKV--RGTDRRTRAAKATETGDQLSLQ-GLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:COG4172 375 LSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-213 |
1.25e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 169.10 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVFQDY--ALFPH 90
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafRRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLK-VRGTDRRTRAAKATETGDQLSLQ-GLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-213 |
3.01e-50 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 167.07 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 24 TFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDYALFPHMSVVDNIA---YP 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGlglNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 101 -LKVRGTDRRTRAAKAtetgDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKK 179
Cdd:PRK10771 99 gLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|....
gi 2068383214 180 LQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-235 |
8.55e-50 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 166.75 E-value: 8.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTkVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL--ETP---TGGQIRIGEKDVtrLSPG---- 74
Cdd:COG1117 12 IEVRNLN-VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDI--YDPDvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 --RRDVAMVFQDYALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETgdqlSLQG----------LmaRRPA-ELSGGQQQ 141
Cdd:COG1117 89 elRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEE----SLRKaalwdevkdrL--KKSAlGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 142 RVALARAMACRPKVFLFDEPLSNLD--ARLRLEArtflkkLQLELG--VTTVFVTHDQAEALALADRIAVMSDGRIRQLD 217
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDpiSTAKIEE------LILELKkdYTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|....*...
gi 2068383214 218 TAREVFRRPADTFVANFI 235
Cdd:COG1117 236 PTEQIFTNPKDKRTEDYI 253
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-227 |
2.76e-49 |
|
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: 165.75 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVFQDY--ALFPH 90
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLK-VRGTDRRTRAAKATETGDQLSLQG-LMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI-RQLDTAREV-FRRPA 227
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDVAQLLsFKHPA 245
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.76e-48 |
|
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: 159.74 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHMSVVDNI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARR----PAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-237 |
2.35e-48 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 163.08 E-value: 2.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEK--------------DV 68
Cdd:TIGR03005 1 VRFSDVTKRF-GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQlyhmpgrngplvpaDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 69 TRLSPGRRDVAMVFQDYALFPHMSVVDNIAY-PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALAR 147
Cdd:TIGR03005 80 KHLRQMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 148 AMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239
|
250
....*....|
gi 2068383214 228 DTFVANFIGS 237
Cdd:TIGR03005 240 EERTREFLSK 249
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
3.34e-48 |
|
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: 159.33 E-value: 3.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP--GRRDVAMVFQ 83
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 dyalfphmsvvdniayplkvrgtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 164 NLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-227 |
5.74e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.41 E-value: 5.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlspGRRDVAMVFQDYAL---FPhM 91
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYVPQRAEVdwdFP-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIA---YP----LKVRGTDRRTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSN 164
Cdd:COG1121 93 TVRDVVLmgrYGrrglFRRPSRADREAVDEALE---RVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 165 LDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQlDTAREVFRRPA 227
Cdd:COG1121 170 VDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-225 |
8.83e-48 |
|
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: 170.79 E-value: 8.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpHM 91
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslRRQIGVVLQDVFLF-SG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAYPLKVRGTDRRTRAAKATETGD-----QLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:COG2274 564 TIRENITLGDPDATDEEIIEAARLAGLHDfiealPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 167 ARlrlEARTFLKKL-QLELGVTTVFVTHDqAEALALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:COG2274 644 AE---TEAIILENLrRLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-213 |
2.06e-47 |
|
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: 157.98 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP--GRRDVAMVFQdyALfphms 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkeLARKIAYVPQ--AL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 vvdniayplkvrgtdrrtraakatetgDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLE 172
Cdd:cd03214 83 ---------------------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068383214 173 ARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-226 |
2.90e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 160.35 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIG------------------E 65
Cdd:COG4598 9 LEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkpdrdgelvpadR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 66 KDVTRLspgRRDVAMVFQDYALFPHMSVVDN-IAYPLKVRGTDRrtraAKATETGDQLsLQ--GLMARR---PAELSGGQ 139
Cdd:COG4598 88 RQLQRI---RTRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPK----AEAIERAEAL-LAkvGLADKRdayPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 140 QQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTA 219
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
....*..
gi 2068383214 220 REVFRRP 226
Cdd:COG4598 239 AEVFGNP 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-234 |
6.37e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 163.28 E-value: 6.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 24 TFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVAMVFQDYALFPHMSVVDNI 97
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFL 177
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 178 KKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANF 234
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
7-235 |
9.63e-47 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 158.61 E-value: 9.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 7 VELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-----ETPTGGQIRIGEKDVTrlSPG------R 75
Cdd:TIGR00972 4 IENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIY--DKKidvvelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQDYALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETgdqlSLQGL---------MARRPAELSGGQQQRVALA 146
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEE----SLKKAalwdevkdrLHDSALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 147 RAMACRPKVFLFDEPLSNLD--ARLRLEARTFlkklQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDpiATGKIEELIQ----ELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFT 232
|
250
....*....|.
gi 2068383214 225 RPADTFVANFI 235
Cdd:TIGR00972 233 NPKEKRTEDYI 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-212 |
1.56e-46 |
|
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: 155.23 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpHM 91
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAYVPQDPFLF-SG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIayplkvrgtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDArlRL 171
Cdd:cd03228 91 TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP--ET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068383214 172 EARTFLKKLQLELGVTTVFVTHDqAEALALADRIAVMSDGR 212
Cdd:cd03228 132 EALILEALRALAKGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-213 |
3.71e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 163.27 E-value: 3.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQDY 85
Cdd:COG1129 10 ISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqAAGIAIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 86 ALFPHMSVVDNIA---YPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:COG1129 89 NLVPNLSVAENIFlgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 163 SNLDARlrlEARTFLK---KLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG1129 169 ASLTER---EVERLFRiirRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.01e-45 |
|
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: 154.84 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVF 82
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 163 SNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTARE 221
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-225 |
3.76e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 154.47 E-value: 3.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTrlSPGRrDVAMVFQDYALFPHMSVVDNIA 98
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGA-ERGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 99 YPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLK 178
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 179 KLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:PRK11248 173 KLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFAR 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-205 |
4.43e-45 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 152.77 E-value: 4.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVA 79
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskfrREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEAlALADRI 205
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA-KQADRV 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-200 |
3.96e-44 |
|
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: 150.32 E-value: 3.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAM 80
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGtdRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068383214 161 PLSNLDArlrlEARTFLKKL---QLELGVTTVFVTHDQAEALA 200
Cdd:COG4133 158 PFTALDA----AGVALLAELiaaHLARGGAVLLTTHQPLELAA 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-224 |
4.09e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 152.89 E-value: 4.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVF----PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT----RLSPGR 75
Cdd:PRK13637 3 IKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQ--DYALFPHmSVVDNIAYPLKVRG---TDRRTRAAKATET-GdqLSLQGLMARRPAELSGGQQQRVALARAM 149
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGlseEEIENRVKRAMNIvG--LDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 150 ACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
5.25e-44 |
|
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: 148.73 E-value: 5.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAM 80
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQdyalfphmsvvdniayplkvrgtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 161 PLSNLDARlrlEARTF---LKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03216 109 PTAALTPA---EVERLfkvIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-226 |
1.03e-43 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 152.94 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVFQD--YA 86
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewravRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKV------RGTDRRTRAAKATETGdqlSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTyhpklsRQEVKDRVKAMMLKVG---LLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-222 |
1.75e-43 |
|
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: 149.12 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRDVAMVFQDYALFPHM 91
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNiaypLKVRGTDRRTRAAKATEtgDQL-----SLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:cd03224 91 TVEEN----LLLGAYARRRAKRKARL--ERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 167 ARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:cd03224 165 PKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
2.13e-43 |
|
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: 149.06 E-value: 2.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVF---PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlSP--GRRDV 78
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPaeARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLF 158
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 159 DEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIR 214
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-239 |
7.26e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 150.89 E-value: 7.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVFQD-YA- 86
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKVRGT-DRRTRAAKATETGDQLSLQGLMARR-PAELSGGQQQRVALARAMACRPKVFLFDEPLSN 164
Cdd:PRK11308 105 LNPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 165 LDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTP 239
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATP 259
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-225 |
1.25e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 148.62 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVT-ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKdvtRLSPG-----RRD 77
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEEtvwdvRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDY-ALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVF 156
Cdd:PRK13635 83 VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 157 LFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-228 |
8.71e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 146.70 E-value: 8.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT------RLSPGRRDVAMVFQ--DYALFPH 90
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 mSVVDNIAY-PLK--VRGTDRRTRAAKAtetgdqLSLQGL----MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:PRK13634 102 -TVEKDICFgPMNfgVSEEDAKQKAREM------IELVGLpeelLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPAD 228
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-227 |
1.91e-41 |
|
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: 144.35 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRDVAMVFQDYALFPHM 91
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNI---AYPLKVRGTDRRTRAA--------KAtetgdqlslqglMARRPA-ELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:COG0410 94 TVEENLllgAYARRDRAEVRADLERvyelfprlKE------------RRRQRAgTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-213 |
2.01e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpHM 91
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslRRQIGVVPQDTFLF-SG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAYplkvrGTDRRT--------RAAKATETGDQLSlQGLMAR---RPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:COG1132 429 TIRENIRY-----GRPDATdeeveeaaKAAQAHEFIEALP-DGYDTVvgeRGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 161 PLSNLDArlRLEARTF--LKKLqLElGVTTVFVTHdQAEALALADRIAVMSDGRI 213
Cdd:COG1132 503 ATSALDT--ETEALIQeaLERL-MK-GRTTIVIAH-RLSTIRNADRILVLDDGRI 552
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-208 |
7.39e-41 |
|
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: 142.29 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlspGRRDVAMVFQDYAL---FPhM 91
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRSIdrdFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAYPL--KVRGTDRRTRA--AKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:cd03235 86 SVRDVVLMGLygHKGLFRRLSKAdkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068383214 168 RLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVM 208
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
1.46e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.71 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSpgRRDVAmvfq 83
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED--RRRIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 dY-----ALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLF 158
Cdd:COG4152 75 -YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 159 DEPLSNLDArlrlEARTFLKKLQLEL---GVTTVFVTH--DQAEalALADRIAVMSDGRIR---QLDTAREVFRR 225
Cdd:COG4152 154 DEPFSGLDP----VNVELLKDVIRELaakGTTVIFSSHqmELVE--ELCDRIVIINKGRKVlsgSVDEIRRQFGR 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
20-214 |
3.07e-40 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 140.92 E-value: 3.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI--------GEKDVTRLspgRRDVAMVFQDYALFPHM 91
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVlgqelhgaSKKQLVQL---RRRIGYIFQAHNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAYPLKV-RGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:TIGR02982 98 TARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068383214 171 LEARTFLKKLQLELGVTTVFVTHDQaEALALADRIAVMSDGRIR 214
Cdd:TIGR02982 178 RDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKLL 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-227 |
4.80e-40 |
|
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: 147.52 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKS----TLLRTIAGLETPTGGQIRIGEKDVTRLSPGR------RDVAMVFQD 84
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 85 --YALFPHMSVVDNIAYPLKV-RGTDRRTRAAKATETgdqLSLQGL------MARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALEL---LERVGIpdperrLDAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDqaeaLAL----ADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-213 |
6.94e-40 |
|
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: 138.12 E-value: 6.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSVVDNI 97
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 ayplkvrgtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDA---RLRLEAr 174
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegeRALNQA- 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 2068383214 175 tfLKKLQLElGVTTVFVTHdQAEALALADRIAVMSDGRI 213
Cdd:cd03246 139 --IAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-221 |
7.31e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 147.21 E-value: 7.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAM 80
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFpHMSVVDNIAypLKVRGTDRRT-----RAAKATETGDQLSlQGLMAR---RPAELSGGQQQRVALARAMACR 152
Cdd:COG4988 416 VPQNPYLF-AGTIRENLR--LGRPDASDEEleaalEAAGLDEFVAALP-DGLDTPlgeGGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 153 PKVFLFDEPLSNLDARLRLEARTFLKKLQleLGVTTVFVTHDQAeALALADRIAVMSDGRIRQLDTARE 221
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLA-LLAQADRILVLDDGRIVEQGTHEE 557
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-212 |
7.94e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.33 E-value: 7.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAM 80
Cdd:COG3845 6 LELRGITKRFGG-VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAY---PLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFL 157
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 158 FDEPLSNLDARlrlEARTF---LKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:COG3845 165 LDEPTAVLTPQ---EADELfeiLRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-226 |
8.69e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 140.74 E-value: 8.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVF--------PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEKdvtrL 71
Cdd:COG4167 2 SALLEVRNLSKTFkyrtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILInGHK----L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 72 SPG----R-RDVAMVFQD--YALFPHMSVVDNIAYPLKvRGTD--RRTRAAKATETgdqLSLQGLMAR----RPAELSGG 138
Cdd:COG4167 78 EYGdykyRcKHIRMIFQDpnTSLNPRLNIGQILEEPLR-LNTDltAEEREERIFAT---LRLVGLLPEhanfYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 139 QQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDT 218
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
....*...
gi 2068383214 219 AREVFRRP 226
Cdd:COG4167 234 TAEVFANP 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-213 |
1.20e-39 |
|
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: 138.54 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlSPGRRDVAMVFQD--YALFPH 90
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQDvdYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 mSVVDNIAYPLKvRGTDRRTRAAKATETgdqLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR-L 169
Cdd:cd03226 88 -SVREELLLGLK-ELDAGNEQAETVLKD---LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068383214 170 RLEARTFlKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03226 163 ERVGELI-RELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
7.96e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 138.29 E-value: 7.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVF----PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRR--D 77
Cdd:COG1101 2 LELKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYAL--FPHMSVVDNIAYPL---KVRGTDRRTRAAKATETGDQLSLQGL-----MARRPAELSGGQQQrvALAR 147
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRRELFRELLATLGLglenrLDTKVGLLSGGQRQ--ALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 148 AMAC--RPKVFLFDEPLSNLD---ARLRLEArTflKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG1101 160 LMATltKPKLLLLDEHTAALDpktAALVLEL-T--EKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-228 |
8.96e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 138.71 E-value: 8.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekDVTRLSPG-----RRDVAMVFQDY-ALFPHMSV 93
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEEnvwdiRHKIGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEA 173
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 174 RTFLKKLQLELGVTTVFVTHDQAEaLALADRIAVMSDGRIRQLDTAREVFRRPAD 228
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-215 |
1.35e-38 |
|
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: 136.17 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVtALDGLTFTIQDGeFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 163 SNLDARLRLEARTFLKklQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQ 215
Cdd:cd03264 159 AGLDPEERIRFRNLLS--ELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-213 |
1.77e-38 |
|
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: 136.18 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 7 VELTKV---FPGDVT-ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAM 80
Cdd:cd03245 3 IEFRNVsfsYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFpHMSVVDNIAYPLKVRGTDRRTRAAKATETGD--QLSLQGL---MARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLADDERILRAAELAGVTDfvNKHPNGLdlqIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 156 FLFDEPLSNLDarLRLEARtFLKKLQLEL-GVTTVFVTHDQAeALALADRIAVMSDGRI 213
Cdd:cd03245 162 LLLDEPTSAMD--MNSEER-LKERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-213 |
2.00e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 136.16 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 8 ELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-----RRDVAMVF 82
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGT---DRRTRAAKATetgDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGAsgdDIRRRVSAAL---DKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-214 |
3.64e-38 |
|
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: 135.10 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLspGRRDVAMVFQ 83
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--ARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 164 NLDArlrLEARTFLKKL--QLELGVTTVFVTHDQAEALALADRIAVMSDGRIR 214
Cdd:cd03269 158 GLDP---VNVELLKDVIreLARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-213 |
3.90e-38 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 143.85 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVT-ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFp 89
Cdd:TIGR03375 473 YPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAypLKVRGTDRRT--RAAKATETGD--QLSLQGL---MARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:TIGR03375 552 YGTLRDNIA--LGAPYADDEEilRAAELAGVTEfvRRHPDGLdmqIGERGRSLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 163 SNLDArlRLEARtFLKKLQLEL-GVTTVFVTHDQAeALALADRIAVMSDGRI 213
Cdd:TIGR03375 630 SAMDN--RSEER-FKDRLKRWLaGKTLVLVTHRTS-LLDLVDRIIVMDNGRI 677
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-214 |
1.86e-37 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 133.11 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNiaypLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd03268 80 APGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 164 NLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIR 214
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
3.59e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 133.81 E-value: 3.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELtKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-----ETPTGGQIRIGEKDVtrLSPG---- 74
Cdd:PRK14267 5 IETVNL-RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 --RRDVAMVFQDYALFPHMSVVDNIAYPLKVRG-------TDRRTRAA--KAT---ETGDQLSlqglmaRRPAELSGGQQ 140
Cdd:PRK14267 82 evRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvkskkeLDERVEWAlkKAAlwdEVKDRLN------DYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 141 QRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELgvTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAR 220
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
....*.
gi 2068383214 221 EVFRRP 226
Cdd:PRK14267 234 KVFENP 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-225 |
6.23e-37 |
|
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: 139.11 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFPG-DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGR--RDV 78
Cdd:COG4618 329 GRLSVENLTVVPPGsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDYALFPHmSVVDNIAY-----PLKVrgtdrrTRAAKA---------------TETGDQLSLqglmarrpaeLSGG 138
Cdd:COG4618 409 GYLPQDVELFDG-TIAENIARfgdadPEKV------VAAAKLagvhemilrlpdgydTRIGEGGAR----------LSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 139 QQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAeALALADRIAVMSDGRIRQLDT 218
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGP 549
|
....*..
gi 2068383214 219 AREVFRR 225
Cdd:COG4618 550 RDEVLAR 556
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
2.49e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR--LSPGRRDVAMVFQ--DYAlFPHMSVV 94
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQnpDNQ-FIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 DNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEAR 174
Cdd:PRK13632 103 DDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 175 TFLKKLQLELGVTTVFVTHDQAEALaLADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK13632 183 KIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-227 |
2.70e-36 |
|
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: 137.59 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpHM 91
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlRRRIAVVPQRPHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDN--IAYPlkvRGTDRRTRAAKatetgDQLSLQGLMARRP-----------AELSGGQQQRVALARAMACRPKVFLF 158
Cdd:COG4987 424 TLRENlrLARP---DATDEELWAAL-----ERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 159 DEPLSNLDArlrLEARTFLKKLqLEL--GVTTVFVTHDQAeALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:COG4987 496 DEPTEGLDA---ATEQALLADL-LEAlaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-235 |
2.72e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.63 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT--RLSPGRRDVA- 79
Cdd:PRK10619 5 KLNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvRDKDGQLKVAd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 ------------MVFQDYALFPHMSVVDNI-AYPLKVRG---TDRRTRAAK-ATETGDQLSLQGlmaRRPAELSGGQQQR 142
Cdd:PRK10619 84 knqlrllrtrltMVFQHFNLWSHMTVLENVmEAPIQVLGlskQEARERAVKyLAKVGIDERAQG---KYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 143 VALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
250
....*....|...
gi 2068383214 223 FRRPADTFVANFI 235
Cdd:PRK10619 240 FGNPQSPRLQQFL 252
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-235 |
3.61e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 131.32 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 5 DVVELTKVF--PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL------ETPTGGQIRIGEKDVTRLSP--G 74
Cdd:PRK14246 9 DVFNISRLYlyINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAikL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 75 RRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATEtgDQLSLQGLMAR------RPA-ELSGGQQQRVALAR 147
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVE--ECLRKVGLWKEvydrlnSPAsQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 148 AMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElgVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
....*...
gi 2068383214 228 DTFVANFI 235
Cdd:PRK14246 245 NELTEKYV 252
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-213 |
1.78e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 136.01 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVAMVFQDYALF 88
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlrREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068383214 169 LRLEARTFLKKLQlELGVTTVFVTHDQAEAlALADRIAVMSDGRI 213
Cdd:PRK10535 179 SGEEVMAILHQLR-DRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-215 |
2.77e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.39 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG------RRDVAMVFQDYALFPHMSV 93
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAKATEtgdQLSLQGLMAR---RPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALE---MLAAVGLEHRanhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068383214 171 LEARTFLKKLQLELGVTTVFVTHDqaeaLALADRIA---VMSDGRIRQ 215
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMSrqlEMRDGRLTA 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-226 |
2.91e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 128.69 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG----RRdvAMVFQDYAL-FP 89
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRR--AVLPQHSSLaFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 hMSVVDNIA---YPLKVRGTDRRTRAAKATETGDqlsLQGLMARRPAELSGGQQQRVALARAMA-------CRPKVFLFD 159
Cdd:COG4559 90 -FTVEEVVAlgrAPHGSSAAQDRQIVREALALVG---LAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 160 EPLSNLD-----ARLRLeARTFLKKlqlelGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:COG4559 166 EPTSALDlahqhAVLRL-ARQLARR-----GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-227 |
3.23e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.15 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 34 ALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEK---DVTR---LSPGRRDVAMVFQDYALFPHMSVVDNIAYPLKvrgtd 107
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 108 rRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVT 187
Cdd:PRK11144 103 -KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068383214 188 TVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
9.83e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 127.34 E-value: 9.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-----ETPTGGQIRIGEKDVTR--LSP 73
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKmdVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 GRRDVAMVFQDYALFPHMSVVDNIAYPLKV-------RGTDRRTRAA--KAT---ETGDQLSLQGlmarrpAELSGGQQQ 141
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLnrlvkskKELQERVRWAleKAQlwdEVKDRLDAPA------GKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 142 RVALARAMACRPKVFLFDEPLSNLDArlrlEARTFLKKLQLELG--VTTVFVTHDQAEALALADRIAVMSDGRIRQLDTA 219
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDP----ENTAKIESLFLELKkdMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
....*..
gi 2068383214 220 REVFRRP 226
Cdd:PRK14247 230 REVFTNP 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-213 |
1.04e-34 |
|
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: 126.49 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 12 VFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRDVAMVFQDYALF 88
Cdd:TIGR03410 8 VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPherARAGIAYVPQGREIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGTDRRTRAAKATEtgdqL--SLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:TIGR03410 88 PRLTVEENLLTGLAALPRRSRKIPDEIYE----LfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 167 ARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-213 |
2.24e-34 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 124.08 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQD---YALFPHMS 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAyplkvrgtdrrtraakatetgdqLSLQglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDarlrLE 172
Cdd:cd03215 95 VAENIA-----------------------LSSL---------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068383214 173 ARTFLKKLQLEL---GVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03215 139 AKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-215 |
2.43e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 125.66 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTK-VFPGD--VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRR---- 76
Cdd:PRK10584 7 VEVHHLKKsVGQGEheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 77 --DVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:PRK10584 87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQ 215
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-227 |
3.27e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 125.35 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRR---DVAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
4.80e-34 |
|
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: 130.69 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTK----VFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQ--IRIGEK--DVTRLSP-- 73
Cdd:TIGR03269 280 IKVRNVSKryisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 -GR--RDVAMVFQDYALFPHMSVVDNIA-----------------YPLKVRGTDRRtraaKATEtgdqlslqgLMARRPA 133
Cdd:TIGR03269 360 rGRakRYIGILHQEYDLYPHRTVLDNLTeaiglelpdelarmkavITLKMVGFDEE----KAEE---------ILDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 134 ELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|.
gi 2068383214 214 RQLDTAREVFR 224
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-205 |
8.56e-34 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 124.06 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmS 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRGtdRRTRAAKATETGDQLSL-QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRL 171
Cdd:PRK10247 97 VYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....
gi 2068383214 172 EARTFLKKLQLELGVTTVFVTHDQAEaLALADRI 205
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE-INHADKV 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-224 |
1.16e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.50 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG----RRdvAMVFQDYAL-FP 89
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRR--AVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 hMSVVDNIA---YPLKVRGTDRRTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMA------CRPKVFLFDE 160
Cdd:PRK13548 91 -FTVEEVVAmgrAPHGLSRAEDDALVAAALA---QVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 161 PLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-235 |
1.18e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.50 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 12 VFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-----ETPTGGQIRIGEKDVtrLSPG------RRDVAM 80
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSPRtdtvdlRKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETgdqlSLQGL---------MARRPAELSGGQQQRVALARAMAC 151
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK----SLKGAsiwdevkdrLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 152 RPKVFLFDEPLSNLD--ARLRLEARTFLKKLQLelgvTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADT 229
Cdd:PRK14239 166 SPKIILLDEPTSALDpiSAGKIEETLLGLKDDY----TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
....*.
gi 2068383214 230 FVANFI 235
Cdd:PRK14239 242 ETEDYI 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.25e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.92 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR--LSPGRRDV 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQ--DYALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVF 156
Cdd:PRK13652 81 GLVFQnpDDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 157 LFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-235 |
1.27e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 124.76 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-----ETPTGGQIR-----IGEKDVTrLSPGRRDVAMVFQDYALFP 89
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEffnqnIYERRVN-LNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 hMSVVDNIAYPLKVRG-------TDRRTRAAKATETGDQLSLQglMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEIKHK--IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 163 SNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVM--SDGRIRQL---DTAREVFRRPADTFVANFI 235
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTKKIFNSPHDSRTREYV 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-240 |
1.52e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.36 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQI-----RIGEKDVTRLSPGRRDVAMVFQD-YA-LF 88
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRIDTLSPGKLQALRRDIQFIFQDpYAsLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGT-DRRTRAAKATETGDQLSLQGLMA-RRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 167 ARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTPM 240
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-221 |
4.18e-33 |
|
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: 122.65 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPhMSV 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAKATETGDQLS-----LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDFIMslpdgYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 169 LRLEARTFLKKLQleLGVTTVFVTHDQAeALALADRIAVMSDGRIRQLDTARE 221
Cdd:cd03249 174 SEKLVQEALDRAM--KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
4.46e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.65 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEK----DVTRLSPGRRDVA 79
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQ--DYALF-PhmSVVDNIAY-PLKVrGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:PRK13639 82 IVFQnpDDQLFaP--TVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-235 |
5.38e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 123.34 E-value: 5.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDV-----TRLSPGRRDVAMVFQDYALFP 89
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAYPLKvRGTD------RRTRAAKATETGdqlsLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:PRK11831 98 DMNVFDNVAYPLR-EHTQlpapllHSTVMMKLEAVG----LRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 164 NLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVfRRPADTFVANFI 235
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPDPRVRQFL 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-208 |
5.88e-33 |
|
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: 127.79 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAM 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHmSVVDNIAYPLKVRGTDRRTRAAKATETGDQLS-----LQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 156 FLFDEPLSNLDArlRLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVM 208
Cdd:TIGR02857 480 LLLDEPTAHLDA--ETEAEVLEALRALAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-213 |
1.74e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.90 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRR---D 77
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLmARRPA-ELSGGQQQRVALARAMACRPKVF 156
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHL-RKSKAySLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 157 LFDEPLSNLDARLRLEARTFLKKL-QLELGvttVFVT-HDQAEALALADRIAVMSDGRI 213
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKV 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-212 |
2.47e-32 |
|
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: 120.23 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFP----GDVT--ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI----GEKDVTRL 71
Cdd:COG4778 3 TLLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 72 SPG------RRDVAMVFQdyalF----PHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSL-QGLMARRPAELSGGQQ 140
Cdd:COG4778 83 SPReilalrRRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 141 QRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-224 |
2.56e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.81 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR------LSPGRRDVAMVFQdyal 87
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 88 FPHM-----SVVDNIAYPLKVRGTDRRTRAAKATETGDQLSL-QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEP 161
Cdd:PRK13646 93 FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 162 LSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-279 |
3.71e-32 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 125.41 E-value: 3.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 10 TKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDV----TR--LSPGrrdVAMVFQ 83
Cdd:PRK11288 11 GKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTaaLAAG---VAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNI---AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK11288 87 ELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 161 PLSNLDAR-----------LRLEARTFLkklqlelgvttvFVTHDQAEALALADRIAVMSDGR-IRQLDTAREVFRrpaD 228
Cdd:PRK11288 167 PTSSLSAReieqlfrvireLRAEGRVIL------------YVSHRMEEIFALCDAITVFKDGRyVATFDDMAQVDR---D 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 229 TFVAnfigstpmnlipgELVGLEPSVIWGARPEYLG---YSAEAVDG-GLHGVVS 279
Cdd:PRK11288 232 QLVQ-------------AMVGREIGDIYGYRPRPLGevrLRLDGLKGpGLREPIS 273
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-222 |
3.97e-32 |
|
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: 125.54 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRdVAMVFQDYALFPH 90
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRetfGKH-IGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 mSVVDNIAyplkvrgtdRRTRAAKATETGDQLSLQG---LMARRP-----------AELSGGQQQRVALARAMACRPKVF 156
Cdd:TIGR01842 407 -TVAENIA---------RFGENADPEKIIEAAKLAGvheLILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 157 LFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHdQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-223 |
8.54e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 8.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGR--RDVAMVFQDYALFPHMS 92
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAY------PLKVR-GTDRRTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:PRK11231 93 VRELVAYgrspwlSLWGRlSAEDNARVNQAME---QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 166 DARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK11231 170 DINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-226 |
1.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 120.32 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT------RLSPGRRDVAMVFQ--DY 85
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 86 ALFPHmSVVDNIAY-PLKVRGTDRRTRAaKATETGDQLSL-QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:PRK13641 97 QLFEN-TVLKDVEFgPKNFGFSEDEAKE-KALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 164 NLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
1.26e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.03 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlSPGR---RDVAM 80
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRelaKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIA---YPLKvRGtdRRTRA--AKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:COG4604 80 LRQENHINSRLTVRELVAfgrFPYS-KG--RLTAEdrEIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-213 |
1.83e-31 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 116.88 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 11 KVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTG--GQIRIGEKDVTRLSPGRRdVAMVFQDYALF 88
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI-IGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:cd03213 95 PTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068383214 169 LRLEARTFLKKLQLElGVTTVFVTHD-QAEALALADRIAVMSDGRI 213
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-225 |
3.33e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.69 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLS------PGRRDVAMVFQdyalFPHM- 91
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 ----SVVDNIAYPLKVRGTDRRTRAAKATEtgdQLSLQG----LMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:PRK13649 98 lfeeTVLKDVAFGPQNFGVSQEEAEALARE---KLALVGisesLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 164 NLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-245 |
3.35e-31 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 119.83 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGgqiRIG------------- 64
Cdd:PRK09473 10 DALLDVKDLRVTFStpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGgsatfngreilnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 65 -EKDVTRLSPgrRDVAMVFQD--YALFPHMSVVDNI--------------AYPLKVRGTDrrtrAAKATETGDQlslqgl 127
Cdd:PRK09473 87 pEKELNKLRA--EQISMIFQDpmTSLNPYMRVGEQLmevlmlhkgmskaeAFEESVRMLD----AVKMPEARKR------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 128 MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAV 207
Cdd:PRK09473 155 MKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2068383214 208 MSDGRIRQLDTAREVFRRPADTFVANFIGSTP--------MNLIPG 245
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPrldaegesLLTIPG 280
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-213 |
5.73e-31 |
|
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: 117.11 E-value: 5.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTK--VFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPT-GGQIRI-GEK----DVTRLspgRRD 77
Cdd:COG1119 3 LLELRNvtVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLfGERrggeDVWEL---RKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMV---FQDYaLFPHMSVVD--------NIAYPLKVRGTDRRtraaKATETGDQLSLQGLMARRPAELSGGQQQRVALA 146
Cdd:COG1119 80 IGLVspaLQLR-FPRDETVLDvvlsgffdSIGLYREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 147 RAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-223 |
5.87e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 5.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQI---RIGEKDVTRLSPGRRDVAMVFQDyalfPHMSVV 94
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdGLDTSDEENLWDIRNKAGMVFQN----PDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 -----DNIAY-P--LKVRGTDRRTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:PRK13633 100 ativeEDVAFgPenLGIPPEEIRERVDESLK---KVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 167 ARLRLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-213 |
2.78e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.72 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVF----PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-------------GE 65
Cdd:PRK13651 2 QIKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkeKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 66 KDVTRLSPG-------------RRDVAMVFQ--DYALFpHMSVVDNIAYPLKVRGTDR---RTRAAKatetgdQLSLQGL 127
Cdd:PRK13651 82 KVLEKLVIQktrfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKeeaKKRAAK------YIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 128 ----MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALAD 203
Cdd:PRK13651 155 desyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTK 233
|
250
....*....|
gi 2068383214 204 RIAVMSDGRI 213
Cdd:PRK13651 234 RTIFFKDGKI 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-239 |
3.25e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.41 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRd 77
Cdd:PRK09536 1 MPMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraaSRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALfphmsvvdniAYPLKVRG------TDRRTRAAKATETGD--------QLSLQGLMARRPAELSGGQQQRV 143
Cdd:PRK09536 79 VASVPQDTSL----------SFEFDVRQvvemgrTPHRSRFDTWTETDRaaverameRTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 144 ALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
250
....*....|....*....
gi 2068383214 224 RRP--ADTFVAN-FIGSTP 239
Cdd:PRK09536 228 TADtlRAAFDARtAVGTDP 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-213 |
3.60e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 119.77 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRD---VAM 80
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLqglmARRPAELSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 161 PLSNLDArlrLEARTFLKKLQ--LELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK15439 167 PTASLTP---AETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-225 |
4.53e-30 |
|
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: 114.63 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR--LSPGRRDVAMVFQDYALFpH 90
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVVPQDTVLF-N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPlKVRGTDRRT-RAAKATETGD-----------QLSLQGLMarrpaeLSGGQQQRVALARAMACRPKVFLF 158
Cdd:cd03253 89 DTIGYNIRYG-RPDATDEEViEAAKAAQIHDkimrfpdgydtIVGERGLK------LSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 159 DEPLSNLDA---RLRLEARTFLKKlqlelGVTTVFVTHDQAEALAlADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:cd03253 162 DEATSALDThteREIQAALRDVSK-----GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-213 |
6.74e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 113.97 E-value: 6.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEKDVTRLSPGRRDVAMVF-QDYALFPHMSV 93
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEA 173
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068383214 174 RTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-227 |
1.41e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.11 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTK---VFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRT-------IAGLETPtgGQIRIGEKDV-- 68
Cdd:PRK14243 4 LNGTETVLRTEnlnVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFRVE--GKVTFHGKNLya 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 69 TRLSPG--RRDVAMVFQDYALFPHmSVVDNIAYPLKVRG--------TDRRTR-AAKATETGDQLSLQGLmarrpaELSG 137
Cdd:PRK14243 82 PDVDPVevRRRIGMVFQKPNPFPK-SIYDNIAYGARINGykgdmdelVERSLRqAALWDEVKDKLKQSGL------SLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 138 GQQQRVALARAMACRPKVFLFDEPLSNLD--ARLRLEartflkKLQLELG--VTTVFVTHDQAEALALADRIAVMS---- 209
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDpiSTLRIE------ELMHELKeqYTIIIVTHNMQQAARVSDMTAFFNvelt 228
|
250 260
....*....|....*....|...
gi 2068383214 210 -----DGRIRQLDTAREVFRRPA 227
Cdd:PRK14243 229 egggrYGYLVEFDRTEKIFNSPQ 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-213 |
1.73e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.81 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQD---YALFPHMS 92
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaiRAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYP-LKVRGT----DRRTRAAKATETGDQLSLQglmARRP----AELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:COG1129 347 IRENITLAsLDRLSRggllDRRRERALAEEYIKRLRIK---TPSPeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 164 NLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-236 |
2.23e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 113.65 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 7 VELTKVFPGDvTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPT-----------GGQIRIGEKDVTRLspgR 75
Cdd:PRK14271 25 VNLTLGFAGK-TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrysgdvllGGRSIFNYRDVLEF---R 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 76 RDVAMVFQDYALFPhMSVVDNI-----AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMA 150
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 151 CRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELgvTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTF 230
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
....*.
gi 2068383214 231 VANFIG 236
Cdd:PRK14271 258 TARYVA 263
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
2.72e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.45 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFpGDVT----ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-ETP---TGGQIRIGEKDVTRLS 72
Cdd:PRK11022 1 MALLNVDKLSVHF-GDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 73 PGRR------DVAMVFQD--YALFPHMSVVDNIAYPLKV-RGTDRRTRAAKATETGDQLSLQGLMAR---RPAELSGGQQ 140
Cdd:PRK11022 80 EKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 141 QRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAR 220
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
....*.
gi 2068383214 221 EVFRRP 226
Cdd:PRK11022 240 DIFRAP 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-213 |
2.83e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.29 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDY--ALFPhMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-212 |
3.00e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 112.78 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLsPG----RRDVAMVFQDYALFPH 90
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGhqiaRMGVVRTFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDN-------------IAYPLKVRGTDRRTRAA--KATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:PRK11300 95 MTVIENllvaqhqqlktglFSGLLKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-229 |
4.52e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 111.69 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP----TGGQIRIGEKDVTRLSPGRRDVAMVFQD--YALFPHMS 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQG---LMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADT 229
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-223 |
5.08e-29 |
|
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: 111.55 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSVVDN 96
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IAYplkvrGTDRRT--------RAAKATETGDQL--SLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:cd03254 97 IRL-----GRPNATdeevieaaKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 167 ARLRLEARTFLKKLQleLGVTTVFVTHdQAEALALADRIAVMSDGRIRQLDTAREVF 223
Cdd:cd03254 172 TETEKLIQEALEKLM--KGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-228 |
5.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekDVTRLSPG-----RRDVAMVFQDY-ALFP 89
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAEnvwnlRRKIGMVFQNPdNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQLDTAREVFRRPAD 228
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-221 |
8.03e-29 |
|
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: 111.17 E-value: 8.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVT-ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT--RLSPGRRDVAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFpHMSVVDNIAYplkvrGTDRRT--------RAAKATETGDQL--SLQGLMARRPAELSGGQQQRVALARAMA 150
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY-----GRPGATreeveeaaRAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 151 CRPKVFLFDEPLSNLDARLRLEARTFLKKLQleLGVTTVFVTHdQAEALALADRIAVMSDGRIRQLDTARE 221
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEE 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-226 |
8.28e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.20 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP--------TGGQIRIGEKDVTRLspgRRDVAMVFQDY-ALFP 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVWDI---REKVGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEAlALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-244 |
1.25e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.64 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVF----PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGE-------------- 65
Cdd:PRK13631 22 LRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 66 -------KDVTRLspgRRDVAMVFQ--DYALFPHmSVVDNIAY---PLKVRGTDRRTRAAKatetgdQLSLQGL----MA 129
Cdd:PRK13631 102 npyskkiKNFKEL---RRRVSMVFQfpEYQLFKD-TIEKDIMFgpvALGVKKSEAKKLAKF------YLNKMGLddsyLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 130 RRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMS 209
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMD 250
|
250 260 270
....*....|....*....|....*....|....*
gi 2068383214 210 DGRIRQLDTAREVFRRPAdtfvanFIGSTPMNLIP 244
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQH------IINSTSIQVPR 279
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-225 |
2.51e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.17 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLspgrrDVAMVFQdyalfPHMSV 93
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH-----PELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNI-----AYPLKVRGTDRRTRAAKA-TETGDQLSLQglmARRpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:COG1134 106 RENIylngrLLGLSRKEIDEKFDEIVEfAELGDFIDQP---VKT---YSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 168 RLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:COG1134 180 AFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-214 |
2.68e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgEKDVTrlspgrrdVAMVFQDYALF 88
Cdd:COG0488 4 LSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR--------IGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKVRGTDRR------TRAAKATETGDQLS---------------------LQGL------MARRPAEL 135
Cdd:COG0488 74 DDLTVLDTVLDGDAELRALEAeleeleAKLAEPDEDLERLAelqeefealggweaearaeeiLSGLgfpeedLDRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 136 SGGQQQRVALARAMACRPKVFLFDEPLSNLD--ARLRLEarTFLKKLQlelgVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEWLE--EFLKNYP----GTVLVVSHDRYFLDRVATRILELDRGKL 227
|
.
gi 2068383214 214 R 214
Cdd:COG0488 228 T 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-213 |
2.78e-28 |
|
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: 109.48 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSV 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAKATETGDQLSL--QGL---MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISElaSGYdteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068383214 169 LRLEARtflKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:cd03248 185 SEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-217 |
3.57e-28 |
|
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: 109.16 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 11 KVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLspgrrDVAMVFQdyalfPH 90
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 171 LEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLD 217
Cdd:cd03220 179 EKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
5.71e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 5.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG----RRDVA 79
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQ--DYALFPhMSVVDNIAY---PLKVRGTDRRTRAAKATE-TGdqlsLQGLMARRPAELSGGQQQRVALARAMACRP 153
Cdd:PRK13636 86 MVFQdpDNQLFS-ASVYQDVSFgavNLKLPEDEVRKRVDNALKrTG----IEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 154 KVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
6.90e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.18 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 17 VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGE-------KDVTRLSPG-----RR----DVAM 80
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQsaaqmRHvrgaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQD--YALFPHMSVVDNIAYPLKV-RGTDRRTRAAKATETGDQLSL---QGLMARRPAELSGGQQQRVALARAMACRPK 154
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 155 VFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANF 234
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRAL 268
|
....*
gi 2068383214 235 IGSTP 239
Cdd:PRK10261 269 LAAVP 273
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-213 |
6.93e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 6.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 17 VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRD--VAMVFQD---YALFPH 90
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPReRRRlgVAYIPEDrlgRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIA------YPLKVRGTDRRTRAAKATETgdqlslqgLMAR---RPA-------ELSGGQQQRVALARAMACRPK 154
Cdd:COG3845 351 MSVAENLIlgryrrPPFSRGGFLDRKAIRAFAEE--------LIEEfdvRTPgpdtparSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 155 VFLFDEPLSNLDARlrleARTFLKKLQLEL---GVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG3845 423 LLIAAQPTRGLDVG----AIEFIHQRLLELrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-224 |
1.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLS------PGRRDVAMVFQ--DYALFPH 90
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 mSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSL-QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 170 RLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:PRK13643 180 RIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-220 |
3.38e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.41 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDvTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLET---PTGGQIRIGEKDVTRLSPGRRDV-- 78
Cdd:PRK09984 5 IRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 -----AMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGL----MA----RRPAELSGGQQQRVAL 145
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALtrvgMVhfahQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 146 ARAMACRPKVFLFDEPLSNLD---ARLRLEArtfLKKLQLELGVTTVFVTHDQAEALALADRIA------VMSDGRIRQL 216
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDpesARIVMDT---LRDINQNDGITVVVTLHQVDYALRYCERIValrqghVFYDGSSQQF 240
|
....
gi 2068383214 217 DTAR 220
Cdd:PRK09984 241 DNER 244
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-208 |
4.41e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGekdvtrlsPGRRdVAMVFQdyalfpHMSVV 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA--------GGAR-VAYVPQ------RSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 DniAYPLKVRGT---------------DRRTRAAkATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:NF040873 68 D--SLPLTVRDLvamgrwarrglwrrlTRDDRAA-VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDqAEALALADRIAVM 208
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-223 |
5.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.79 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 10 TKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGE----------KDVTRLspgRRDVA 79
Cdd:PRK13645 17 AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVKRL---RKEIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQ--DYALFPHmSVVDNIAY-PLKVrGTDRRTRAAKATETGDQLSLQGLMARR-PAELSGGQQQRVALARAMACRPKV 155
Cdd:PRK13645 94 LVFQfpEYQLFQE-TIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 156 FLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-243 |
6.37e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.00 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTKV---FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQI---RIGEKDVTRLSPGRRDVA 79
Cdd:PRK13644 1 MIRLENVsysYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQD-YALFPHMSVVDNIAY--------PLKVRgtdRRTRAAKAtETGdqlsLQGLMARRPAELSGGQQQRVALARAMA 150
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFgpenlclpPIEIR---KRVDRALA-EIG----LEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 151 CRPKVFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDqAEALALADRIAVMSDGRIRQLDTAREVFRRPAdtf 230
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS--- 227
|
250
....*....|...
gi 2068383214 231 vANFIGSTPMNLI 243
Cdd:PRK13644 228 -LQTLGLTPPSLI 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
7.34e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.09 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLeTPTGGQIRIGEKDVTRLSPG--RRDVAMV 81
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPEswRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDYALFpHMSVVDNIAyPLKVRGTDRRTRA----AKATETGDQLSlQGL---MARRPAELSGGQQQRVALARAMACRPK 154
Cdd:PRK11174 429 GQNPQLP-HGTLRDNVL-LGNPDASDEQLQQalenAWVSEFLPLLP-QGLdtpIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 155 VFLFDEPLSNLDA---RLRLEARTflkklQLELGVTTVFVTHdQAEALALADRIAVMSDGRIRQ 215
Cdd:PRK11174 506 LLLLDEPTASLDAhseQLVMQALN-----AASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-212 |
1.20e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.61 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEKDVTRLSPGRRDVAMVF 82
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 163 SNLDARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:PRK13536 201 TGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
19-226 |
2.23e-26 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 109.66 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSVVDN 96
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IA--YPLKVrgtDRRTRAAK-ATETGD----QLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:TIGR03797 547 IAggAPLTL---DEAWEAARmAGLAEDiramPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 170 RLEARTFLKKLQlelgVTTVFVTHdQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:TIGR03797 624 QAIVSESLERLK----VTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
2.71e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKdvtrLSPGrrdvamVF- 82
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET----VKIG------YFd 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALF-PHMSVVDNIayplkvrgtdrrtraAKATETGDQLSLQGLMAR---RPAE-------LSGGQQQRVALARAMAC 151
Cdd:COG0488 385 QHQEELdPDKTVLDEL---------------RDGAPGGTEQEVRGYLGRflfSGDDafkpvgvLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 152 RPKVFLFDEPLSNLDarlrLEARTFLKKLQLELGVTTVFVTHDQaEAL-ALADRIAVMSDGRIRQLD 217
Cdd:COG0488 450 PPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDR-YFLdRVATRILEFEDGGVREYP 511
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-167 |
2.79e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.42 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRDVAMVFQDyALFPHMSVV 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN-AMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 95 DNIAYPLKVRGTDRRTRAAKATETGdqlsLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAALEAVG----LAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-225 |
3.97e-26 |
|
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: 104.11 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpHMSVVDN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IAypLKVRGTDRR-----TRAAKATETGDQLSL--QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARl 169
Cdd:cd03252 96 IA--LADPGMSMErvieaAKLAGAHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 170 rlEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:cd03252 173 --SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
5.63e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVF------PG--------------DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI 63
Cdd:COG4586 2 IEVENLSKTYrvyekePGlkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 64 GEKDVTRLSPG-RRDVAMVF-QDYALFPHMSVVDNiaYPL-----KVRGTDRRTRAAKATETgdqLSLQGLMaRRPA-EL 135
Cdd:COG4586 82 LGYVPFKRRKEfARRIGVVFgQRSQLWWDLPAIDS--FRLlkaiyRIPDAEYKKRLDELVEL---LDLGELL-DTPVrQL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 136 SGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-213 |
8.13e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 108.56 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTKVF-PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDV-TRLSPGRRDVAMVFQ 83
Cdd:TIGR01257 931 VKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGtdrRTRAAKATETGDQLSLQGLMARRPAE---LSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKG---RSWEEAQLEMEAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 161 PLSNLDARLRLEARTFLkkLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-226 |
3.42e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.34 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSV 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAKATETGDQLS--LQGL---MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAKAANAHDFIMefPNGYdteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 169 LRlEARTFLKKLQlelGVTTVFVTHdQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:TIGR00958 652 CE-QLLQESRSRA---SRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
3.46e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.14 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQI-----RIGEKDVTRLspgRRDVAMVFQDyalfPHMSV 93
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL---RKHIGIVFQN----PDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNI-----AYPLK---VRGTDRRTRAAKAtetgdqLSLQGLMARR---PAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK13648 97 VGSIvkydvAFGLEnhaVPYDEMHRRVSEA------LKQVDMLERAdyePNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 163 SNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALAlADRIAVMSDGRIRQLDTAREVF 223
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-212 |
4.64e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.58 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEKDVTRLSPGRRDVAM 80
Cdd:PRK13537 6 APIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNiaypLKVRGTDRRTRAAKATETGDQL----SLQGLMARRPAELSGGQQQRVALARAMACRPKVF 156
Cdd:PRK13537 85 VPQFDNLDPDFTVREN----LLVFGRYFGLSAAAARALVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 157 LFDEPLSNLDARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-227 |
6.34e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKST----LLRTIAgletpTGGQIRIGEKDVTRLS-----PGRRDVAMVFQD--YA 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVFQDpnSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKVR-----GTDRRTRAAKA-TETG-DQLSLQglmaRRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHqptlsAAQREQQVIAVmEEVGlDPETRH----RYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
20-213 |
7.31e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 105.21 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSVVDNI 97
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AYPLKVRGTDRRTRAAKATETGDQLS-----LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDArlRLE 172
Cdd:TIGR01846 552 ALCNPGAPFEHVIHAAKLAGAHDFISelpqgYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDY--ESE 629
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068383214 173 ARTFLKKLQLELGVTTVFVTHdQAEALALADRIAVMSDGRI 213
Cdd:TIGR01846 630 ALIMRNMREICRGRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-213 |
2.03e-24 |
|
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: 98.88 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL---ETPTGGQIRIGEKDVTRlSPGRRDVAMVFQDYALFPHMSVVDN 96
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKP-DQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IAYPLKVRGTDRRTRAAKATETGD----QLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLE 172
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDvllrDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068383214 173 ARTFLKklQLELGVTTVFVTHDQ--AEALALADRIAVMSDGRI 213
Cdd:cd03234 182 LVSTLS--QLARRNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-213 |
3.36e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.81 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFPGDvTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRL---SPGRRD 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 78 VAMVFQDYALFPHMSVVDNIAYPLKVR-GTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 157 LFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-213 |
3.87e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.23 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEK-----DVTRLSPGRR---- 76
Cdd:PRK11701 9 VRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 77 --DVAMVFQDYA--LFPHMSVVDNIAYPLKVRGtDRRTRAAKATeTGDQLSLQGLMARR----PAELSGGQQQRVALARA 148
Cdd:PRK11701 88 rtEWGFVHQHPRdgLRMQVSAGGNIGERLMAVG-ARHYGDIRAT-AGDWLERVEIDAARiddlPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 149 MACRPKVFLFDEPLSNLD----ARLrLEartFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDvsvqARL-LD---LLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-212 |
4.76e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 8 ELTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLeTPTG---GQIRI-GEKDVTRlspGRRD-----V 78
Cdd:PRK13549 10 NITKTFGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFeGEELQAS---NIRDteragI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 79 AMVFQDYALFPHMSVVDNI---AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKV 155
Cdd:PRK13549 85 AIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 156 FLFDEPLSNLDARlrlEARTFL---KKLQlELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:PRK13549 165 LILDEPTASLTES---ETAVLLdiiRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-213 |
7.95e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 97.98 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTALDgLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-----GEKDVTRLSPGRR-- 76
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRD-VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 77 ----DVAMVFQDYA--LFPHMSVVDNIAYPLKVRGtDRRTRAAKATeTGDQLSLQGLMARR----PAELSGGQQQRVALA 146
Cdd:TIGR02323 83 lmrtEWGFVHQNPRdgLRMRVSAGANIGERLMAIG-ARHYGNIRAT-AQDWLEEVEIDPTRiddlPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 147 RAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-212 |
1.83e-23 |
|
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: 96.00 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlsPGRrdVAMVFQdYALFPHMSVVDNI- 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---------PGS--IAYVSQ-EPWIQNGTIRENIl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 -AYPLKvrgTDRRTRAAKA---------------TETGDQlslqGLMarrpaeLSGGQQQRVALARAMACRPKVFLFDEP 161
Cdd:cd03250 88 fGKPFD---EERYEKVIKAcalepdleilpdgdlTEIGEK----GIN------LSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 162 LSNLDARLrleARTFLKKL---QLELGVTTVFVTHdQAEALALADRIAVMSDGR 212
Cdd:cd03250 155 LSAVDAHV---GRHIFENCilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-226 |
1.93e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.55 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 17 VTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRD--VAMVFQD--YALFPHMS 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQDpsTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVR-GTDRRTRAAKATETGDQLSLQGLMARR-PAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:PRK15112 106 ISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 171 LEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP 226
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
2.04e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.63 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSP---GRRDVAM 80
Cdd:PRK09700 6 ISMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHMSVVDNI---AYPLK----VRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 154 KVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDG 211
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-239 |
2.81e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKS-TLLRTIAGLETP----TGGQIRIGEKDVTRLSPGR------RDVAMVFQD-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTlrgvrgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 85 YALFPHMSVVDNIAYPLKV-RGTdrRTRAAKAtETGDQLSLQGL--MARR----PAELSGGQQQRVALARAMACRPKVFL 157
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLhRGM--RREAARG-EILNCLDRVGIrqAAKRltdyPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 158 FDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGS 237
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNS 259
|
..
gi 2068383214 238 TP 239
Cdd:PRK15134 260 EP 261
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-213 |
3.50e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLE--TPTGGQIRIGEKDVTRLSP---GRRDVAMVFQDYALFPHMSVV 94
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPderARAGIFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 D--NIAYPlKVRGTDRRTRA--AKATETGDQLSLQGLMARRP--AELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA- 167
Cdd:COG0396 96 NflRTALN-ARRGEELSAREflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDId 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068383214 168 RLRLEARTFlKKLQLElGVTTVFVTHdQAEALAL--ADRIAVMSDGRI 213
Cdd:COG0396 175 ALRIVAEGV-NKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRI 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
3.94e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.86 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 6 VVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVF 82
Cdd:PRK09700 265 VFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 Q---DYALFPHMSVVDNIAYP--LKVRG-------TDRRTRAAKATETGDQLSLQ-GLMARRPAELSGGQQQRVALARAM 149
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAISrsLKDGGykgamglFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 150 ACRPKVFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTARE 221
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-213 |
4.55e-23 |
|
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: 94.52 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLE--TPTGGQIRIGEKDVTRLSP---GRRDVAMVFQDYALFP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIayplkvRGTDrrtraakatetgdqlslqglmarrpAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA-R 168
Cdd:cd03217 91 GVKNADFL------RYVN-------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 169 LRLEARTfLKKLqLELGVTTVFVTHDQaEALAL--ADRIAVMSDGRI 213
Cdd:cd03217 140 LRLVAEV-INKL-REEGKSVLIITHYQ-RLLDYikPDRVHVLYDGRI 183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-213 |
5.37e-23 |
|
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: 93.92 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRD-VAMVFQDYALFphmsvvdn 96
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQRPYLF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 iayplkvrgtdrrtraakATETGDQLSLQglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEA-RT 175
Cdd:cd03247 88 ------------------DTTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLlSL 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 2068383214 176 FLKKLQlelGVTTVFVTHdQAEALALADRIAVMSDGRI 213
Cdd:cd03247 141 IFEVLK---DKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-213 |
5.55e-23 |
|
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: 99.51 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpHMSVVDNI 97
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AY--PlkvrGTDRR--TRAAKATETGD-QLSL-QGLMAR---RPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:COG5265 453 AYgrP----DASEEevEAAARAAQIHDfIESLpDGYDTRvgeRGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 169 LRLEARTFLKklQLELGVTTVFVTH------DqaealalADRIAVMSDGRI 213
Cdd:COG5265 529 TERAIQAALR--EVARGRTTLVIAHrlstivD-------ADEILVLEAGRI 570
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-213 |
9.45e-23 |
|
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: 93.87 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLetpTGGQIRIgEKDVT--------RLS 72
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSV-EGDIHyngipykeFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 73 PGRRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDrrtraakatetgdqlSLQGLmarrpaelSGGQQQRVALARAMACR 152
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGNE---------------FVRGI--------SGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 153 PKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTvFVTHDQA--EALALADRIAVMSDGRI 213
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTT-FVSLYQAsdEIYDLFDKVLVLYEGRQ 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-167 |
3.24e-22 |
|
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: 92.42 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGR-RDVAMVFQDYALFPHMSV 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 94 VDNIAYPLKVRGTDRRTraakATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
15-218 |
3.42e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.40 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQDYALFPHM 91
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAY-PLKVRGTDRRTRAAKATETGDQlsLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:PRK11614 96 TVEENLAMgGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068383214 171 LEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDT 218
Cdd:PRK11614 174 QQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
3.93e-22 |
|
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: 96.80 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLET--PTGGQI-----------------RIG 64
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 65 EK-------------DVTRLSPG-----RRDVAMVFQ-DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQ 125
Cdd:TIGR03269 80 EPcpvcggtlepeevDFWNLSDKlrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 126 GLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD---ARLRLEArtfLKKLQLELGVTTVFVTHdQAEALA-L 201
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNA---LEEAVKASGISMVLTSH-WPEVIEdL 235
|
250 260
....*....|....*....|.
gi 2068383214 202 ADRIAVMSDGRIRQLDTAREV 222
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEV 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-224 |
4.34e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLeTPTGGQIRIGEKDVTRLSPGR--RDVAMVFQDYALFPHMSVVDNI 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 A--YPLKVRGTDRRTRAAKATEtgdQLSLQGLMARRPAELSGGQQQRVALARAM-----ACRP--KVFLFDEPLSNLDAR 168
Cdd:COG4138 91 AlhQPAGASSEAVEQLLAQLAE---ALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 169 LRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:COG4138 168 QQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-222 |
4.47e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.51 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGR--RDVAMVFQDYALFPHMS 92
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIA---YPLKVRGTDRRTRAAKATETGDQLS-LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:PRK10253 98 VQELVArgrYPHQPLFTRWRKEDEEAVTKAMQATgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-194 |
5.14e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 96.66 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFpH 90
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLKVRGTDRRTRAAKATETGDQLS-----LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:TIGR02868 423 TTVRENLRLARPDATDEELWAALERVGLADWLRalpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*....
gi 2068383214 166 DARLRLEARTFLkkLQLELGVTTVFVTHD 194
Cdd:TIGR02868 503 DAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-213 |
7.34e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 7.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GE--KDVTRLSPgRRDVAMVFQDYALFp 89
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTdiRTVTRASL-RRNIAVVFQDAGLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNI------AYPLKVRGTDRRTRAAKATETGDQlSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:PRK13657 422 NRSIEDNIrvgrpdATDEEMRAAAERAQAHDFIERKPD-GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 164 NLDArlRLEARTFLKKLQLELGVTTVFVTHDQAeALALADRIAVMSDGRI 213
Cdd:PRK13657 501 ALDV--ETEAKVKAALDELMKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-230 |
2.17e-21 |
|
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: 91.32 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 26 TIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIrigEKDVTRLSPGRRDVAMVFQdyalfphMSVVDNIAYPLKVRG 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYE-------GTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 106 TDRRTRaakaTETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELG 185
Cdd:cd03237 91 THPYFK----TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 186 VTTVFVTHDQAEALALADRIAV----------------MSDGRIRQLDTAREVFRRPADTF 230
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVfegepsvngvanppqsLRSGMNRFLKNLDITFRRDPETG 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-219 |
4.82e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFPGDVTALDGLTFTIQDGEffALL--GPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlsPGRRDVA 79
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQD-YalFPHMSVVDNIAYPLKVRGTDRrtraAKATETGDQLSLQGLMARRPAE------LSGGQQQRVALARAMACR 152
Cdd:COG4178 430 FLPQRpY--LPLGTLREALLYPATAEAFSD----AELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 153 PKVFLFDEPLSNLDArlRLEARtFLKKLQLEL-GVTTVFVTHdQAEALALADRIAVMSDGRIRQLDTA 219
Cdd:COG4178 504 PDWLFLDEATSALDE--ENEAA-LYQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-213 |
5.44e-21 |
|
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: 94.04 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSVVDN 96
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IAYPLKVRGT-DRRTRAAKATETGD-----QLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDArlr 170
Cdd:TIGR01193 568 LLLGAKENVSqDEIWAACEIAEIKDdienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT--- 644
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068383214 171 LEARTFLKKLQLELGVTTVFVTHdQAEALALADRIAVMSDGRI 213
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-212 |
1.08e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 86.73 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPGDVTaLDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKdvtrlspgrrdvamvfQ 83
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHmsvvdniayplkvrgtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:cd03221 64 KIGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 164 NLDarlrLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:cd03221 100 HLD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-213 |
1.58e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 24 TFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQDY---ALFPHMSVVDNI 97
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaiRAGIMLCPEDRkaeGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 ---AYPLKVRG---TDRRTRAAKATETGDQLSLQGLMARRP-AELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:PRK11288 353 nisARRHHLRAgclINNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068383214 171 LEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK11288 433 HEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-218 |
2.54e-20 |
|
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: 87.55 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHm 91
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlRSRISIIPQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAyPLKVRGTDRRTRA---AKATETGDQLS--LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:cd03244 93 TIRSNLD-PFGEYSDEELWQAlerVGLKEFVESLPggLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 167 ----ARLRLEARTFLKklqlelGVTTVFVTHdQAEALALADRIAVMSDGRIRQLDT 218
Cdd:cd03244 172 petdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-227 |
5.18e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.83 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP----TGGQIRIgekDVTRLSPGR---RDVAMVFQD--YA 86
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLL---DGKPVAPCAlrgRKIATIMQNprSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKVRG-TDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGkPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 166 DARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPA 227
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-212 |
6.51e-20 |
|
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: 90.27 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLEtPTG---GQIRIGEKDVTRLS---PGRRDVAMVF 82
Cdd:TIGR02633 7 IVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNirdTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNI-------------AYPLKVRgtdrrtraaKATETGDQLSLQGLMARRP-AELSGGQQQRVALARA 148
Cdd:TIGR02633 85 QELTLVPELSVAENIflgneitlpggrmAYNAMYL---------RAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 149 MACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-239 |
1.05e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.04 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVFP---GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP----TGGQIRIGEKDVTRLSP 73
Cdd:COG4170 1 MPLLDIRNLTIEIDtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 G------RRDVAMVFQD--YALFPHMSVVDNI-----AYPLKVRGTDR---RTRAAKAT--ETGDQlSLQGLMARRPAEL 135
Cdd:COG4170 81 RerrkiiGREIAMIFQEpsSCLDPSAKIGDQLieaipSWTFKGKWWQRfkwRKKRAIELlhRVGIK-DHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 136 SGGQQQRVALARAMACRPKVFLFDEPLSNLDAR-----LRLEARtfLKKLQlelGVTTVFVTHDQAEALALADRIAVMSD 210
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTtqaqiFRLLAR--LNQLQ---GTSILLISHDLESISQWADTITVLYC 234
|
250 260
....*....|....*....|....*....
gi 2068383214 211 GRIRQLDTAREVFRRPADTFVANFIGSTP 239
Cdd:COG4170 235 GQTVESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-210 |
1.87e-19 |
|
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: 83.74 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlsPGRRDVAMVFQDyALF 88
Cdd:cd03223 6 LSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR-PYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNIAYPLKvrgtdrrtraakatetgdqlslqglmarrpAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:cd03223 76 PLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068383214 169 LrleARTFLKKLQlELGVTTVFVTHdQAEALALADRIAVMSD 210
Cdd:cd03223 126 S---EDRLYQLLK-ELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-214 |
2.24e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHmSVVDN 96
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISVVSQRVHLFSA-TLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IAYplkvrgtdrrtraAKATETGDQLS--------------LQGLMA-----RRPaeLSGGQQQRVALARAMACRPKVFL 157
Cdd:PRK11160 434 LLL-------------AAPNASDEALIevlqqvgleklledDKGLNAwlgegGRQ--LSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 158 FDEPLSNLDARLRLEARTFLkkLQLELGVTTVFVTHdQAEALALADRIAVMSDGRIR 214
Cdd:PRK11160 499 LDEPTEGLDAETERQILELL--AEHAQNKTVLMITH-RLTGLEQFDRICVMDNGQII 552
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-225 |
1.21e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG----RRDVAMVFQD--YALFp 89
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalRQQVATVFQDpeQQIF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 170 RLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRR 225
Cdd:PRK13638 172 RTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-193 |
1.38e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 21 DGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVFQDYALFPHMSVVDNIAY 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRGTDRRTRAAKATEtgdQLSLQG---LMARRpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR--LRLEAR 174
Cdd:PRK13538 98 YQRLHGPGDDEALWEALA---QVGLAGfedVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgvARLEAL 171
|
170
....*....|....*....
gi 2068383214 175 tFLKklQLELGVTTVFVTH 193
Cdd:PRK13538 172 -LAQ--HAEQGGMVILTTH 187
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-215 |
1.75e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPG-DVTALDGLTFTIQDGEFFALLGPSGCGKSTllrtIAGLETP----TGGQIRIGEKDVT--RLSPGRR 76
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRdyTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 77 DVAMVFQDYALFpHMSVVDNIAYPLKVRGT----DRRTRAAKATETGDQLSlQGL---MARRPAELSGGQQQRVALARAM 149
Cdd:PRK11176 418 QVALVSQNVHLF-NDTIANNIAYARTEQYSreqiEEAARMAYAMDFINKMD-NGLdtvIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 150 ACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElgvTTVFVTHDQAEALALADRIAVMSDGRIRQ 215
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-236 |
1.89e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.33 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEKdvtrLSPG----RRDVAMVFQ 83
Cdd:NF033858 272 LTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQP----VDAGdiatRRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLS 163
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 164 NLD--AR---LRLeartfLKKLQLELGVtTVFV-THDQAEAlALADRIAVMSDGRIRQLDTARE-VFRRPADTFVANFIG 236
Cdd:NF033858 427 GVDpvARdmfWRL-----LIELSREDGV-TIFIsTHFMNEA-ERCDRISLMHAGRVLASDTPAAlVAARGAATLEEAFIA 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-212 |
1.91e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.94 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGR---RDVAMVFQDY 85
Cdd:PRK10982 4 ISKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 86 ALFPHMSVVDNI---AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK10982 83 NLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 163 SNLDARLRLEARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGR 212
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-235 |
2.38e-18 |
|
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: 86.15 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlspgRRDVAMVFQDyALFPHMSVV 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 DNIAY--PLKVRGTDRRTRAA------KATETGDQLSLqglmARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:TIGR00957 717 ENILFgkALNEKYYQQVLEACallpdlEILPSGDRTEI----GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 167 ARLrleARTFLKKLQLELGV----TTVFVTHDQAeALALADRIAVMSDGRIRQLDTAREVFRRpaDTFVANFI 235
Cdd:TIGR00957 793 AHV---GKHIFEHVIGPEGVlknkTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQR--DGAFAEFL 859
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-167 |
7.33e-18 |
|
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: 80.61 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG-RRDVAMVFQDYALFPHMSV 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 94 VDNIAYPLKVRGTDRRTRAAkatetgDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:cd03231 91 LENLRFWHADHSDEQVEEAL------ARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-195 |
9.11e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLE--TPTGGQIRIGEKDVTRLSPgrrdvamvfqdyalfphmsVVD 95
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS-------------------LID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 96 NIAyplkvrgtdRRTRAAKATETgdqLSLQGL-----MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL- 169
Cdd:COG2401 105 AIG---------RKGDFKDAVEL---LNAVGLsdavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTa 172
|
170 180
....*....|....*....|....*.
gi 2068383214 170 RLEARTFLKKLQlELGVTTVFVTHDQ 195
Cdd:COG2401 173 KRVARNLQKLAR-RAGITLVVATHHY 197
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-251 |
1.64e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.77 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQIDVVELTKVF---PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP----TGGQIRIGEKDVTRLSP 73
Cdd:PRK15093 1 MPLLDIRNLTIEFktsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 GRR------DVAMVFQD--YALFPHMSV----VDNI-AYPLKVRGTDR-RTRAAKATETGDQLSLQ---GLMARRPAELS 136
Cdd:PRK15093 81 RERrklvghNVSMIFQEpqSCLDPSERVgrqlMQNIpGWTYKGRWWQRfGWRKRRAIELLHRVGIKdhkDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 137 GGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQL 216
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2068383214 217 DTAREVFRRPADTFVANFIGSTP-----------MNLIPGELVGLE 251
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPdfgsamphksrLNTLPGAIPLLE 286
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-221 |
3.46e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 10 TKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLeTPTG---GQIRI-GE----KDVtRLSPgRRDVAMV 81
Cdd:NF040905 8 TKTFPG-VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFdGEvcrfKDI-RDSE-ALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDYALFPHMSVVDNI--AYPLKVRGT-DRRTRAAKATEtgdqlslqgLMAR-----RPAELSG----GQQQRVALARAM 149
Cdd:NF040905 84 HQELALIPYLSIAENIflGNERAKRGViDWNETNRRARE---------LLAKvgldeSPDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 150 ACRPKVFLFDEP---LSNLDARLRLEartflkkLQLEL---GVTTVFVTHDQAEALALADRIAVMSDGR-IRQLDTARE 221
Cdd:NF040905 155 SKDVKLLILDEPtaaLNEEDSAALLD-------LLLELkaqGITSIIISHKLNEIRRVADSITVLRDGRtIETLDCRAD 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-205 |
6.21e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.54 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgEKD--VTRLS--PGRRDVAMVFqDY----- 85
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDliVARLQqdPPRNVEGTVY-DFvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 86 -ALFPHMSVVDNIAYPLKVRGTDRR-TRAAKATETGDQ-------------LSLQGLMARRP-AELSGGQQQRVALARAM 149
Cdd:PRK11147 92 eEQAEYLKRYHDISHLVETDPSEKNlNELAKLQEQLDHhnlwqlenrinevLAQLGLDPDAAlSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 150 ACRPKVFLFDEPLSNLDarlrLEARTFLKKLQLELGVTTVFVTHDQAEALALADRI 205
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-212 |
1.54e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTG--GQIRIGEKDVTRlsPGRRDVAMVFQDYALFPHMSVVD 95
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 96 NIAYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPA--------ELSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTiignsfirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 168 ----RLRLEARTFLKKlqlelGVTTVFVTHD-QAEALALADRIAVMSDGR 212
Cdd:PLN03211 240 taayRLVLTLGSLAQK-----GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-213 |
1.96e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 23 LTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRR-DVAMVF-----QDYALFPHMSVVDN 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 I-AYPLKVRGTDRRTRAAKATETG--DQLSLQGLMARRPAE-LSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLE 172
Cdd:PRK15439 362 VcALTHNRRGFWIKPARENAVLERyrRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARND 441
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068383214 173 ARTFLKKLQlELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK15439 442 IYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-208 |
2.28e-16 |
|
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: 77.41 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 28 QDGEFFALLGPSGCGKSTLLRTIAGLETPTGGqiRIGEKD-----------------VTRLSPGRRDVAMVFQdyalfph 90
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeildefrgselqnyFTKLLEGDVKVIVKPQ------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 msVVDNIayPLKVRGT-----DRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:cd03236 95 --YVDLI--PKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068383214 166 DARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVM 208
Cdd:cd03236 171 DIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-213 |
2.51e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQDY---ALFPHMSV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglANGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNI---AYPLKVRGTDRRTRAAKATETGDQLSLQGL----MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:PRK10762 348 KENMsltALRYFSRAGGSLKHADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 167 ARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK10762 428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-217 |
3.04e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 23 LTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHMsvvdniayp 100
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQL--------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 101 LKVRGTDRRTRAAKA----TETGDQLSLQGLMARRPaELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRleaRTF 176
Cdd:PRK10522 413 LGPEGKPANPALVEKwlerLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR---REF 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068383214 177 LKKL--QL-ELGVTTVFVTHDQAeALALADRIAVMSDGRIRQLD 217
Cdd:PRK10522 489 YQVLlpLLqEMGKTIFAISHDDH-YFIHADRLLEMRNGQLSELT 531
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-218 |
3.44e-16 |
|
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: 75.91 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR--LSPGRRDVAMVFQDYALFphMSVVDN 96
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipLEDLRSSLTIIPQDPTLF--SGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 IAYPLKvRGTDRRTRAA-KATETGDQlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNL----DARLRL 171
Cdd:cd03369 101 NLDPFD-EYSDEEIYGAlRVSEGGLN-------------LSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 172 EARTFLKklqlelGVTTVFVTHdQAEALALADRIAVMSDGRIRQLDT 218
Cdd:cd03369 167 TIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-244 |
3.92e-16 |
|
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: 79.67 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 8 ELTKVFPGDVT-ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTrlspgrRDVAMVFQDYA 86
Cdd:TIGR01257 1942 ELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------TNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYP-------LKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANF-IGST 238
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSP 2174
|
....*.
gi 2068383214 239 PMNLIP 244
Cdd:TIGR01257 2175 KDDLLP 2180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-213 |
6.82e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLeTPTGGQI---------RIGEKDVTRLSpgrrdvAMVFQDYALFPH 90
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR-SPKGVKGsgsvllngmPIDAKEMRAIS------AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 MSVVDNIAYPLKVR---GTDRRTRAAKATETGDQLSLQ-------GLMARRPAeLSGGQQQRVALARAMACRPKVFLFDE 160
Cdd:TIGR00955 114 LTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 161 PLSNLDArlrLEARTFLKKLQ-LELGVTTVFVTHDQ--AEALALADRIAVMSDGRI 213
Cdd:TIGR00955 193 PTSGLDS---FMAYSVVQVLKgLAQKGKTIICTIHQpsSELFELFDKIILMAEGRV 245
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-215 |
9.12e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.83 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPG-DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT--RLSPGRRDVAMVFQDYALFP 89
Cdd:PRK10789 323 YPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HmSVVDNIAYPLKVRGTDRRTRAAK-ATETGDQLSL-QGL---MARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSN 164
Cdd:PRK10789 403 D-TVANNIALGRPDATQQEIEHVARlASVHDDILRLpQGYdteVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 165 LDARLRleaRTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQ 215
Cdd:PRK10789 482 VDGRTE---HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-244 |
1.09e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 18 TALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHMSVVD 95
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 96 NIA---YPLkvRGTDRRTRAAKATETGDQLSLQGL--MARRPAE-LSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL 169
Cdd:PRK10575 105 LVAigrYPW--HGALGRFGAADREKVEEAISLVGLkpLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 170 RLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPadtfVANFIGSTPMNLIP 244
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE----TLEQIYGIPMGILP 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-210 |
1.46e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGE----KDVTrLSPGRRDVAMVFQDYALFPHm 91
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSKIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAYPL-------------------KVRGTDRRT--RAAKA--------TETGDQL-------------------- 122
Cdd:PTZ00265 475 SIKNNIKYSLyslkdlealsnyynedgndSQENKNKRNscRAKCAgdlndmsnTTDSNELiemrknyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 123 -------------SLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTV 189
Cdd:PTZ00265 555 kvlihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250 260
....*....|....*....|.
gi 2068383214 190 FVTHdQAEALALADRIAVMSD 210
Cdd:PTZ00265 635 IIAH-RLSTIRYANTIFVLSN 654
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-234 |
1.78e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 23 LTFTIQDGEFFALLGPSGCGKSTLLRTIAGLeTPTGGQIRIGEKDVTRLSPG----RRD---------VAM-VFQDYALf 88
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAelarHRAylsqqqtppFAMpVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 pHMSVVDNIAYPLKVrgtdrrtraakATETGDQLSLQGLMARRPAELSGGQQQRVALARAM-----ACRP--KVFLFDEP 161
Cdd:PRK03695 93 -HQPDKTRTEAVASA-----------LNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 162 LSNLDARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRP--ADTFVANF 234
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEnlAQVFGVNF 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-221 |
1.92e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.47 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAG-LETPTGGQIRIgekdvtrlspgRRDVAMVFQDYALFpHMSV 93
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI-----------RGTVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRgTDRRTRAAKATETGDQLSL-----QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:PLN03130 696 RDNILFGSPFD-PERYERAIDVTALQHDLDLlpggdLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 169 LrleAR-TFLKKLQLEL-GVTTVFVThDQAEALALADRIAVMSDGRIRQLDTARE 221
Cdd:PLN03130 775 V---GRqVFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-211 |
3.04e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGdVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPgrRD-----VAMVFQ 83
Cdd:PRK10762 10 IDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP--KSsqeagIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DYALFPHMSVVDNI----AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:PRK10762 87 ELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 160 EPlsnLDARLRLEARTFLKKLQlEL---GVTTVFVTHDQAEALALADRIAVMSDG 211
Cdd:PRK10762 167 EP---TDALTDTETESLFRVIR-ELksqGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-213 |
4.11e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.30 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLtftIQDGEFFALLGPSGCGKSTLLRTIA----GLETPTGGQIR---IGEKDVTRLSPGrrDVAMVFQDYALFPHMS 92
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITydgITPEEIKKHYRG--DVVYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVR-------GTDRRTRAAKATETgdQLSLQGLMARRPAE--------LSGGQQQRVALARAMACRPKVFL 157
Cdd:TIGR00956 155 VGETLDFAARCKtpqnrpdGVSREEYAKHIADV--YMATYGLSHTRNTKvgndfvrgVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 158 FDEPLSNLDARLRLEartFLKKLQLELGV--TTVFVTHDQA--EALALADRIAVMSDGRI 213
Cdd:TIGR00956 233 WDNATRGLDSATALE---FIRALKTSANIldTTPLVAIYQCsqDAYELFDKVIVLYEGYQ 289
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-214 |
4.44e-15 |
|
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: 75.63 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-ETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQD---YALFPHMS 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRGTdRRTRAAKATETG------DQLSLQGLMARRP-AELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:TIGR02633 356 VGKNITLSVLKSFC-FKMRIDAAAELQiigsaiQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 166 DARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRIR 214
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-205 |
4.75e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRigekdvtrlSPGRRDVAMVFQDYALFPHMsvv 94
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQKLYLDTTL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 dniayPLKVRgtdRRTRAAKATETGDQL------SLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR 168
Cdd:PRK09544 83 -----PLTVN---RFLRLRPGTKKEDILpalkrvQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2068383214 169 LRLEARTFLKKLQLELGVTTVFVTHDQAEALALADRI 205
Cdd:PRK09544 155 GQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-207 |
4.99e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 26 TIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIrigEKDVT------RLSPgrrdvamvfqDYalfpHMSVVDNIAy 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKisykpqYISP----------DY----DGTVEEFLR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 plKVRGTDRRTRAAKaTETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKK 179
Cdd:COG1245 424 --SANTDDFGSSYYK-TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180
....*....|....*....|....*...
gi 2068383214 180 LQLELGVTTVFVTHDQAEALALADRIAV 207
Cdd:COG1245 501 FAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-218 |
7.28e-15 |
|
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: 75.22 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 25 FTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAMVFQDYALFPHMSVVDNIAYPLK 102
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLFSAVFSDFHLFDRLLGLDGEADPAR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 103 VRGTDRRTR-AAKATETGDQLSLQglmarrpaELSGGQQQRVALARAMA-CRPkVFLFDEPLSNLDARLRleaRTFLKKL 180
Cdd:COG4615 433 ARELLERLElDHKVSVEDGRFSTT--------DLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEFR---RVFYTEL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068383214 181 QLEL---GVTTVFVTHDQAeALALADRIAVMSDGRIRQLDT 218
Cdd:COG4615 501 LPELkarGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTG 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-214 |
9.19e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 21 DGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGL-ETPTGGQIRIGEKDVTRLSPG---RRDVAMVFQD---YALFPHMSV 93
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 94 VDNIAYPLKVRGTdRRTRAAKATETGD-QLSLQGLMARRP------AELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:PRK13549 359 GKNITLAALDRFT-GGSRIDDAAELKTiLESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 167 ARLRLEartfLKKLQLEL---GVTTVFVTHDQAEALALADRIAVMSDGRIR 214
Cdd:PRK13549 438 VGAKYE----IYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-205 |
1.10e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 23 LTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRRdVAMVFQDYALFPHMSVVDNIAYPLK 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF-MAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 103 VRGtdrrtRAAKATeTGDQLSLQGLMARRPA---ELSGGQQQRVALARAMACRPKVFLFDEPLSNLDarlrLEARTFLKK 179
Cdd:PRK13543 109 LHG-----RRAKQM-PGSALAIVGLAGYEDTlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD----LEGITLVNR 178
|
170 180
....*....|....*....|....*....
gi 2068383214 180 L---QLELGVTTVFVTHDQAEALALADRI 205
Cdd:PRK13543 179 MisaHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-224 |
1.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTggqirigEKDVTRLspgRRDVAMVFQDYALFpHMSVVDNIAY 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA-------ETSSVVI---RGSVAYVPQVSWIF-NATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRgTDRRTRAAKATETGDQLSL-----QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEAR 174
Cdd:PLN03232 702 GSDFE-SERYWRAIDVTALQHDLDLlpgrdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 175 TFLKKLQLElGVTTVFVThDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:PLN03232 781 DSCMKDELK-GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-194 |
1.42e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.20 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 9 LTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQirigekdvTRLSPGRRdVAMVFQDYALF 88
Cdd:TIGR03719 10 VSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGIK-VGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 89 PHMSVVDNI--AYPLKVRGTDR--RTRAAKATETGD-------QLSLQGLMA------------------RRP------A 133
Cdd:TIGR03719 81 PTKTVRENVeeGVAEIKDALDRfnEISAKYAEPDADfdklaaeQAELQEIIDaadawdldsqleiamdalRCPpwdadvT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 134 ELSGGQQQRVALARAMACRPKVFLFDEPLSNLDArlrlEARTFLKKLQLELGVTTVFVTHD 194
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-206 |
1.89e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKdvtrlspgrRDVAMVFQ 83
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET---------VKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DY-ALFPHMSVVDNIAYP---LKVRGTDRRTRA---AKATETGDQLSLQGlmarrpaELSGGQQQRVALARAMACRPKVF 156
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGldiIKLGKREIPSRAyvgRFNFKGSDQQKKVG-------QLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 157 LFDEPLSNLDarlrLEARTFLKKLQLELGVTTVFVTHDQaealALADRIA 206
Cdd:TIGR03719 466 LLDEPTNDLD----VETLRALEEALLNFAGCAVVISHDR----WFLDRIA 507
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-227 |
2.04e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.23 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSG---------------------------CGKSTLLRTIAGLETP 56
Cdd:NF000106 14 VEVRGLVKHF-GEVKAVDGVDLDVREGTVLGVLGP*Gaa**rgalpahv*gpdagrrpwrf*twCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 57 tggqIRIGEKDVTRlspGRRDVAMVFQDYALfphmsvvdniayplkvrgtDRRTRAAKATETGDQLSLQGLMARRPAELS 136
Cdd:NF000106 93 ----VR*GRRESFS---GRENLYMIGR*LDL-------------------SRKDARARADELLERFSLTEAAGRAAAKYS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 137 GGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTH--DQAEALA----LADRIAVMSD 210
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQymEEAEQLAheltVIDRGRVIAD 225
|
250 260
....*....|....*....|
gi 2068383214 211 GRIRQLDT---AREVFRRPA 227
Cdd:NF000106 226 GKVDELKTkvgGRTLQIRPA 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-208 |
3.08e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 26 TIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIrigEKDvtrlsPGRRDVAMVFQDYALFPHMS------------- 92
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEE-----PSWDEVLKRFRGTELQDYFKklangeikvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 -VVDNIAYPLK--VR----GTDRRtraAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:COG1245 167 qYVDLIPKVFKgtVRelleKVDER---GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068383214 166 DARLRLEARTFLKKLqLELGVTTVFVTHDQAEALALADRIAVM 208
Cdd:COG1245 244 DIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-224 |
8.63e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLET----PTGGQIR---------IGEKDVTRLSPGRRDVAMVFQDYA 86
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaPRGARVTgdvtlngepLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 LFPHMSVVDNIAYPLKVRG--TDRRTR--AAKATETGDQLSLQGlmaRRPAELSGGQQQRVALARAMA---------CRP 153
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAgaLTHRDGeiAWQALALAGATALVG---RDVTTLSGGELARVQFARVLAqlwpphdaaQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068383214 154 KVFLFDEPLSNLDA----RLRLEARTFLKKLQleLGVTTvfVTHDQAEALALADRIAVMSDGRIRQLDTAREVFR 224
Cdd:PRK13547 174 RYLLLDEPTAALDLahqhRLLDTVRRLARDWN--LGVLA--IVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
1.04e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.85 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPgrRDVAMVF- 82
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA--QDHAYDFe 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSvvdniayplkvrgtdrrtraAKATETGDQLSLQGLMAR---------RPAE-LSGGQQQRVALARAMACR 152
Cdd:PRK15064 397 NDLTLFDWMS--------------------QWRQEGDDEQAVRGTLGRllfsqddikKSVKvLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 153 PKVFLFDEPLSNLDarlrLEArtfLKKLQLELGV---TTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK15064 457 PNVLVMDEPTNHMD----MES---IESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-229 |
1.11e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 26 TIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIrigEKDVT------RLSPgrrDVAMVFQDYAlfphMSVVDNIA- 98
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisykpqYIKP---DYDGTVEDLL----RSITDDLGs 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 99 YPLKvrgtdrrtraakaTETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLK 178
Cdd:PRK13409 431 SYYK-------------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 179 KLQLELGVTTVFVTHDQAEALALADRIAV----------------MSDGRIRQLDTAREVFRRPADT 229
Cdd:PRK13409 498 RIAEEREATALVVDHDIYMIDYISDRLMVfegepgkhghasgpmdMREGMNRFLKELGITFRRDEET 564
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-211 |
1.41e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 68.90 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAG-LETPTG-----GQIRIGEKDVTRLSPGRRDVAMVFQDYALFp 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGkvhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 90 HMSVVDNIAY--PLKVRGTDRRTRAAKATETGDQLSL--QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:cd03290 92 NATVEENITFgsPFNKQRYKAVTDACSLQPDIDLLPFgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068383214 166 DARL--RLEARTFLKKLQlELGVTTVFVTHdQAEALALADRIAVMSDG 211
Cdd:cd03290 172 DIHLsdHLMQEGILKFLQ-DDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-196 |
1.74e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGekdvTRLspgrrDVAMvFQDY--ALFPHMS 92
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKL-----EVAY-FDQHraELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIA---YPLKVRGTDRRTraakatetgdqLS-LQGLM-----ARRPAE-LSGGQQQRVALARaMACRPKVFL-FDEP 161
Cdd:PRK11147 400 VMDNLAegkQEVMVNGRPRHV-----------LGyLQDFLfhpkrAMTPVKaLSGGERNRLLLAR-LFLKPSNLLiLDEP 467
|
170 180 190
....*....|....*....|....*....|....*
gi 2068383214 162 LSNLDarlrLEARTFLKKLQLELGVTTVFVTHDQA 196
Cdd:PRK11147 468 TNDLD----VETLELLEELLDSYQGTVLLVSHDRQ 498
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-168 |
3.00e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFPgDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR-LSPGRRDVAMVF 82
Cdd:PRK13540 2 LDVIELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYALFPHMSVVDNIAYPLKVRGTdrrtrAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPL 162
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....*.
gi 2068383214 163 SNLDAR 168
Cdd:PRK13540 156 VALDEL 161
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-213 |
3.37e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 2 AQIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlspgrrdvAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ--------ALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 82 FQDYALFPHMSVVDnIAYPLKVR-----------GTDRRTRA---AKATETGDQLSLQGLMARRPAELSGGQQQRVALAR 147
Cdd:PRK15056 77 KNLVAYVPQSEEVD-WSFPVLVEdvvmmgryghmGWLRRAKKrdrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 148 AMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADrIAVMSDGRI 213
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-213 |
3.51e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 30 GEFFALLGPSGCGKSTLLRTIAGletptggQIRIGEKDVTrlspGRRDVAMVFQDyALFPHMSVVDNIAYplkvRGTDRR 109
Cdd:PTZ00243 686 GKLTVVLGATGSGKSTLLQSLLS-------QFEISEGRVW----AERSIAYVPQQ-AWIMNATVRGNILF----FDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 110 TRAAKATET----GDQLSLQGLMARRPAE----LSGGQQQRVALARAMACRPKVFLFDEPLSNLDARL--RLEARTFLKK 179
Cdd:PTZ00243 750 ARLADAVRVsqleADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRVVEECFLGA 829
|
170 180 190
....*....|....*....|....*....|....
gi 2068383214 180 LQlelGVTTVFVTHdQAEALALADRIAVMSDGRI 213
Cdd:PTZ00243 830 LA---GKTRVLATH-QVHVVPRADYVVALGDGRV 859
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-207 |
8.88e-13 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 65.67 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 27 IQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlspgrrdvamvfqdyalfphmsvvdniayplkvrgt 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW------------------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 107 DRRTRAAKATETgdqlslqglmarrpaELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGV 186
Cdd:cd03222 59 DGITPVYKPQYI---------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 2068383214 187 TTVFVTHDQAEALALADRIAV 207
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-170 |
1.38e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 65.66 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 37 GPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSpgRRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKAt 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIH- 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 117 etgdQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLR 170
Cdd:PRK13541 110 ----YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-208 |
2.12e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 26 TIQDGEFFALLGPSGCGKSTLLRTIAGLETPT-GGQIRIGEKD--------------VTRLSPGRRDVAMVFQdYalfph 90
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNlGDYEEEPSWDevlkrfrgtelqnyFKKLYNGEIKVVHKPQ-Y----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 msvVDNIayPLKVRGTDRRTrAAKATETG------DQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSN 164
Cdd:PRK13409 169 ---VDLI--PKVFKGKVREL-LKKVDERGkldevvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068383214 165 LDARLRLEARTFLKKLQleLGVTTVFVTHDQAEALALADRIAVM 208
Cdd:PRK13409 243 LDIRQRLNVARLIRELA--EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-241 |
5.33e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 14 PGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR--LSPGRRDVAMVFQDYALFPHm 91
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 92 SVVDNIAyPLKVRGTDRRTRAAKATETGDQLS-----LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLD 166
Cdd:PLN03232 1325 TVRFNID-PFSEHNDADLWEALERAHIKDVIDrnpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 167 ARL-RLEARTflkkLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTFVANFIGSTPMN 241
Cdd:PLN03232 1404 VRTdSLIQRT----IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-213 |
6.67e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPG--RRDVAM 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 81 VFQDYALFPHmSVVDNIAYplkvrGTD-RRTRAAKATETGDQLSL-----QGLMAR---RPAELSGGQQQRVALARAMAC 151
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTL-----GRDiSEEQVWQALETVQLAELarslpDGLYTPlgeQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 152 RPKVFLFDEPLSNLDARLRleaRTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PRK10790 494 TPQILILDEATANIDSGTE---QAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-166 |
9.52e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 4 IDVVELTKVFpGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKdvtrlspgrrdVAMVFQ 83
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET-----------VKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 84 DY---ALFPHMSVVDNIA----YpLKVRGTDRRTRAAKAT---ETGDQLSLQGlmarrpaELSGGQQQRVALARAMACRP 153
Cdd:PRK11819 393 DQsrdALDPNKTVWEEISggldI-IKVGNREIPSRAYVGRfnfKGGDQQKKVG-------VLSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 2068383214 154 KVFLFDEPLSNLD 166
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-213 |
7.13e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 59.69 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 30 GEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlspgrrdvamvfqdyalfphmsvvdniayplkVRGTDRR 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 110 TRAakatetgDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR-----LRLEARTFLKKLQLEL 184
Cdd:smart00382 43 EEV-------LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLKSEK 115
|
170 180
....*....|....*....|....*....
gi 2068383214 185 GVTTVFVTHDQAEALALADRIavMSDGRI 213
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRR--RFDRRI 142
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-193 |
8.46e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.84 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 23 LTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLSPGRrdvamvfqdyalfPHMSV---VDNIAY 99
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQR-------------PYMTLgtlRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRGTDRR-TRAAKATETGDQLSLQGLMARRPA---------ELSGGQQQRVALARAMACRPKVFLFDEPLSNLDarL 169
Cdd:TIGR00954 538 PDSSEDMKRRgLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS--V 615
|
170 180
....*....|....*....|....
gi 2068383214 170 RLEARTFlkKLQLELGVTTVFVTH 193
Cdd:TIGR00954 616 DVEGYMY--RLCREFGITLFSVSH 637
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-166 |
1.09e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 16 DVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLE--TPTGGQIRIGEKDVTRLSPGRR---DVAMVFQdyalfph 90
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQ------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 msvvdniaYPLKVRGTDRR---------TRAAKATETGDQLSLQGLMARR------PAEL---------SGGQQQRVALA 146
Cdd:PRK09580 86 --------YPVEIPGVSNQfflqtalnaVRSYRGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDIL 157
|
170 180
....*....|....*....|
gi 2068383214 147 RAMACRPKVFLFDEPLSNLD 166
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD 177
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-211 |
2.16e-10 |
|
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: 61.85 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRigekdvtrlSPGRrdVAMVFQDYALFPHmSVVDNIAY 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK---------HSGR--ISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVrGTDRRTRAAKATETGDQLSL-----QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDarLRLEAR 174
Cdd:TIGR01271 510 GLSY-DEYRYTSVIKACQLEEDIALfpekdKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD--VVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*...
gi 2068383214 175 TFLKKL-QLELGVTTVFVThDQAEALALADRIAVMSDG 211
Cdd:TIGR01271 587 IFESCLcKLMSNKTRILVT-SKLEHLKKADKILLLHEG 623
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-213 |
3.98e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 13 FPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKdvTRLSpgrrdvamVFQDYalfpHMS 92
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--VRMA--------VFSQH----HVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRG------TDRRTRAAKATetgdqLSLQGLMARRPA-ELSGGQQQRVALARAMACRPKVFLFDEPLSNL 165
Cdd:PLN03073 584 GLDLSSNPLLYMMrcfpgvPEQKLRAHLGS-----FGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068383214 166 DarlrLEA-RTFLKKLQLELGvTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:PLN03073 659 D----LDAvEALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-198 |
4.24e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGlETPTG--------GQIR-IGEK--DVT-------------- 69
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRgSGETiwDIKkhigyvssslhldy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 70 RLSPGRRDVamVFQDYalfphmsvVDNIAYPLKVrgTDRRTRaaKATETGDQLSLQGLMARRP-AELSGGQQQRVALARA 148
Cdd:PRK10938 350 RVSTSVRNV--ILSGF--------FDSIGIYQAV--SDRQQK--LAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRA 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068383214 149 MACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLELGVTTVFVTHDQAEA 198
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-180 |
5.05e-10 |
|
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: 58.02 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETP--TGGQIRIG--EKDVTRlspgRRDVAMVFQDYALFPHMSVVD 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINgrPLDKNF----QRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 96 NIAYPLKVRGtdrrtraakatetgdqlslqglmarrpaeLSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEART 175
Cdd:cd03232 99 ALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
....*
gi 2068383214 176 FLKKL 180
Cdd:cd03232 150 FLKKL 154
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-211 |
7.14e-10 |
|
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: 59.10 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRigekdvtrlSPGRrdVAMVFQDYALFPHmSVVDNIAY 99
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK---------HSGR--ISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVrGTDRRTRAAKATETGDQLSL-----QGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDarLRLEAR 174
Cdd:cd03291 121 GVSY-DEYRYKSVVKACQLEEDITKfpekdNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD--VFTEKE 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 2068383214 175 TFLKKL-QLELGVTTVFVThDQAEALALADRIAVMSDG 211
Cdd:cd03291 198 IFESCVcKLMANKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-194 |
7.56e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 1 MAQI--DVVELTKVFPGDVTALDGLTFTiqdgeFF-----ALLGPSGCGKSTLLRTIAGLETPTGGQirigekdvTRLSP 73
Cdd:PRK11819 2 MAQYiyTMNRVSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 74 GRRdVAMVFQDYALFPHMSVVDNI--AYPLKVRGTDR--RTRAAKATETGD-------QLSLQGLMA------------- 129
Cdd:PRK11819 69 GIK-VGYLPQEPQLDPEKTVRENVeeGVAEVKAALDRfnEIYAAYAEPDADfdalaaeQGELQEIIDaadawdldsqlei 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 130 -----RRP------AELSGGQQQRVALARAMACRPKVFLFDEPLSNLDAR--LRLEArtFLKKLQlelGvTTVFVTHD 194
Cdd:PRK11819 148 amdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvAWLEQ--FLHDYP---G-TVVAVTHD 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-235 |
2.06e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRlspgRRDVAMVFQDYA-------- 86
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCPRIAympqglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 87 -LFPHMSVVDNIAYPLKVRGTDRRTRAA------KATetgdqlslqGL--MARRPA-ELSGGQQQRVALARAMACRPKVF 156
Cdd:NF033858 88 nLYPTLSVFENLDFFGRLFGQDAAERRRridellRAT---------GLapFADRPAgKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 157 LFDEP------LS-----NLDARLRLEARtflkklQLELGVTTVFVthDQAEALalaDRIAVMSDGRIRQLDTAREVFRR 225
Cdd:NF033858 159 ILDEPttgvdpLSrrqfwELIDRIRAERP------GMSVLVATAYM--EEAERF---DWLVAMDAGRVLATGTPAELLAR 227
|
250
....*....|.
gi 2068383214 226 -PADTFVANFI 235
Cdd:NF033858 228 tGADTLEAAFI 238
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-230 |
2.92e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTR--LSPGRRDVAMVFQDYALFPHmSVVDNI 97
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 -----AYPLKVRG----TDRRTRAAKATETGDQLSLQGlmarrPAELSGGQQQRVALARAMACRPKVF-LFDEPLSNLDA 167
Cdd:PTZ00243 1405 dpfleASSAEVWAalelVGLRERVASESEGIDSRVLEG-----GSNYSVGQRQLMCMARALLKKGSGFiLMDEATANIDP 1479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 168 RLrleartflkKLQLELGVTTVFVTHD------QAEALALADRIAVMSDGRIRQLDTAREVFRRPADTF 230
Cdd:PTZ00243 1480 AL---------DRQIQATVMSAFSAYTvitiahRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-218 |
4.70e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.40 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELT-KVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETpTGGQIRIG--EKDVTRLSPGRRDVA 79
Cdd:cd03289 2 QMTVKDLTaKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDgvSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDYALFphmsvvdniayplkvRGTDRRT-------RAAKATETGDQLSLQGLMARRPAEL-----------SGGQQQ 141
Cdd:cd03289 81 VIPQKVFIF---------------SGTFRKNldpygkwSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 142 RVALARAMACRPKVFLFDEPLSNLDArlrLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDT 218
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-222 |
6.80e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQI-RIGEKDVTRLSPGrrdvamvfqdyaLFPHMSVVDNI 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISAG------------LSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLrleARTFL 177
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF---AQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 178 KKLQ--LELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:PRK13546 184 DKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-218 |
2.42e-08 |
|
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: 55.69 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 3 QIDVVELTKVFPGDVTA-LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETpTGGQIRIG--EKDVTRLSPGRRDVA 79
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDgvSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDYALFphmsvvdniayplkvRGTDRRTRAAKAT-------ETGDQLSLQGLMARRPAE-----------LSGGQQQ 141
Cdd:TIGR01271 1296 VIPQKVFIF---------------SGTFRKNLDPYEQwsdeeiwKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068383214 142 RVALARAMACRPKVFLFDEPLSNLDArlrLEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDT 218
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-210 |
2.54e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 25 FTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRLS---------------------PGRRD----VA 79
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeqlqklvsdewqrnntdmlsPGEDDtgrtTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 80 MVFQDYalfphmsvvdniayplkVRGTDRRTRAAKatetgdQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFD 159
Cdd:PRK10938 104 EIIQDE-----------------VKDPARCEQLAQ------QFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 160 EPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSD 210
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-213 |
1.47e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 8 ELTKVFP------GDV-------TALD-----GLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVT 69
Cdd:PRK10982 234 SLTQRFPdkenkpGEVilevrnlTSLRqpsirDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 70 RLSPG---RRDVAMVFQD------YALFP--HMSVVDNIAYPLKVRGTDRRTRAAKATetgdQLSLQGLMARRPAE---- 134
Cdd:PRK10982 314 NHNANeaiNHGFALVTEErrstgiYAYLDigFNSLISNIRNYKNKVGLLDNSRMKSDT----QWVIDSMRVKTPGHrtqi 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 135 --LSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEartfLKKLQLEL---GVTTVFVTHDQAEALALADRIAVMS 209
Cdd:PRK10982 390 gsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFE----IYQLIAELakkDKGIIIISSEMPELLGITDRILVMS 465
|
....
gi 2068383214 210 DGRI 213
Cdd:PRK10982 466 NGLV 469
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-205 |
2.82e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIgekdvtrlsPGRRDVAMVFQDYALFPHMSVVDNIAY 99
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQLAWVNQETPALPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 PLKVRGTDRRTRAAKATETGDQLS---------------------LQGL------MARRPAELSGGQQQRVALARAMACR 152
Cdd:PRK10636 88 DREYRQLEAQLHDANERNDGHAIAtihgkldaidawtirsraaslLHGLgfsneqLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068383214 153 PKVFLFDEPLSNLDarlrLEARTFLKKLQLELGVTTVFVTHDQAEALALADRI 205
Cdd:PRK10636 168 SDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-205 |
3.56e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 11 KVFPGDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTiaGLETPtgGQIRIgEKDVTRlsPGRRDVAMVFQDYALfph 90
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYAS--GKARL-ISFLPK--FSRNKLIFIDQLQFL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 91 msVVDNIAYplkvrgtdrrtraakatetgdqLSLQglmaRRPAELSGGQQQRVALARAMACRPK--VFLFDEPLSNLDAR 168
Cdd:cd03238 72 --IDVGLGY----------------------LTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 2068383214 169 lrlEARTFLKKLQ--LELGVTTVFVTHDQaEALALADRI 205
Cdd:cd03238 124 ---DINQLLEVIKglIDLGNTVILIEHNL-DVLSSADWI 158
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-217 |
6.49e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGeKDVTRLSPGRRDVAMVFQDYALFPHMSvv 94
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKLGYFAQHQLEFLRADESPLQHLA-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 95 dniayPLKVRGTDRRTRaakatetgDQLS---LQGLMARRPAE-LSGGQQQRVALARAMACRPKVFLFDEPLSNLDarlr 170
Cdd:PRK10636 400 -----RLAPQELEQKLR--------DYLGgfgFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD---- 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068383214 171 LEARTFLKKLQLELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLD 217
Cdd:PRK10636 463 LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-213 |
7.71e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 15 GDVTALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLE--TPTGGQIRIGEKDVTRLSPGRRdvamvfqdyalfPHMS 92
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER------------AHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRGTD-----RRTRAAKATETG--------------DQLSLQGL----MARRPAE-LSGGQQQRVALARA 148
Cdd:CHL00131 86 IFLAFQYPIEIPGVSnadflRLAYNSKRKFQGlpeldplefleiinEKLKLVGMdpsfLSRNVNEgFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 149 MACRPKVFLFDEPLSNLDA-RLRLEARTFLKKLQLELGVttVFVTHDQaealALADRIA-----VMSDGRI 213
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIdALKIIAEGINKLMTSENSI--ILITHYQ----RLLDYIKpdyvhVMQNGKI 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-205 |
9.83e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTL-LRTIAgletpTGGQIRIgekdVTRLSPGRRDvamvfqdyaLFPHMSV--VDN 96
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIY-----AEGQRRY----VESLSAYARQ---------FLGQMDKpdVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 97 I-----AYPLKVRGTDRRTRAAKATETG--DQLSLQ----------------GL----MARRPAELSGGQQQRVALARAM 149
Cdd:cd03270 73 IeglspAIAIDQKTTSRNPRSTVGTVTEiyDYLRLLfarvgirerlgflvdvGLgyltLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 150 ACRPK--VFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQaEALALADRI 205
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDE-DTIRAADHV 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-213 |
1.44e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 1.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068383214 135 LSGGQQQRVALARAMACRPKVFLFDEPLSNLDARLRLEARTFLKKLQLElGVTTVFVTHDQAEALALADRIAVMSDGRI 213
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-166 |
2.93e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 29 DGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIrigekdvtRLSPGRRdVAMVFQDYALFPHMSVVDNI----------- 97
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV--------SLDPNER-LGKLRQDQFAFEEFTVLDTVimghtelwevk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 -------AYP------------LKVR--GTDRRTRAAKATE----TGDQLSL-QGLMarrpAELSGGQQQRVALARAMAC 151
Cdd:PRK15064 97 qerdriyALPemseedgmkvadLEVKfaEMDGYTAEARAGElllgVGIPEEQhYGLM----SEVAPGWKLRVLLAQALFS 172
|
170
....*....|....*
gi 2068383214 152 RPKVFLFDEPLSNLD 166
Cdd:PRK15064 173 NPDILLLDEPTNNLD 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-167 |
5.86e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 5.86e-06
10 20 30
....*....|....*....|....*....|...
gi 2068383214 135 LSGGQQQRVALARAMACRPKVFLFDEPLSNLDA 167
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-205 |
7.50e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.06 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 29 DGEFFALLGPSGCGKSTLLRTI-AGL--ETPTGGQIRIGEKDVTRLSPGRRDVAMVFQ-----DYALFPHMSVVDNIAYp 100
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALkYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFEnangkKYTITRSLAILENVIF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 101 lkVRgtdrrtraakatetgdQLSLQGLMARRPAELSGGQQQ------RVALARAMACRPKVFLFDEPLSNLDA-RLRLEA 173
Cdd:cd03240 100 --CH----------------QGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESL 161
|
170 180 190
....*....|....*....|....*....|..
gi 2068383214 174 RTFLKKLQLELGVTTVFVTHDQaEALALADRI 205
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDE-ELVDAADHI 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-180 |
2.63e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAglETPTGGQIRIGEkdvtRLSPGR-------RDVAMVFQDYALFPHMS 92
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGD----RLVNGRpldssfqRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 93 VVDNIAYPLKVRGTDRRTRAAK---ATETGDQLSLQGL---MARRPAE-LSGGQQQRVALARAMACRPKVFLF-DEPLSN 164
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYadaVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSG 932
|
170
....*....|....*.
gi 2068383214 165 LDARLRLEARTFLKKL 180
Cdd:TIGR00956 933 LDSQTAWSICKLMRKL 948
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-222 |
4.73e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 19 ALDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRI-GEKDVTRLSPGrrdvamvfqdyaLFPHMSVVDNI 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSG------------LNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 98 AYPLKVRGTDRRTRAAKATETGDQLSLQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDarlrleaRTF- 176
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD-------QTFt 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2068383214 177 ---LKKLQ--LELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREV 222
Cdd:PRK13545 180 kkcLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
69-211 |
1.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 69 TRLSPGRRDVAMVFQDYALFPHMSVVDNIAYPLKVRGTDRRTRAAKAT--ETGDQLS-LQ--GL----MARRPAELSGGQ 139
Cdd:TIGR00630 414 TRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVlkEIRERLGfLIdvGLdylsLSRAAGTLSGGE 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068383214 140 QQRVALARAMACRPK--VFLFDEPLSNLDAR--LRLeARTfLKKLQlELGVTTVFVTHDQaEALALADRIAVMSDG 211
Cdd:TIGR00630 494 AQRIRLATQIGSGLTgvLYVLDEPSIGLHQRdnRRL-INT-LKRLR-DLGNTLIVVEHDE-DTIRAADYVIDIGPG 565
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-179 |
1.82e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 24 TFTIQDGEFFALLGPSGCGKSTLLRTIA-----GLetPTGGQIR------IGEK----------DVTRLSPGRRDVAMVF 82
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqevVGDDttalqcvlntDIERTQLLEEEAQLVA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 83 QDYAL-FPHMSVVDNIAYPLKVRG----------------TDRRTRAAKATETGDQLSLQGLMARRPAE-LSGGQQQRVA 144
Cdd:PLN03073 275 QQRELeFETETGKGKGANKDGVDKdavsqrleeiykrlelIDAYTAEARAASILAGLSFTPEMQVKATKtFSGGWRMRIA 354
|
170 180 190
....*....|....*....|....*....|....*
gi 2068383214 145 LARAMACRPKVFLFDEPLSNLDARLRLEARTFLKK 179
Cdd:PLN03073 355 LARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK 389
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-208 |
4.79e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 20 LDGLTFTIQDGEFFALLGPSGCGKSTLLRTIAgletptggqirigekdvtrlspgrrdvamvfqdYALFPHMSVVdniay 99
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSAT----- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 100 plkvrgtdRRTRAAKATETGDQLSLQgLMARRPaELSGGQQQRVALARAMA---CRPKVF-LFDEPLSNLDAR--LRLEA 173
Cdd:cd03227 53 --------RRRSGVKAGCIVAAVSAE-LIFTRL-QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRdgQALAE 122
|
170 180 190
....*....|....*....|....*....|....*
gi 2068383214 174 RTflkKLQLELGVTTVFVTHDQaEALALADRIAVM 208
Cdd:cd03227 123 AI---LEHLVKGAQVIVITHLP-ELAELADKLIHI 153
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
119-205 |
1.10e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.94 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 119 GDQLSLQglmarrpaELSGGQQQRVALARAMA---CRPKVF-LFDEPLSNLDArlrlEARTFLKKLQLELGVTTVFV-TH 193
Cdd:cd03272 151 DEQQEMQ--------QLSGGQKSLVALALIFAiqkCDPAPFyLFDEIDAALDA----QYRTAVANMIKELSDGAQFItTT 218
|
90
....*....|..
gi 2068383214 194 DQAEALALADRI 205
Cdd:cd03272 219 FRPELLEVADKF 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-205 |
2.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 2.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068383214 130 RRPAELSGGQQQRVALARAMACRPK--VFLFDEPLSNLDARLRLEARTFLKKLQlELGVTTVFVTHDQaEALALADRI 205
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEHDE-QMISLADRI 547
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
21-58 |
3.83e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 3.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2068383214 21 DGLTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTG 58
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-230 |
5.15e-03 |
|
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: 37.97 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 27 IQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRIGEKDVTRL--SPGRRDVAMVFQDYALFPHmSVVDNIAyPLKVR 104
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILFSG-SIRFNLD-PECKC 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068383214 105 GTDRRTRAAKATETGDQLS-----LQGLMARRPAELSGGQQQRVALARAMACRPKVFLFDEPLSNLDarlrLEARTFLKK 179
Cdd:cd03288 122 TDDRLWEALEIAQLKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID----MATENILQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068383214 180 LQL-ELGVTTVFVTHDQAEALALADRIAVMSDGRIRQLDTAREVFRRPADTF 230
Cdd:cd03288 198 VVMtAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
17-75 |
8.68e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 8.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068383214 17 VTALDG-----LTFTIQDGEFFALLGPSGCGKSTLLRTIAGLETPTGGQIRigEKDvtrlSPGR 75
Cdd:PRK01889 177 VSALDGegldvLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR--EDD----SKGR 234
|
|
| |
