|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-341 |
2.39e-124 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 360.95 E-value: 2.39e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIG 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMrgvPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGDA 237
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 238 VILPAQLAAGYA--VCALG---EVPTDNAQATGQ-GRVMMRPEQLRVTAcAAHESPIS--ILDVDFTGQLSTLTLGLAGQ 309
Cdd:COG3842 240 NLLPGTVLGDEGggVRTGGrtlEVPADAGLAAGGpVTVAIRPEDIRLSP-EGPENGLPgtVEDVVFLGSHVRYRVRLGDG 318
|
330 340 350
....*....|....*....|....*....|....
gi 697052228 310 QQPVILKTVSQ-PGWNPGTAVRIDI-AGTARVFE 341
Cdd:COG3842 319 QELVVRVPNRAaLPLEPGDRVGLSWdPEDVVVLP 352
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-340 |
3.50e-113 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 332.50 E-value: 3.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFdenSFVPAHLRRIGF 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---TNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLD---GTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRvrpPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGDAV 238
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 239 ILPAQLAAGYAVCALGEVPTDNAQATGQGRVMMRPEQLRVTACAAHESPIS--ILDVDFTGQLSTLTLGLAGQQQPVILK 316
Cdd:COG1118 239 VLRGRVIGGQLEADGLTLPVAEPLPDGPAVAGVRPHDIEVSREPEGENTFPatVARVSELGPEVRVELKLEDGEGQPLEA 318
|
330 340
....*....|....*....|....*....
gi 697052228 317 TVSQPGW-----NPGTAVRIDIAgTARVF 340
Cdd:COG1118 319 EVTKEAWaelglAPGDPVYLRPR-PARVF 346
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-340 |
1.75e-98 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 295.06 E-value: 1.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHlRRIG 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR---DVTDLPPKD-RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGL---DGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLklrKVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGD- 236
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 237 -AVILPAQLAAGYAVCALGEVPTDNAQATGQGR---VMMRPEQLRVTACAAHESPISILDVDFTGQLSTLTLGLAGqqQP 312
Cdd:COG3839 238 pMNLLPGTVEGGGVRLGGVRLPLPAALAAAAGGevtLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLGG--QE 315
|
330 340
....*....|....*....|....*....
gi 697052228 313 VILKTVSQPGWNPGTAVRIDI-AGTARVF 340
Cdd:COG3839 316 LVARVPGDTRLRPGDTVRLAFdPERLHLF 344
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
2.48e-97 |
|
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: 287.11 E-value: 2.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIGF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLD---GTRHEKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKlrgVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-319 |
7.19e-85 |
|
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: 260.35 E-value: 7.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRRIGF 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI----TRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNrgmGRAEVAERVAELLDLVGLPGS-ERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGDAV 238
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 239 ILPAQLAAGYAVcALGEVPTDNAQATGQ----GRVMMRPEQLRVT-ACAAHES-PISILDVDFTGQLSTLTLGLAGQQQP 312
Cdd:TIGR03265 240 WLPGTRGGGSRA-RVGGLTLACAPGLAQpgasVRLAVRPEDIRVSpAGNAANLlLARVEDMEFLGAFYRLRLRLEGLPGQ 318
|
....*..
gi 697052228 313 VILKTVS 319
Cdd:TIGR03265 319 ALVADVS 325
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-235 |
2.51e-83 |
|
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: 252.16 E-value: 2.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIGF 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDGTRHEK---RQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKaeiKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLG 235
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-278 |
1.05e-80 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 250.25 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIGF 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH----VPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLdgtRHEK------RQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGL---RMQKtpaaeiTPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 156 LLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLG 235
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 236 DAVILPAQLAAGYA-----------VCalgEVPTDNAQATGQG-RVMMRPEQLRV 278
Cdd:PRK09452 247 EINIFDATVIERLDeqrvranvegrEC---NIYVNFAVEPGQKlHVLLRPEDLRV 298
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
2.86e-79 |
|
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: 241.86 E-value: 2.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdENSFVPAHLRRIGF 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLD-------GTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRvkprserPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
..
gi 697052228 235 GD 236
Cdd:cd03296 238 GE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
6.43e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 241.92 E-value: 6.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfVPAHL 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-------VTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPS 153
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLELrgvPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 154 LMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMrSGRFTQVGTPYDV 221
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL-SARPGRIVEEIDV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
6.18e-77 |
|
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: 235.44 E-value: 6.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSD----VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfVPAHLR 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-------VTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 RIGFVPQEGALFPHLNVADNIAWGLDGTRH---EKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVpkaEARERAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVM--RSGR 211
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGR 211
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-240 |
6.81e-76 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 233.54 E-value: 6.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdENSFVPAHLRRIGF 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ----DATRVHARDRKIGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDGTRH---EKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:TIGR00968 77 VFQHYALFKHLTVRDNIAFGLEIRKHpkaKIKARVEELLELVQLEG-LGDRYPNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGDAV 238
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
|
..
gi 697052228 239 IL 240
Cdd:TIGR00968 236 VL 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-235 |
1.53e-74 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 229.88 E-value: 1.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIA----WGLDGTRHEKRQRVEALMEMVSL-DRqlATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTlapiKVKKMSKAEAEERAMELLERVGLaDK--ADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 156 LLDEPFSALD---TG--LRAMTRkatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEET 230
Cdd:COG1126 159 LFDEPTSALDpelVGevLDVMRD------LAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
....*
gi 697052228 231 ALFLG 235
Cdd:COG1126 233 RAFLS 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-311 |
2.98e-74 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 233.05 E-value: 2.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRRIGF 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDG-TRHEK------RQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVlPRRERpnaaaiKAKVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 235 G-----DAVILPAQLAAGYAVCALGEVPTDnaqatgQGRV--MMRPEQLRVTACAAHES--PISILDVDFTGQLSTLTLG 305
Cdd:PRK10851 238 GevnrlQGTIRGGQFHVGAHRWPLGYTPAY------QGPVdlFLRPWEVDISRRTSLDSplPVQVLEVSPKGHYWQLVVQ 311
|
....*.
gi 697052228 306 LAGQQQ 311
Cdd:PRK10851 312 PLGWYN 317
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-235 |
4.01e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 228.44 E-value: 4.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQV-LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRR- 78
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD---PVELRRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIA-------WgldgTRHEKRQRVEALMEMVSLDR-QLATHWPHEISGGQQQRVALARALAQ 150
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIAtvprllgW----DKERIRARVDELLELVGLDPeEYRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 RPSLMLLDEPFSALDtglrAMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:COG1125 154 DPPILLMDEPFGALD----PITREQLQDELlrlqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPA 229
|
....*....
gi 697052228 227 DEETALFLG 235
Cdd:COG1125 230 NDFVADFVG 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-309 |
9.89e-72 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 226.52 E-value: 9.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvpAHLRRIGF 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS----IQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSL----DRqlathWPHEISGGQQQRVALARALAQRPSL 154
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMlgvPKEERKQRVKEALELVDLagfeDR-----YVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 235 GDAVILPAQLAAGYAVCALGEVPTDNAQAT----GQGRVMMRPEQLRVTACAAHESPISILDVDFTGQLSTLTLGLAGQ 309
Cdd:PRK11432 238 GDANIFPATLSGDYVDIYGYRLPRPAAFAFnlpdGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQ 316
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-314 |
6.76e-71 |
|
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: 223.52 E-value: 6.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 32 IVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRRIGFVPQEGALFPHLNVADNIAWGL--DGT-RHE 108
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLkmRKVpRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 109 KRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASI 188
Cdd:TIGR01187 77 IKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 189 LVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGDAVILPAQL---AAGYAVCALGEVPTDNA---- 261
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVierKSEQVVLAGVEGRRCDIytdv 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 262 --QATGQGRVMMRPEQLRVTACAAHES----PISILDVDFTGQLSTLTLGLAGQQQPVI 314
Cdd:TIGR01187 236 pvEKDQPLHVVLRPEKIVIEEEDEANSsnaiIGHVIDITYLGMTLEVHVRLETGQKVLV 294
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
1.22e-70 |
|
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: 219.05 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIGF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGL---DGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLklrKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-235 |
1.26e-69 |
|
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: 217.20 E-value: 1.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQvLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIGF 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDGTRHEKRQRVEALMEMVS-------LDRQLAThwpheISGGQQQRVALARALAQRPSL 154
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEmlgidhlLNRKPET-----LSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
.
gi 697052228 235 G 235
Cdd:cd03299 231 G 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-216 |
2.73e-69 |
|
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: 215.62 E-value: 2.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 19 SLNLS-VAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD--ENSFVPAHLRRIGFVPQEGALFPHLNVA 95
Cdd:cd03297 14 TLKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrKKINLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWGLDGTRH-EKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRK 174
Cdd:cd03297 94 ENLAFGLKRKRNrEDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 697052228 175 ATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-235 |
3.95e-69 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 220.86 E-value: 3.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRRIG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQdklPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLG 235
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-319 |
8.47e-67 |
|
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: 214.19 E-value: 8.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELtAISKSFSDVQvLDsLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENS--FVPAHLRR 78
Cdd:COG4148 2 MLEV-DFRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiFLPPHRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLDGTRHEKRQ-RVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRiSFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 158 DEPFSALDtglraMTRKatADLL-------AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEET 230
Cdd:COG4148 158 DEPLAALD-----LARK--AEILpylerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 231 ALFLGDAVILPAQLAA-----GYAVCALGEVP---TDNAQATGQG---RVMMR--------PEQL--------RVTACAA 283
Cdd:COG4148 231 AGGEEAGSVLEATVAAhdpdyGLTRLALGGGRlwvPRLDLPPGTRvrvRIRARdvslalepPEGSsilnilpgRVVEIEP 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 697052228 284 HESPISILDVDFTGQ--LSTLT------LGLA-GQQQPVILKTVS 319
Cdd:COG4148 311 ADGGQVLVRLDLGGQtlLARITrrsadeLGLApGQTVYAQIKSVA 355
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-235 |
3.52e-66 |
|
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: 208.69 E-value: 3.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQ-VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR-I 79
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE---DIREQDPVELRRkI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNIA-------WGldgtRHEKRQRVEALMEMVSLD-RQLATHWPHEISGGQQQRVALARALAQR 151
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAlvpkllkWP----KEKIRERADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 152 PSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETA 231
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
....
gi 697052228 232 LFLG 235
Cdd:cd03295 234 EFVG 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-218 |
1.60e-65 |
|
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: 206.75 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHL---- 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLS---EKELyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPHLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRP 152
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLrehtDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 153 SLMLLDEPFSALDtglrAMTRKATADLLAE----AGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:COG1127 161 EILLYDEPTAGLD----PITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-211 |
2.98e-65 |
|
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: 203.96 E-value: 2.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIGF 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLdgtrhekrqrvealmemvsldrqlathwpheiSGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL--------------------------------SGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 697052228 162 SALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-211 |
4.23e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 205.28 E-value: 4.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RR--IGFVPQEGALFPHLNVADNIA--WGLDGT-RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQR 151
Cdd:COG1136 84 RRrhIGFVFQFFNLLPELTALENVAlpLLLAGVsRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 152 PSLMLLDEPFSALDTglraMTRKATADLL----AEAGVASILVTHDQnEALSFATQVAVMRSGR 211
Cdd:COG1136 163 PKLILADEPTGNLDS----KTGEEVLELLrelnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
5.83e-65 |
|
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: 213.61 E-value: 5.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF-----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAH 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 LRR-IGFVPQ--EGALFPHLNVADNIAWGLD----GTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARAL 148
Cdd:COG1123 340 LRRrVQMVFQdpYSSLNPRMTVGDIIAEPLRlhglLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 149 AQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDE 228
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
..
gi 697052228 229 ET 230
Cdd:COG1123 500 YT 501
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
6.15e-62 |
|
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: 198.10 E-value: 6.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS----DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdENSFVPAHL 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQ--EGALFPHLNVADNIAWGLDGTRH-EKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPS 153
Cdd:COG1124 79 RRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLpDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 154 LMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALF 233
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
....*....
gi 697052228 234 LGDAVILPA 242
Cdd:COG1124 239 LAASLAFER 247
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-211 |
1.02e-60 |
|
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: 193.86 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSD----VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLR 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 R--IGFVPQEGALFPHLNVADNIAWGLDGTRH---EKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRP 152
Cdd:cd03255 81 RrhIGFVFQSFNLLPDLTALENVELPLLLAGVpkkERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEAlSFATQVAVMRSGR 211
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-235 |
1.21e-59 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 191.51 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVldSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRRIG 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLD-GTR--HEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRpGLKltAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLG 235
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-221 |
6.43e-59 |
|
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: 189.64 E-value: 6.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLR-RIG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLML 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrehtRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 157 LDEPFSALDtglrAMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:cd03261 160 YDEPTAGLD----PIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-239 |
4.43e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 187.58 E-value: 4.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVpahLRRIGF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV---RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAW-----GLDgtRHEKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLML 156
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFfarlyGLP--RKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 157 LDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPydvytrpvDEETALFLGD 236
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP--------DELKARLLED 225
|
...
gi 697052228 237 AVI 239
Cdd:COG1131 226 VFL 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
5.72e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.60 E-value: 5.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfVPAHLRRIG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-------PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGAL---FPhLNVADNIAWGLDGTR-------HEKRQRVEALMEMVSL----DRQLAthwphEISGGQQQRVALAR 146
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRDVVLMGRYGRRglfrrpsRADREAVDEALERVGLedlaDRPIG-----ELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 147 ALAQRPSLMLLDEPFSALDtglrAMTRKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGRFTQvGTPYDVYT 223
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVD----AATEEALYELLRElrrEGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLT 227
|
....*..
gi 697052228 224 RPVDEET 230
Cdd:COG1121 228 PENLSRA 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-211 |
1.62e-57 |
|
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: 185.43 E-value: 1.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIGF 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNI------AWGLDgtRHEKRQRVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:cd03262 81 VFQQFNLFPHLTVLENItlapikVKGMS--KAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 156 LLDEPFSALD---TG--LRAMTRkatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03262 158 LFDEPTSALDpelVGevLDVMKD------LAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-234 |
3.20e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 182.99 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWG----LDGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLML 156
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGplrvRGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 157 LDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
5.09e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 5.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR-IG 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL---SAMPPPEWRRqVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHlNVADNIA--WGLDGtRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPfpFQLRE-RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRF 212
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-223 |
1.35e-55 |
|
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: 181.78 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHL-RRI 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL---ASLSRRELaRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNIAWG-------LDGTRHEKRQRVEALMEMVSL----DRQLathwpHEISGGQQQRVALARAL 148
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREAVEEALERTGLehlaDRPV-----DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 149 AQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-277 |
1.43e-55 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 185.05 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS-DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHlRRI 79
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPAD-RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNIAWGLD--GT-RHEKRQRVEALMEMVS----LDRQlathwPHEISGGQQQRVALARALAQRP 152
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKirGMpKAEIEERVAEAARILEleplLDRK-----PRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETAL 232
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVAS 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 233 FLGDAVI--LPAQLAAGYAVCALG---EVPTDNAQATGQGRVM---MRPEQLR 277
Cdd:PRK11650 234 FIGSPAMnlLDGRVSADGAAFELAggiALPLGGGYRQYAGRKLtlgIRPEHIA 286
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
5.32e-55 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 179.45 E-value: 5.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSD-VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIG 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQ--EGALFpHLNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:COG1122 79 LVFQnpDDQLF-APTVEEDVAFGpenLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 156 LLDEPFSALDtglrAMTRKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:COG1122 157 VLDEPTAGLD----PRGRRELLELLKRlnkEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-211 |
6.83e-55 |
|
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: 179.24 E-value: 6.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD----VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD-ENSFVPAH 75
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 LRRIGFVPQE--GALFPHLNVADNIA-----WGLDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARAL 148
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 149 AQRPSLMLLDEPFSALDtglrAMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03257 161 ALNPKLLIADEPTSALD----VSVQAQILDLLkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-246 |
7.19e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 182.58 E-value: 7.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS----DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHL 76
Cdd:COG1135 1 MIELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL---TALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 R----RIGFVPQEGALFPHLNVADNIA-----WGLDgtRHEKRQRVEALMEMVSL-DRqlATHWPHEISGGQQQRVALAR 146
Cdd:COG1135 78 RaarrKIGMIFQHFNLLSSRTVAENVAlpleiAGVP--KAEIRKRVAELLELVGLsDK--ADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 147 ALAQRPSLMLLDEPFSALDTGlramTRKATADLLAEA----GVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPE----TTRSILDLLKDInrelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
250 260
....*....|....*....|....*.
gi 697052228 223 TRPVDEETALFLGDAV--ILPAQLAA 246
Cdd:COG1135 230 ANPQSELTRRFLPTVLndELPEELLA 255
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-198 |
3.00e-54 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 176.90 E-value: 3.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPD---TGRIVMQGRTLFDensfVPAHLR 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA----LPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 RIGFVPQEGALFPHLNVADNIAWGLDGT--RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFALPPTigRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 697052228 156 LLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEAL 198
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-211 |
3.56e-53 |
|
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: 174.19 E-value: 3.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 3 ELTAISKSFSD--VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIG 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--LKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQ--EGALFpHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQRPSLM 155
Cdd:cd03225 79 LVFQnpDDQFF-GPTVEEEVAFGLENlglPEEEIEERVEEALELVGLEGLRDRS-PFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 156 LLDEPFSALDtglrAMTRKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03225 157 LLDEPTAGLD----PAGRRELLELLKKlkaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-235 |
6.83e-53 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 178.30 E-value: 6.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 4 LTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfVPAHLRRIGFVP 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 84 QEGALFPHLNVADNIAWGLD---GTRHEKRQRVEALMEMVSL----DRQlathwPHEISGGQQQRVALARALAQRPSLML 156
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKlagAKKEEINQRVNQVAEVLQLahllDRK-----PKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 157 LDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLG 235
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-211 |
2.11e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 172.54 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS-DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD-ENSFVPAHLRR 78
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLD--GT-RHEKRQRVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRvtGKsRKEIRRRVREVLDLVGLSDK-AKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 156 LLDEPFSALD--TGLRAMtrkataDLLAE---AGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:COG2884 160 LADEPTGNLDpeTSWEIM------ELLEEinrRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-229 |
2.23e-52 |
|
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: 173.12 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRRIG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNI-----AWGLDGtrHEKRQRVEALMEMVSLDRQLATHWpHEISGGQQQRVALARALAQRPSLM 155
Cdd:COG4555 78 VLPDERGLYDRLTVRENIryfaeLYGLFD--EELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 156 LLDEPFSALDtglrAMTRKATADLL---AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEE 229
Cdd:COG4555 155 LLDEPTNGLD----VMARRLLREILralKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-236 |
2.35e-52 |
|
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: 173.98 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 5 TAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLR-----RI 79
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ---DIAAMSRKELRelrrkKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNIAWGLD--G-TRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLML 156
Cdd:cd03294 105 SMVFQSFALLPHRTVLENVAFGLEvqGvPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 157 LDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGD 236
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
1.67e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 171.58 E-value: 1.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfvPAHL 76
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-----PGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RriGFVPQEGALFPHLNVADNIAWGLD--GT-RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPS 153
Cdd:COG4525 78 R--GVVFQKDALLPWLNVLDNVAFGLRlrGVpKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 154 LMLLDEPFSALDtglrAMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVM--RSGRFTQV 215
Cdd:COG4525 155 FLLMDEPFGALD----ALTREQMQELLldvwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
1.69e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 171.01 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF-SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLR-- 77
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV---TALRGRALRrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 --RIGFVPQEGALFPHLNVADNIAWGLDGTRH-----------EKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVAL 144
Cdd:COG3638 79 rrRIGMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsllglfppEDRERALEALERVGLA-DKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 145 ARALAQRPSLMLLDEPFSALD--TGLRAMtrkataDLLAEA----GVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDpkTARQVM------DLLRRIaredGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-218 |
9.61e-51 |
|
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: 168.51 E-value: 9.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF-----ETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPhLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLDRQLATH-WPHEISGGQQQRVALARALAQR 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLrlhgIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 152 PSLMLLDEPFSALDtglramtRKATA---DLLAEAG--VASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:cd03260 160 PEVLLLDEPTSALD-------PISTAkieELIAELKkeYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
2.13e-50 |
|
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: 165.65 E-value: 2.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPahlRRIGF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIawgldgtrhekrqrvealmemvsldrqlathwphEISGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 697052228 162 SALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRF 212
Cdd:cd03230 124 SGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-226 |
2.55e-50 |
|
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: 171.06 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 20 LNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD--ENSFVPAHLRRIGFVPQEGALFPHLNVADN 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 98 IAWGLDGTRHEKRQ-RVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKAT 176
Cdd:TIGR02142 96 LRYGMKRARPSERRiSFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 697052228 177 ADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-211 |
2.93e-50 |
|
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: 167.23 E-value: 2.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD----VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLF--DENSFvpA 74
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDAR--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HLRR--IGFVPQEGALFPHLNVADNIAWGLDGTRH-EKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQR 151
Cdd:COG4181 86 RLRArhVGFVFQSFQLLPTLTALENVMLPLELAGRrDARARARALLERVGLG-HRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 152 PSLMLLDEPFSALDTGlramTRKATADLL----AEAGVASILVTHDQNEALSFATQVAvMRSGR 211
Cdd:COG4181 165 PAILFADEPTGNLDAA----TGEQIIDLLfelnRERGTTLVLVTHDPALAARCDRVLR-LRAGR 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-225 |
4.02e-49 |
|
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: 164.29 E-value: 4.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD----VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGR--TLFDENSFVPA 74
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdlTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HlRRIGFVPQEGALFPHLNVADNIA-----WGLDgtRHEKRQRVEALMEMVSL-DRqlATHWPHEISGGQQQRVALARAL 148
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVAlpleiAGVP--KAEIEERVLELLELVGLeDK--ADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 149 AQRPSLMLLDEPFSALDtglrAMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:cd03258 156 ANNPKVLLCDEATSALD----PETTQSILALLrdinRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 697052228 225 P 225
Cdd:cd03258 232 P 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-309 |
1.11e-48 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 170.85 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF--SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPD---TGRIVMQGRTLFDENSFVPAh 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 lRRIGFVPQE--GALFPhLNVADNIAWGL---DGTRHEKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQ 150
Cdd:COG1123 83 -RRIGMVFQDpmTQLNP-VTVGDQIAEALenlGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRpvdeet 230
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 231 alflgdavilPAQLAagyAVCALGEVPTDNAQATGQGRVMMRPEQLRVTACAAHESPISIL-DVDFT---GQlstlTLGL 306
Cdd:COG1123 234 ----------PQALA---AVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVdDVSLTlrrGE----TLGL 296
|
...
gi 697052228 307 AGQ 309
Cdd:COG1123 297 VGE 299
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-207 |
2.83e-48 |
|
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: 161.55 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 3 ELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvpahlRRIGFV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-------KRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 83 PQEGAL---FPhLNVADNIAWGLDGT-------RHEKRQRVEALMEMVSL----DRQLAthwphEISGGQQQRVALARAL 148
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGLYGHkglfrrlSKADKAKVDEALERVGLselaDRQIG-----ELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 149 AQRPSLMLLDEPFSALDtglrAMTRKATADLLAE---AGVASILVTHDQNEALSFATQVAVM 207
Cdd:cd03235 148 VQDPDLLLLDEPFAGVD----PKTQEDIYELLRElrrEGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-236 |
4.39e-48 |
|
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: 165.80 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLR-----RIGFVPQEGALFPH 91
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQS---PVELRevrrkKIGMVFQQFALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLD---GTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGL 168
Cdd:TIGR01186 86 MTILQNTSLGPEllgWPEQERKEKALELLKLVGLE-EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 169 RAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGD 236
Cdd:TIGR01186 165 RDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-228 |
3.91e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 163.74 E-value: 3.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 21 NLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLR-----RIGFVPQEGALFPHLNVA 95
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLS---KKELRelrrkKMSMVFQHFALLPHRTVL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWGLD--GT-RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD------- 165
Cdd:COG4175 124 ENVAFGLEiqGVpKAERRERAREALELVGLA-GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDplirrem 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 166 ----TGLRAMTRKATadllaeagvasILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDE 228
Cdd:COG4175 203 qdelLELQAKLKKTI-----------VFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAND 258
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-225 |
5.35e-47 |
|
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: 160.31 E-value: 5.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR-IGFVPQ--EGALFpH 91
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKkVGLVFQfpEHQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDtgl 168
Cdd:TIGR04521 98 ETVYKDIAFGpknLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD--- 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 169 rAMTRKATADLLA----EAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:TIGR04521 175 -PKGRKEILDLFKrlhkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-162 |
1.33e-46 |
|
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: 155.11 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIGFVPQEGALFPHLNVAD 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 97 NIAWGLDG---TRHEKRQRVEALMEMVSLDRQLATHW---PHEISGGQQQRVALARALAQRPSLMLLDEPFS 162
Cdd:pfam00005 79 NLRLGLLLkglSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
1.56e-46 |
|
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: 156.87 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDEnsfVPAHLRRIG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA---REDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAW--GLDGTRHEkRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFwaALYGLRAD-REAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAeAGVASILVTHD 193
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQ 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-211 |
3.94e-46 |
|
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: 156.11 E-value: 3.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 20 LNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdENSFVPAHLRRIGFVPQEGALFPHLNVADNIA 99
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 100 WGLDGTRH---EKRQRVEALMEMVSLDRQLAtHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKAT 176
Cdd:cd03298 93 LGLSPGLKltaEDRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*
gi 697052228 177 ADLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-228 |
2.17e-45 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 155.03 E-value: 2.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSF-SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQG-RTLFDENSFVPAHLRRI 79
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNIAWGLDGTRH-----------EKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARAL 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRStwrslfglfpkEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 149 AQRPSLMLLDEPFSALDTglrAMTRKATADLLA---EAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:cd03256 160 MQQPKLILADEPVASLDP---ASSRQVMDLLKRinrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
...
gi 697052228 226 VDE 228
Cdd:cd03256 237 LDE 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-217 |
9.19e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.80 E-value: 9.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSFVPAHLRRIG 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDGTRH------EKRQRVEALMEMVSLD---RQLAThwphEISGGQQQRVALARALAQR 151
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGglidwrAMRRRARELLARLGLDidpDTPVG----DLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 152 PSLMLLDEPFSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRFtqVGT 217
Cdd:COG1129 159 ARVLILDEPTASL-------TEREVERLfriirrLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-226 |
1.27e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 153.35 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHL-RRI 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL---AAWSPWELaRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGAL-FPhLNVADNIAWGLD---GTRHEKRQRVEALMEMVSLDRQLATHWPhEISGGQQQRVALARALAQ----- 150
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRAphgSSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGGEQQRVQLARVLAQlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 --RPSLMLLDEPFSALDTG--LRAMTrkaTADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAhqHAVLR---LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-221 |
5.00e-44 |
|
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: 151.44 E-value: 5.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLR-RIG 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI----TGLPPHEIaRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVP--QEGALFPHLNVADNI-------------AWGLDGTRHEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALA 145
Cdd:cd03219 77 IGRtfQIPRLFPELTVLENVmvaaqartgsgllLARARREEREARERAEELLERVGLADLADRP-AGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 146 RALAQRPSLMLLDEPFSaldtGLRAMTRKATADL---LAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:cd03219 156 RALATDPKLLLLDEPAA----GLNPEETEELAELireLRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-234 |
1.08e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 151.06 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRI------VMQGRTLFDENSFVPA 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HLRRIGFVPQEGALFPHLNVADNIAWGLDGTRHEKRQRVEA----LMEMVSLDRQlATHWPHEISGGQQQRVALARALAQ 150
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATArareLLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRkATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEET 230
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVL-NTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....
gi 697052228 231 ALFL 234
Cdd:PRK11264 241 RQFL 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-216 |
1.31e-43 |
|
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: 148.35 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 3 ELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHL-RRIGF 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL---ASLSPKELaRKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQegALfphlnvadniawgldgtrhekrqrveALMEMVSL-DRQLathwpHEISGGQQQRVALARALAQRPSLMLLDEP 160
Cdd:cd03214 78 VPQ--AL--------------------------ELLGLAHLaDRPF-----NELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 161 FSALDTG--------LRAMTRkatadllaEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03214 125 TSHLDIAhqiellelLRRLAR--------ERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
1.62e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 150.72 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL-FDEN---SFVPA-- 74
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrLKPDrdgELVPAdr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 ----HLR-RIGFVPQEGALFPHLNVADNIAWG----LDGTRHEKRQRVEALMEMVSL-DRqlATHWPHEISGGQQQRVAL 144
Cdd:COG4598 88 rqlqRIRtRLGMVFQSFNLWSHMTVLENVIEApvhvLGRPKAEAIERAEALLAKVGLaDK--RDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 145 ARALAQRPSLMLLDEPFSALD---TG--LRAMtRKatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPY 219
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDpelVGevLKVM-RD-----LAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*
gi 697052228 220 DVYTRPVDEETALFL 234
Cdd:COG4598 240 EVFGNPKSERLRQFL 254
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-211 |
1.78e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 149.73 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 21 NLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHlRRIGFVPQEGALFPHLNVADNIAW 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSR-RPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 101 GLD-GTR--HEKRQRVEALMEMVSLDRQLaTHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATA 177
Cdd:PRK10771 95 GLNpGLKlnAAQREKLHAIARQMGIEDLL-ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....
gi 697052228 178 DLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-223 |
1.95e-43 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 150.31 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHL-RRI 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL---ADWSPAELaRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGAL-FPhLNVADNIAWGLD---GTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQ----- 150
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMGRAphgLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 151 -RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-211 |
1.97e-43 |
|
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: 147.01 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 3 ELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvPAHLRRIGFV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--EELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 83 PQegalfphlnvadniawgldgtrhekrqrvealmemvsldrqlathwpheISGGQQQRVALARALAQRPSLMLLDEPFS 162
Cdd:cd00267 79 PQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 697052228 163 ALDTGLRAMTRKATADLLAEaGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-211 |
2.28e-43 |
|
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: 147.53 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSD--VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR- 78
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV---DLRDLDLESLRKn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFpHLNVADNIawgldgtrhekrqrvealmemvsldrqlathwpheISGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVasILVTHDQnEALSFATQVAVMRSGR 211
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTV--IVIAHRL-STIRDADRIIVLDDGR 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
3.22e-43 |
|
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: 149.80 E-value: 3.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLR-RI 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI----TGLPPHRIaRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 G----FvpQEGALFPHLNVADNIA------------------WGLDGTRHEKRQRVEALMEMVSLDRqLATHWPHEISGG 137
Cdd:COG0411 80 GiartF--QNPRLFPELTVLENVLvaaharlgrgllaallrlPRARREEREARERAEELLERVGLAD-RADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 138 QQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....
gi 697052228 218 PYDV 221
Cdd:COG0411 237 PAEV 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-229 |
3.38e-43 |
|
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: 149.15 E-value: 3.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfvPAHLRRIGFvpQEGALFPHLNVAD 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-----PGPDRMVVF--QNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 97 NIAWGLDGTRH-----EKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDtglrAM 171
Cdd:TIGR01184 74 NIALAVDRVLPdlsksERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD----AL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 172 TRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV-YTRPVDEE 229
Cdd:TIGR01184 149 TRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDRL 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-218 |
4.14e-43 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 158.07 E-value: 4.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR-IGFVPQEGALFpHLNV 94
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQIDPASLRRqIGVVLQDVFLF-SGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDGTRHEkrqRVEALMEMVSLDRQLATHwPH-----------EISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:COG2274 566 RENITLGDPDATDE---EIIEAARLAGLHDFIEAL-PMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 164 LDtglrAMTRKATADLLAE--AGVASILVTHDQnEALSFATQVAVMRSGRFTQVGTP 218
Cdd:COG2274 642 LD----AETEAIILENLRRllKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTH 693
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
1.12e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.49 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtLFDENSFVPAHLRRIG 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV------LWDGEPLDPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAW-----GLDgtRHEKRQRVEALmemvsLDR-QLATHWPHEI---SGGQQQRVALARALAQR 151
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVYlarlkGLS--KAEAKRRADEW-----LERlGLGDRANKKVeelSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 152 PSLMLLDEPFSALD--------TGLRAmtrkatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:COG4152 148 PELLILDEPFSGLDpvnvellkDVIRE---------LAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-246 |
1.43e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 150.72 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS----DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGR--TLFDENSFVPA 74
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HlRRIGFVpqegalFPHLN------VADNIAWGL--DGT-RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALA 145
Cdd:PRK11153 81 R-RQIGMI------FQHFNllssrtVFDNVALPLelAGTpKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 146 RALAQRPSLMLLDEPFSALDTGlramTRKATADLLA----EAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPA----TTRSILELLKdinrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250 260
....*....|....*....|....*..
gi 697052228 222 YTRPVDEETALFLGDA--VILPAQLAA 246
Cdd:PRK11153 229 FSHPKHPLTREFIQSTlhLDLPEDYLA 255
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-194 |
4.32e-42 |
|
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: 145.45 E-value: 4.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 4 LTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR--IGF 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRekLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGLDGTR---HEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKlskKEKREKKKEALEKVGLNLKLKQK-IYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 697052228 159 EPFSALDTglraMTRKATADLL---AEAGVASILVTHDQ 194
Cdd:TIGR03608 160 EPTGSLDP----KNRDEVLDLLlelNDEGKTIIIVTHDP 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
5.15e-42 |
|
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: 148.28 E-value: 5.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS----DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETP---DTGRIVMQGRTL--FDENSF 71
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlkLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 72 VPAHLRRIGFVPQE--GALFPHLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLD--RQLATHWPHEISGGQQQRVA 143
Cdd:COG0444 81 RKIRGREIQMIFQDpmTSLNPVMTVGDQIAEPLrihgGLSKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 144 LARALAQRPSLMLLDEPFSALDTGLRA-----MtrkatADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAqilnlL-----KDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
....*..
gi 697052228 219 YDVYTRP 225
Cdd:COG0444 236 EELFENP 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
9.65e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 145.98 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvMQGRTLFdensfvpAHLR---R 78
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPL-------AEARedtR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFvpQEGALFPHLNVADNIAWGLDGtrHEKRQRVEALmEMVSL-DRqlATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK11247 85 LMF--QDARLLPWKKVIDNVGLGLKG--QWRDAALQAL-AAVGLaDR--ANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 158 DEPFSALDtglrAMTRKATADLLA----EAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK11247 158 DEPLGALD----ALTRIEMQDLIEslwqQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-218 |
1.02e-41 |
|
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: 144.88 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLR-R-- 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI----TGLPPHERaRag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGL-DGTRHEKRQRVEALMEM----VSLDRQLATHwpheISGGQQQRVALARALAQRPS 153
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAyARRRAKRKARLERVYELfprlKERRKQLAGT----LSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 154 LMLLDEPFSAL-----DTGLRAMTRkatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:cd03224 153 LLLLDEPSEGLapkivEEIFEAIRE------LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-210 |
1.08e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 146.00 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensfvPAHLRriG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAER--G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDGTRHEKRQRVEALMEM---VSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMlkkVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 158 DEPFSALDtglrAMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSG 210
Cdd:PRK11248 153 DEPFGALD----AFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-216 |
1.56e-41 |
|
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: 144.23 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 21 NLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdENSFVPAHLRRIGFVPQEGALFPHLNVADNIAW 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 101 GLDGT---RHEKRQRVEALMEMVSLDRQLAtHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATA 177
Cdd:TIGR01277 94 GLHPGlklNAEQQEKVVDAAQQVGIADYLD-RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 697052228 178 DLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
14-225 |
2.68e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.80 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR-IGFVPQE--GALFP 90
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRrMQMVFQDpyASLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HLNVADNIAWGLD----GTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:COG4608 111 RMTVGDIIAEPLRihglASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 167 GLRAMTRKATADLLAEAGVASILVTHDqneaLS----FATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:COG4608 191 SIQAQVLNLLEDLQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-234 |
2.80e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlFDENSFVPAH----LR 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ-FDFSQKPSEKairlLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 R-IGFVPQEGALFPHLNVADNI----AWGLDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRP 152
Cdd:COG4161 82 QkVGMVFQQYNLWPHLTVMENLieapCKVLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPyDVYTRPVDEETAL 232
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAH 238
|
..
gi 697052228 233 FL 234
Cdd:COG4161 239 YL 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-211 |
1.05e-40 |
|
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: 141.65 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtLFDENSFVPAHLRRIGF 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV------LFDGKPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAW--GLDG-TRHEKRQRVEALMEMVSL----DRQLathwpHEISGGQQQRVALARALAQRPSL 154
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYlaQLKGlKKEEARRRIDEWLERLELseyaNKRV-----EELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-218 |
2.41e-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: 148.75 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR-IGFVPQEGALFpH 91
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL---SDLDPASWRRqIAWVPQNPYLF-A 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGL-DGTRHEKRQRVEA--LMEMV-SLDRQLAThwphEI-------SGGQQQRVALARALAQRPSLMLLDEP 160
Cdd:COG4988 425 GTIRENLRLGRpDASDEELEAALEAagLDEFVaALPDGLDT----PLgeggrglSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 161 FSALDTGLRAMTRKATADLLAEAGVasILVTHDQnEALSFATQVAVMRSGRFTQVGTP 218
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKGRTV--ILITHRL-ALLAQADRILVLDDGRIVEQGTH 555
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-212 |
7.67e-40 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 139.85 E-value: 7.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS----DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RR--IGFVPQEGALFPHLNVADNIAWGL---DGTRHEKRQRVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQR 151
Cdd:NF038007 81 RRelIGYIFQSFNLIPHLSIFDNVALPLkyrGVAKKERIERVNQVLNLFGIDNR-RNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 152 PSLMLLDEPFSALD-TGLRAMTRKATAdlLAEAGVASILVTHdQNEALSFATQVAVMRSGRF 212
Cdd:NF038007 160 PALLLADEPTGNLDsKNARAVLQQLKY--INQKGTTIIMVTH-SDEASTYGNRIINMKDGKL 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-246 |
2.06e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 145.55 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL-FDEnsfvPAHLRR- 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrIRS----PRDAIAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 -IGFVPQEGALFPHLNVADNIAWGLDGT------RHEKRQRVEALMEM----VSLDRQLathwpHEISGGQQQRVALARA 147
Cdd:COG3845 81 gIGMVHQHFMLVPNLTVAENIVLGLEPTkggrldRKAARARIRELSERygldVDPDAKV-----EDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 148 LAQRPSLMLLDEPFSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRFtqVGTpydV 221
Cdd:COG3845 156 LYRGARILILDEPTAVL-------TPQEADELfeilrrLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT---V 223
|
250 260
....*....|....*....|....*..
gi 697052228 222 YTRPVDEE--TALFLGDAVILPAQLAA 246
Cdd:COG3845 224 DTAETSEEelAELMVGREVLLRVEKAP 250
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-234 |
4.63e-39 |
|
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: 138.58 E-value: 4.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRIL-------AGFETpdTGRIVMQGRTLFDENSFVPA 74
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndlvPGVRI--EGKVLFDGQDIYDKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HLRRIGFVPQEGALFPhLNVADNIAWGLD----GTRHEKRQRVEALMEMVSL-----DRqLATHwPHEISGGQQQRVALA 145
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRlhgiKDKKELDEIVEESLKKAALwdevkDR-LHDS-ALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 146 RALAQRPSLMLLDEPFSALDTglrAMTRK--ATADLLAEAgVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDP---IATGKieELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFT 232
|
250
....*....|.
gi 697052228 224 RPVDEETALFL 234
Cdd:TIGR00972 233 NPKEKRTEDYI 243
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-218 |
8.62e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.92 E-value: 8.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFS---DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR-IGFVPQE 85
Cdd:COG1132 346 SFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV---DIRDLTLESLRRqIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 GALFpHLNVADNIAWG-LDGTRHEkrqrVEALMEMVSLDrQLATHWPH-----------EISGGQQQRVALARALAQRPS 153
Cdd:COG1132 423 TFLF-SGTIRENIRYGrPDATDEE----VEEAAKAAQAH-EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 154 LMLLDEPFSALDTGLRAMTRKATADLLaeAGVASILVTHDqneaLS---FATQVAVMRSGRFTQVGTP 218
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHR----LStirNADRILVLDDGRIVEQGTH 558
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-231 |
9.11e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 138.25 E-value: 9.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRIL-------AGFETpdTGRIVMQGRTLFDENSFVPAHLRRIGFVP 83
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGARV--EGEILLDGEDIYDPDVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 84 QEGALFPHlNVADNIAWGL----DGTRHEKRQRVEALMEMVSL-----DR--QLAThwphEISGGQQQRVALARALAQRP 152
Cdd:COG1117 99 QKPNPFPK-SIYDNVAYGLrlhgIKSKSELDEIVEESLRKAALwdevkDRlkKSAL----GLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 153 SLMLLDEPFSALDTglramtrKATA---DLLAEAG--VASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVD 227
Cdd:COG1117 174 EVLLMDEPTSALDP-------ISTAkieELILELKkdYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
....
gi 697052228 228 EETA 231
Cdd:COG1117 247 KRTE 250
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-223 |
1.05e-38 |
|
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: 137.91 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTG-RIVMQGRTLFDENsfVPAHLRRI 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED--VWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALF--PHLNVADNIAWGLDGT----RH---EKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQ 150
Cdd:COG1119 81 GLVSPALQLRfpRDETVLDVVLSGFFDSiglyREptdEQRERARELLELLGLAH-LADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-218 |
1.28e-38 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 136.48 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQ--VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRRI 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNI-----AWGLdgTRHEKRQRVEALMEMVSLDRQLatHWP-HEISGGQQQRVALARALAQRPS 153
Cdd:cd03263 78 GYCPQFDALFDELTVREHLrfyarLKGL--PKSEIKEEVELLLRVLGLTDKA--NKRaRTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 154 LMLLDEPFSALDtglrAMTRKATADLLAEAGVAS--ILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:cd03263 154 VLLLDEPTSGLD----PASRRAIWDLILEVRKGRsiILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-216 |
3.03e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 139.24 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELtAISKSFSDVQVldSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD--ENSFVPAHLRR 78
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaeKGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLdgtRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYGM---AKSMVAQFDKIVALLGIE-PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 159 EPFSALDtglraMTRKatADLLA-------EAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:PRK11144 154 EPLASLD-----LPRK--RELLPylerlarEINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-230 |
4.21e-38 |
|
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: 142.52 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFEtPDTGRIVMQGRTL--FDENSFVPahLRR-IGFVPQE--GAL 88
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdgLSRRALRP--LRRrMQVVFQDpfGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FPHLNVADNIAWGL-----DGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:COG4172 376 SPRMTVGQIIAEGLrvhgpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEET 230
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYT 522
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-218 |
5.16e-38 |
|
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: 135.49 E-value: 5.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRR-- 78
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI----TGLPPHRIArl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 -IGFVPQEGALFPHLNVADNIAWGldGTRHEKRQRVEALMEMVsLD---------RQLAThwphEISGGQQQRVALARAL 148
Cdd:COG0410 79 gIGYVPEGRRIFPSLTVEENLLLG--AYARRDRAEVRADLERV-YElfprlkerrRQRAG----TLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 149 AQRPSLMLLDEPfSAldtGLRAMTRKATADL---LAEAGVASILVthDQN--EALSFATQVAVMRSGRFTQVGTP 218
Cdd:COG0410 152 MSRPKLLLLDEP-SL---GLAPLIVEEIFEIirrLNREGVTILLV--EQNarFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
6.23e-38 |
|
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: 134.80 E-value: 6.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD----VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHL 76
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPHLNVADNIAW--GLDG-TRHEKRQRVEAL---MEMVS-LDRQLAthwphEISGGQQQRVALARALA 149
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYfaGLYGlKGDELTARLEELadrLGMEElLDRRVG-----GFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 150 QRPSLMLLDEPfsalDTGLRAMTRKATADL---LAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03266 153 HDPPVLLLDEP----TTGLDVMATRALREFirqLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-228 |
9.00e-38 |
|
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: 135.12 E-value: 9.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF-SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDEN-SFVPAHLRR 78
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLDG------------TRHEKRQRVEALmEMVSLDrQLATHWPHEISGGQQQRVALAR 146
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGykptwrsllgrfSEEDKERALSAL-ERVGLA-DKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 147 ALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238
|
..
gi 697052228 227 DE 228
Cdd:TIGR02315 239 RH 240
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-211 |
1.01e-37 |
|
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: 134.30 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF-SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD-ENSFVPAHLRR 78
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLDGTRHEKR---QRVEALMEMVSL-DRqlATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEReiqRRVGAALRQVGLeHK--ADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 155 MLLDEPFSALD--TGLRAMtrkataDLLAE---AGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:TIGR02673 159 LLADEPTGNLDpdLSERIL------DLLKRlnkRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-224 |
1.21e-37 |
|
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: 135.64 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQG-RTLFDENsfVPAHLRRIGFVPQE----- 85
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEEN--LWEIRKKVGMVFQNpdnqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 -GALfphlnVADNIAWGLD--GT-RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:TIGR04520 91 vGAT-----VEDDVAFGLEnlGVpREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 162 SALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALsFATQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-234 |
3.00e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlFDENSFVPAH----LR 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH-FDFSKTPSDKaireLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 R-IGFVPQEGALFPHLNVADNI------AWGLDgtRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQ 150
Cdd:PRK11124 82 RnVGMVFQQYNLWPHLTVQQNLieapcrVLGLS--KDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPyDVYTRPVDEET 230
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAF 236
|
....
gi 697052228 231 ALFL 234
Cdd:PRK11124 237 KNYL 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-232 |
3.33e-37 |
|
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: 133.44 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRR--- 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPMHKRArlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLDGT---RHEKRQRVEALMEMVSLDR---QLATHwpheISGGQQQRVALARALAQRP 152
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRglsKKEREEKLEELLEEFHITHlrkSKASS----LSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 153 SLMLLDEPFSALDTglramtrKATADL------LAEAGVaSILVT-HDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:cd03218 153 KFLLLDEPFAGVDP-------IAVQDIqkiikiLKDRGI-GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
....*..
gi 697052228 226 VDEETAL 232
Cdd:cd03218 225 LVRKVYL 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-213 |
3.91e-37 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 132.38 E-value: 3.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 7 ISKSFSDVQ-VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdeNSFVPAHLRRIGFVPQE 85
Cdd:cd03226 5 ISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-----PIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 --GALFPHlNVADNIAWGLDGTrHEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKEL-DAGNEQAETVLKDLDLYALKERH-PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 164 LDtgLRAMtrKATADL---LAEAGVASILVTHDQNEALSFATQVAVMRSGRFT 213
Cdd:cd03226 157 LD--YKNM--ERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
4.07e-37 |
|
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: 132.32 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSrTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRRIGF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNV---ADNIAWgLDGTRH-EKRQRVEALMEMVSL-DRqlATHWPHEISGGQQQRVALARALAQRPSLML 156
Cdd:cd03264 77 LPQEFGVYPNFTVrefLDYIAW-LKGIPSkEVKARVDEVLELVNLgDR--AKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 157 LDEPFSALDTGLRAMTRKATADLLAEAGVasILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-222 |
6.04e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 132.85 E-value: 6.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSrtaIV---GPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLR 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLPMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 -R--IGFVPQEGALFPHLNVADNIA-----WGLDgtRHEKRQRVEALMEMVSLD---RQLAthwpHEISGGQQQRVALAR 146
Cdd:COG1137 76 aRlgIGYLPQEASIFRKLTVEDNILavlelRKLS--KKEREERLEELLEEFGIThlrKSKA----YSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 147 ALAQRPSLMLLDEPFSALD----TGLRAMTRKatadlLAEAGVaSILVT-HDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpiavADIQKIIRH-----LKERGI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
.
gi 697052228 222 Y 222
Cdd:COG1137 224 L 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-211 |
6.46e-37 |
|
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: 132.15 E-value: 6.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD-ENSFVPAHLRRIGFVPQEGALFPH 91
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLDGTRH---EKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGl 168
Cdd:cd03292 93 RNVYENVAFALEVTGVpprEIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 697052228 169 ramTRKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03292 171 ---TTWEIMNLLKKinkAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-218 |
1.11e-36 |
|
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: 131.72 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 7 ISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPahlRRIGFVPQEG 86
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR---RRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 ALFPHLNVADNIAW--GLDG-TRHEKRQRVEALMEMVSL----DRQLATHwpheiSGGQQQRVALARALAQRPSLMLLDE 159
Cdd:cd03265 83 SVDDELTGWENLYIhaRLYGvPGAERRERIDELLDFVGLleaaDRLVKTY-----SGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 160 PFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-222 |
1.53e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.83 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIGFVPQE------GAl 88
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET--VWDVRRQVGMVFQNpdnqfvGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 fphlNVADNIAWGLDGT---RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK13635 98 ----TVQDDVAFGLENIgvpREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 166 TGLRAMTRKATADLLAEAGVASILVTHDQNEALSfATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
3.44e-36 |
|
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: 128.32 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFV-PAHLRRIG 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----SFAsPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 fvpqegalfphlnvadniawgldgtrhekrqrvealMEMVsldrqlathwpHEISGGQQQRVALARALAQRPSLMLLDEP 160
Cdd:cd03216 77 ------------------------------------IAMV-----------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 161 FSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRftQVGT 217
Cdd:cd03216 110 TAAL-------TPAEVERLfkvirrLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR--VVGT 163
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-230 |
3.78e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 131.50 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSD---------VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL-FDENSF 71
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 72 VPAHLRRIgFVPQEGALFPHLNVadniawG--LDG--------TRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQR 141
Cdd:COG4167 85 RCKHIRMI-FQDPNTSLNPRLNI------GqiLEEplrlntdlTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 142 VALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237
|
....*....
gi 697052228 222 YTRPVDEET 230
Cdd:COG4167 238 FANPQHEVT 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-218 |
6.18e-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: 136.82 E-value: 6.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSF--SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR- 78
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL---RDLDEDDLRRr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFpHLNVADNIAWGLDGTRHEkrqRVEALMEMVSLDRQLATH------WPHE----ISGGQQQRVALARAL 148
Cdd:COG4987 411 IAVVPQRPHLF-DTTLRENLRLARPDATDE---ELWAALERVGLGDWLAALpdgldtWLGEggrrLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 149 AQRPSLMLLDEPFSALDtglRAMTRKATADLLAEAGVAS-ILVTHDQnEALSFATQVAVMRSGRFTQVGTP 218
Cdd:COG4987 487 LRDAPILLLDEPTEGLD---AATEQALLADLLEALAGRTvLLITHRL-AGLERMDRILVLEDGRIVEQGTH 553
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-211 |
1.07e-35 |
|
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: 128.86 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQ--VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRR- 78
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---TDIRQLDPADLRRn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFpHLNVADNIAWGLdgtRHEKRQRVEALMEMVSLDRQLATHwPH-----------EISGGQQQRVALARA 147
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNITLGA---PLADDERILRAAELAGVTDFVNKH-PNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 148 LAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVasILVTHdQNEALSFATQVAVMRSGR 211
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITH-RPSLLDLVDRIIVMDSGR 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-211 |
1.63e-35 |
|
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: 126.95 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQ--VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR- 78
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---SQWDPNELGDh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHlNVADNIawgldgtrhekrqrvealmemvsldrqlathwpheISGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAeAGVASILVTHdQNEALSFATQVAVMRSGR 211
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKA-AGATRIVIAH-RPETLASADRILVLEDGR 172
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-214 |
2.95e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.39 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQ----VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 R--RIGFVPQEGALFPHLNVADNIAWGL---DGTRHEKRQRVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQR 151
Cdd:PRK11629 85 RnqKLGFIYQFHHLLPDFTALENVAMPLligKKKPAEINSRALEMLAAVGLEHR-ANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 152 PSLMLLDEPFSALDtglrAMTRKATADLLAE----AGVASILVTHDQNEALSFATQVAvMRSGRFTQ 214
Cdd:PRK11629 164 PRLVLADEPTGNLD----ARNADSIFQLLGElnrlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-225 |
3.98e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.47 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR-IGFVPQE--GALFP 90
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQkIQIVFQNpyGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:PRK11308 108 RKKVGQILEEPLlintSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 167 GLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-242 |
1.87e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.11 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR-IGFVPQE--GALFPH 91
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRdIQMVFQDsiSAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLdgtRH-------EKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSAL 164
Cdd:PRK10419 106 KTVREIIREPL---RHllsldkaERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 165 DTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFtqvgtpydVYTRPVDEETAL------FLGDAV 238
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI--------VETQPVGDKLTFsspagrVLQNAV 254
|
....
gi 697052228 239 iLPA 242
Cdd:PRK10419 255 -LPA 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-222 |
4.11e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.96 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqGRTLfdensfvpahlrRIG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALF-PHLNVADNIA-WGLDGTRHEKRQRVEALM---EMVsldRQLAthwpHEISGGQQQRVALARALAQRPSLM 155
Cdd:COG0488 382 YFDQHQEELdPDKTVLDELRdGAPGGTEQEVRGYLGRFLfsgDDA---FKPV----GVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 156 LLDEPFSALDTglraMTRKATADLLAE-AGVAsILVTHDQnEAL-SFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:COG0488 455 LLDEPTNHLDI----ETLEALEEALDDfPGTV-LLVSHDR-YFLdRVATRILEFEDGGVREYPGGYDDY 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-193 |
4.64e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.96 E-value: 4.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 4 LTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfvpahlrRIGFVP 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 84 QEGALFPHLNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLA------------------------------THWPH- 132
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLErlaelqeefealggweaearaeeilsglgfPEEDLd 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 133 ----EISGGQQQRVALARALAQRPSLMLLDEPFSALDtglrAMTRKATADLLAEAGVASILVTHD 193
Cdd:COG0488 148 rpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-217 |
6.61e-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: 124.56 E-value: 6.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHLRR--- 78
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI----TKLPPHERArag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGLDGTRHEKRQRVE-------ALMEMvsLDRQLAthwphEISGGQQQRVALARALAQR 151
Cdd:TIGR03410 77 IAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDeiyelfpVLKEM--LGRRGG-----DLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 152 PSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-193 |
7.04e-34 |
|
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: 130.48 E-value: 7.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensFVPAHLRR-IGFVPQEGALFPHlNV 94
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD---ADADSWRDqIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGL-DGTRHEKRQRVEA--LMEMVS-----LDRQLATHwPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:TIGR02857 413 AENIRLARpDASDAEIREALERagLDEFVAalpqgLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180
....*....|....*....|....*..
gi 697052228 167 GLRAMTRKATADLLaeAGVASILVTHD 193
Cdd:TIGR02857 492 ETEAEVLEALRALA--QGRTVLLVTHR 516
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-225 |
8.11e-34 |
|
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: 130.57 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKT----TLLRILAGFETPDTGRIVMQGRTLFdenSFVPAHLR-----RIGFVPQ 84
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL---GLSERELRrirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 85 E--GALFPHLNVADNIAWGLdgTRHEK------RQRVEALMEMVSLD--RQLATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:COG4172 100 EpmTSLNPLHTIGKQIAEVL--RLHRGlsgaaaRARALELLERVGIPdpERRLDAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-199 |
2.48e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.96 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdensfvpahlRRIGFVPQEGAL- 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-------------ARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 --FPhLNVADNIAWGLDGTR-------HEKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLMLLDE 159
Cdd:NF040873 68 dsLP-LTVRDLVAMGRWARRglwrrltRDDRAAVDDALERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 697052228 160 PFSALDtglrAMTRKATADLLAEA---GVASILVTHDQNEALS 199
Cdd:NF040873 146 PTTGLD----AESRERIIALLAEEharGATVVVVTHDLELVRR 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-223 |
4.42e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 123.20 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHL-RRI 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI---SMLSSRQLaRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQ-----EGALF---------PHLNVadniaWGLDGTrhEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALA 145
Cdd:PRK11231 79 ALLPQhhltpEGITVrelvaygrsPWLSL-----WGRLSA--EDNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 146 RALAQRPSLMLLDEPFSALDTG----LRAMTRKatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINhqveLMRLMRE-----LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
..
gi 697052228 222 YT 223
Cdd:PRK11231 226 MT 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-238 |
5.06e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.16 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL------------FDEN 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 70 SFvpAHLR-RIGFVPQEGALFPHLNVADNIAWG----LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVAL 144
Cdd:PRK10619 86 QL--RLLRtRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 145 ARALAQRPSLMLLDEPFSALDTG-----LRAMTRkatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPY 219
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPElvgevLRIMQQ------LAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
250
....*....|....*....
gi 697052228 220 DVYTRPVDEETALFLGDAV 238
Cdd:PRK10619 238 QLFGNPQSPRLQQFLKGSL 256
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-218 |
8.31e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.95 E-value: 8.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlfdENsfVPAHLR--- 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG-----EN--IPAMSRsrl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 -----RIGFVPQEGALFPHLNVADNIAWGLdgtrHEKRQRVEAL--------MEMVSLdRQLATHWPHEISGGQQQRVAL 144
Cdd:PRK11831 80 ytvrkRMSMLFQSGALFTDMNVFDNVAYPL----REHTQLPAPLlhstvmmkLEAVGL-RGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 145 ARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-211 |
1.33e-32 |
|
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: 122.22 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDEN-SFVPAHLRRIGFVPQE--GALFPH 91
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrKQRRAFRRDVQLVFQDspSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLdgtRH-------EKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSAL 164
Cdd:TIGR02769 105 MTVRQIIGEPL---RHltsldesEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 697052228 165 DTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
1.69e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.95 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdENSFVPAHLRRIG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWG-------LDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPS 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtphrsrFDTWTETDRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 154 LMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRR-LVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-234 |
3.04e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.38 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 7 ISKSFSDVQVLDSLNLS---------VAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLR 77
Cdd:PRK10070 25 IEQGLSKEQILEKTGLSlgvkdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG---VDIAKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 -----RIGFVPQEGALFPHLNVADNIAWGLDGT---RHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALA 149
Cdd:PRK10070 102 evrrkKIAMVFQSFALMPHMTVLDNTAFGMELAginAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 150 QRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEE 229
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
....*
gi 697052228 230 TALFL 234
Cdd:PRK10070 261 VRTFF 265
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-211 |
3.91e-32 |
|
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: 119.24 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtLFDENSFVPAH--LRRI 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI------TFDGKSYQKNIeaLRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHLNVADNIAWGLDGTRHEKrQRVEALMEMVSL----DRQLATHwpheiSGGQQQRVALARALAQRPSLM 155
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRK-KRIDEVLDVVGLkdsaKKKVKGF-----SLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 156 LLDEPFSALDT-GLRAMtRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03268 149 ILDEPTNGLDPdGIKEL-RELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-217 |
5.75e-32 |
|
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: 119.57 E-value: 5.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR-IGFVPQEGALFPh 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV---DIRDLNLRWLRSqIGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLDGTRHEKRQRVEALME----MVSLDRQLATH-WPH--EISGGQQQRVALARALAQRPSLMLLDEPFSAL 164
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAKKANihdfIMSLPDGYDTLvGERgsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 165 DTglraMTRKATADLLAEA--GVASILVTHD----QNealsfATQVAVMRSGRFTQVGT 217
Cdd:cd03249 171 DA----ESEKLVQEALDRAmkGRTTIVIAHRlstiRN-----ADLIAVLQNGQVVEQGT 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
9.77e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 119.63 E-value: 9.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF-----ETPDTGRIVMQGRTLFDENsfVPAHL 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--VIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPHLNVADNIAWGLD-----GTRHEKRQRVEALMEMVSL-----DRQLAThwPHEISGGQQQRVALAR 146
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKlnrlvKSKKELQERVRWALEKAQLwdevkDRLDAP--AGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 147 ALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVasILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
....
gi 697052228 227 DEET 230
Cdd:PRK14247 238 HELT 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-235 |
1.27e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 21 NLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvPAHLRRI----GFVPQ--EGALFPHlNV 94
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK--NKKLKPLrkkvGIVFQfpEHQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAM 171
Cdd:PRK13634 104 EKDICFGpmnFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 172 TRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPvDEETALFLG 235
Cdd:PRK13634 184 MMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP-DELEAIGLD 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-218 |
1.46e-31 |
|
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: 118.49 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDV--------QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL--FDENSfvpahLRR-I 79
Cdd:cd03253 3 FENVtfaydpgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDS-----LRRaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFpHLNVADNIAWG-LDGTRHEKRQRVEA------LMEM------VSLDRQLathwphEISGGQQQRVALAR 146
Cdd:cd03253 78 GVVPQDTVLF-NDTIGYNIRYGrPDATDEEVIEAAKAaqihdkIMRFpdgydtIVGERGL------KLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 147 ALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLaeAGVASILVTHDQNEALSfATQVAVMRSGRFTQVGTP 218
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-211 |
2.82e-31 |
|
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: 124.21 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRR-IGFVPQEGALFpHLNV 94
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG---VDIRQIDPADLRRnIGYVPQDPRLF-YGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGldgTRHEKRQRVEALMEMVSLDRQLATHwPH-----------EISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:TIGR03375 556 RDNIALG---APYADDEEILRAAELAGVTEFVRRH-PDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVasILVTHdQNEALSFATQVAVMRSGR 211
Cdd:TIGR03375 632 MDNRSEERFKDRLKRWLAGKTL--VLVTH-RTSLLDLVDRIIVMDNGR 676
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-221 |
4.64e-31 |
|
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: 116.94 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFS---DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLR-RIGFVPQE 85
Cdd:cd03254 9 NFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI---DIRDISRKSLRsMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 GALFPHlNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03254 86 TFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLgenggnlSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 159 EPFSALDTGLRAMTRKATADLLaeAGVASILVTHdqneALS---FATQVAVMRSGRFTQVGTPYDV 221
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLM--KGRTSIIIAH----RLStikNADKILVLDDGKIIEEGTHDEL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
5.03e-31 |
|
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: 116.76 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFS-------DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRI-VMQGRTLFDENSFV 72
Cdd:COG4778 4 LLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 73 P---AHLRR--IGFVPQegalfpHLNV-----ADNI------AWGLDgtRHEKRQRVEALMEMVSLDRQLATHWPHEISG 136
Cdd:COG4778 84 PreiLALRRrtIGYVSQ------FLRViprvsALDVvaepllERGVD--REEARARARELLARLNLPERLWDLPPATFSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 137 GQQQRVALARALAQRPSLMLLDEPFSALDtglrAMTRKATADLLAEA---GVASILVTHDQN--EALsfATQVAVMRSGR 211
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLD----AANRAVVVELIEEAkarGTAIIGIFHDEEvrEAV--ADRVVDVTPFS 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
5.04e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.49 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAhlRRIG 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--KRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGAL--------------FPH----LNVADniawgldgtrHEKRQRVEALMEMVSL-DRQLathwpHEISGGQQQR 141
Cdd:COG4604 79 ILRQENHInsrltvrelvafgrFPYskgrLTAED----------REIIDEAIAYLDLEDLaDRYL-----DELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 142 VALARALAQRPSLMLLDEPFSALD----TGLRAMTRKATADLlaeaGVASILVTHDQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL----GKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
....*....
gi 697052228 218 PYDVYTRPV 226
Cdd:COG4604 220 PEEIITPEV 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-197 |
6.92e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.42 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 R--RIGFVPQEGALFPHLNVADNIAWG--LDGTR-HEKRQRVEALMEMVSLDRQLaTHWPHEISGGQQQRVALARALAQR 151
Cdd:PRK10584 86 RakHVGFVFQSFMLIPTLNALENVELPalLRGESsRQSRNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 697052228 152 PSLMLLDEPFSALD--TGLRamtrkaTADLL----AEAGVASILVTHDQNEA 197
Cdd:PRK10584 165 PDVLFADEPTGNLDrqTGDK------IADLLfslnREHGTTLILVTHDLQLA 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-221 |
1.26e-30 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 121.78 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHL-RRIGFVPQEGALFP 90
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELgRHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HlNVADNIAwgldgtRHEK---RQRVEALM-----EMV-SL----DRQLATHwPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:COG4618 420 G-TIAENIA------RFGDadpEKVVAAAKlagvhEMIlRLpdgyDTRIGEG-GARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 158 DEPFSALDT-GLRAMTRkaTADLLAEAGVASILVTHDQNeALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:COG4618 492 DEPNSNLDDeGEAALAA--AIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
2.17e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 115.76 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTA--ISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlfDENSFVPAH--- 75
Cdd:PRK10895 1 MATLTAknLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLLPLHara 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 LRRIGFVPQEGALFPHLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQR 151
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLMAVLqirdDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 152 PSLMLLDEPFSALDTgLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:PRK10895 156 PKFILLDEPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-222 |
4.70e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIGFVPQ--EGALFPHlNV 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQ-LATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRA 170
Cdd:PRK13637 102 EKDIAFGpinLGLSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 697052228 171 MTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-211 |
7.39e-30 |
|
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: 112.95 E-value: 7.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 8 SKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdensfvpahlrrIGFVPQEGA 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------IAYVSQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 88 LfphLN--VADNIAWGLdgtRHEKrQRVEALMEMVSLDRQLAThWPH----EI-------SGGQQQRVALARALAQRPSL 154
Cdd:cd03250 77 I---QNgtIRENILFGK---PFDE-ERYEKVIKACALEPDLEI-LPDgdltEIgekginlSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 155 MLLDEPFSALD--TGLRAMTRKATADLLAEAGVasILVTHdQNEALSFATQVAVMRSGR 211
Cdd:cd03250 149 YLLDDPLSAVDahVGRHIFENCILGLLLNNKTR--ILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-210 |
4.54e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 117.07 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfVPAHLRRIG 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLdgTRHEKR-QRVEALMemvsldRQLATHWPHEISGG-----QQQRVALARALAQRPSL 154
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGL--PKRQASmQKMKQLL------AALGCQLDLDSSAGslevaDRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 155 MLLDEPFSALDTG-LRAMTRKATAdLLAEaGVASILVTHDQNEALSFATQVAVMRSG 210
Cdd:PRK15439 162 LILDEPTASLTPAeTERLFSRIRE-LLAQ-GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-193 |
5.42e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RR--IGFVPQEGALFPHLNVADNI---AWGLDGTRHEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQR 151
Cdd:PRK10535 84 RRehFGFIFQRYHLLSHLTAAQNVevpAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 697052228 152 PSLMLLDEPFSALD--TGLRAMtrkATADLLAEAGVASILVTHD 193
Cdd:PRK10535 163 GQVILADEPTGALDshSGEEVM---AILHQLRDRGHTVIIVTHD 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-217 |
6.75e-29 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 116.57 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTgrivMQGRTLFDENSFVPAHLRR-- 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGT----YEGEIIFEGEELQASNIRDte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 ---IGFVPQEGALFPHLNVADNIAWGLDGTRH------EKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALA 149
Cdd:PRK13549 81 ragIAIIHQELALVKELSVLENIFLGNEITPGgimdydAMYLRAQKLLAQLKLDINPATP-VGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 150 QRPSLMLLDEPFSALdtglramTRKATADLLA------EAGVASILVTHDQNEALSFATQVAVMRSGRFtqVGT 217
Cdd:PRK13549 160 KQARLLILDEPTASL-------TESETAVLLDiirdlkAHGIACIYISHKLNEVKAISDTICVIRDGRH--IGT 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-224 |
7.04e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.73 E-value: 7.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTT----LLRILAGfetpdTGRIVMQGRTL--FDENSFVPAHlRRIGFVPQE--G 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLhnLNRRQLLPVR-HRIQVVFQDpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 ALFPHLNVADNIAWGL-----DGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 162 SALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG-------TPYDVYTR 224
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGdcervfaAPQQEYTR 523
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-225 |
7.87e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.65 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 18 DSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR-IGFVPQE--GALFPHLNV 94
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGL-----DGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLR 169
Cdd:PRK15079 118 GEIIAEPLrtyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 170 AMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
9.18e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.01 E-value: 9.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF--SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFvpaHLR- 77
Cdd:PRK13632 7 MIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK---EIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 RIGFVPQE-GALFPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLDRQLaTHWPHEISGGQQQRVALARALAQRPS 153
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENkkvPPKKMKDIIDDLAKKVGMEDYL-DKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 154 LMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSfATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
1.27e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.59 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfVPAHLR---- 77
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP-------VPSRARharq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 RIGFVPQEGALFPHLNVADNIA-----WGLdgTRHEKRQRVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQRP 152
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLvfgryFGL--SAAAARALVPPLLEFAKLENK-ADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAeAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-234 |
1.55e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.29 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF-ETPDT-----GRIVMQGRTLFDENSFvpaHLRR-IGFVPQ 84
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAI---KLRKeVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 85 EGALFPHLNVADNIAWGLDG----TRHEKRQRVEALMEMVSLDRQLATHW---PHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKShgikEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEagVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-222 |
2.85e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvpAHLRR-IGFVPQEGA-LFPHLNV 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF---EKLRKhIGIVFQNPDnQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDG--TRHEKRQRV--EALMEMVSLDRqlATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRA 170
Cdd:PRK13648 102 KYDVAFGLENhaVPYDEMHRRvsEALKQVDMLER--ADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 697052228 171 MTRKATADLLAEAGVASILVTHDQNEALSfATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
2.86e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.40 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIV--MQGRTLFDENSFVPAHLRR 78
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 I-----GFVPQEGA--LFPHLNVADNIAWGL--DGTRHEKRQRVEAL--MEMVSLDRQLATHWPHEISGGQQQRVALARA 147
Cdd:PRK11701 86 LlrtewGFVHQHPRdgLRMQVSAGGNIGERLmaVGARHYGDIRATAGdwLERVEIDAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 148 LAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-211 |
2.90e-28 |
|
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: 108.41 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 8 SKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAG--FETPDTGRIVMQGRTLfDENSFVpahlRRIGFVPQE 85
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL-DKRSFR----KIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 GALFPHLNVadniawgldgtrhekrqrVEALMEMVSLDRqlathwpheISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:cd03213 91 DILHPTLTV------------------RETLMFAAKLRG---------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 697052228 166 TG-----LRAMTRkatadlLAEAGVASILVTHD-QNEALSFATQVAVMRSGR 211
Cdd:cd03213 144 SSsalqvMSLLRR------LADTGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-217 |
3.09e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 109.63 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensFVPAHLRR-IGFVPQEGALFpHLNV 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD---YTLASLRRqIGLVSQDVFLF-NDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDG-TRHEKRQRVEA--LMEMV-SLDRQLAThwphEI-------SGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:cd03251 93 AENIAYGRPGaTREEVEEAARAanAHEFImELPEGYDT----VIgergvklSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 164 LDTGLRAMTRKATADLLaeAGVASILVTHdqneALSF---ATQVAVMRSGRFTQVGT 217
Cdd:cd03251 169 LDTESERLVQAALERLM--KNRTTFVIAH----RLSTienADRIVVLEDGKIVERGT 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
3.57e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.85 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfVPAHLR---- 77
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-------VPARARlara 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 RIGFVPQEGALFPHLNVADNIA-----WGLDgTRhEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQRP 152
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLvfgryFGMS-TR-EIEAVIPSLLEFARLESKADAR-VSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAEaGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
3.73e-28 |
|
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: 109.92 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRI--VMQGRTLFDENSFVPAHLRR 78
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyIMRSGAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 I-----GFVPQEGA--LFPHLNVADNIAWGL--DGTRHEKRQRVEAL--MEMVSLDRQLATHWPHEISGGQQQRVALARA 147
Cdd:TIGR02323 83 LmrtewGFVHQNPRdgLRMRVSAGANIGERLmaIGARHYGNIRATAQdwLEEVEIDPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 148 LAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-263 |
4.32e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.21 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFvpaHLR-RIGFVPQ--EGALF 89
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRsKVGLVFQdpDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PhLNVADNIAWG---LDGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:PRK13647 94 S-STVWDDVAFGpvnMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 167 GLRAmTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLGdaviLPAQLAA 246
Cdd:PRK13647 172 RGQE-TLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGLRLP----LVAQIFE 246
|
250
....*....|....*..
gi 697052228 247 GYAVCALGEVPTDNAQA 263
Cdd:PRK13647 247 DLPELGQSKLPLTVKEA 263
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD-VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL-FDENSFVPAHlRR 78
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYDKKSLLEVR-KT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQ--EGALF-PhlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRP 152
Cdd:PRK13639 80 VGIVFQnpDDQLFaP--TVEEDVAFGplnLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAEaGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTrpvDEET 230
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS---DIET 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-217 |
1.09e-27 |
|
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: 108.34 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRR-IGFVPQEGALFpHLNV 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRqVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDGTRHEKRQRV-------EALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTG 167
Cdd:cd03252 93 RDNIALADPGMSMERVIEAaklagahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 697052228 168 LRAMTRKATADLLaeAGVASILVTHdQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:cd03252 173 SEHAIMRNMHDIC--AGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-192 |
2.02e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.59 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqgrtlfdensfvPAHlRRIGFVPQEgALFPHLNVA 95
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR------------PAG-ARVLFLPQR-PYLPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWGLDGTRHEkRQRVEALMEMVSLDRqLATH------WPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLR 169
Cdd:COG4178 444 EALLYPATAEAFS-DAELREALEAVGLGH-LAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180
....*....|....*....|...
gi 697052228 170 AMTRKATADLLAEAGVasILVTH 192
Cdd:COG4178 522 AALYQLLREELPGTTV--ISVGH 542
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-222 |
2.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.68 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGR--TLFDENSFVPAHLRRIGFVPQ--EGALFPHl 92
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTliTSTSKNKDIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 93 NVADNIAWGLDG---TRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDtglr 169
Cdd:PRK13649 102 TVLKDVAFGPQNfgvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD---- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 170 AMTRKATADL---LAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13649 178 PKGRKELMTLfkkLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-224 |
2.77e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIGFVPQE------GAlfp 90
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN--VWDIRHKIGMVFQNpdnqfvGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 hlNVADNIAWGLD--GTRHEK-RQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTG 167
Cdd:PRK13650 98 --TVEDDVAFGLEnkGIPHEEmKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 168 LRAMTRKATADLLAEAGVASILVTHDQNE-ALSfaTQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDEvALS--DRVLVMKNGQVESTSTPRELFSR 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-217 |
2.90e-27 |
|
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: 111.84 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTgrivMQGRTLFDENSFVPAHLRR-- 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT----WDGEIYWSGSPLKASNIRDte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 ---IGFVPQEGALFPHLNVADNIAWG----LDGTR---HEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARAL 148
Cdd:TIGR02633 77 ragIVIIHQELTLVPELSVAENIFLGneitLPGGRmayNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 149 AQRPSLMLLDEPFSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRftQVGT 217
Cdd:TIGR02633 157 NKQARLLILDEPSSSL-------TEKETEILldiirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-225 |
3.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.38 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDE--NSFVPAHLRRIGFVPQ--EGALFP 90
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgNKNLKKLRKKVSLVFQfpEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDtg 167
Cdd:PRK13641 101 N-TVLKDVEFGpknFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD-- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 168 lrAMTRKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK13641 178 --PEGRKEMMQLFKDyqkAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-221 |
3.84e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.43 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRI-VMQGRTLFDENSFVPAHLRR----IGFVPQEGAL 88
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDGRGRakryIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FPHLNVADNI--AWGLDGTRHEKRQRVEALMEMVSLDRQLATH----WPHEISGGQQQRVALARALAQRPSLMLLDEPFS 162
Cdd:TIGR03269 377 YPHRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAEEildkYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 163 ALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
5.81e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.09 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF-----SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAH 75
Cdd:COG1101 1 MLELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV----TKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 LR--RIGFV---PQEGAlFPHLNVADNIA------------WGLDGTRHEK-RQRVEALmEMvSLDRQLAThwphEI--- 134
Cdd:COG1101 77 KRakYIGRVfqdPMMGT-APSMTIEENLAlayrrgkrrglrRGLTKKRRELfRELLATL-GL-GLENRLDT----KVgll 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 135 SGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-225 |
6.93e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFS-----DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL--FDENSFvpaHlRRIGFV 82
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqYDHHYL---H-RQVALV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 83 PQEGALFPHlNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHWPHEI-------SGGQQQRVALARALAQRPSLM 155
Cdd:TIGR00958 561 GQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVgekgsqlSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 156 LLDEPFSALDtglrAMTRKATADLLAEAGVASILVTHDqneaLSF---ATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:TIGR00958 640 ILDEATSALD----AECEQLLQESRSRASRTVLLIAHR----LSTverADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
12-226 |
7.65e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDT---GRIVMQGRTLFDENSFvpaHLR-RIGFVPQE-G 86
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVW---DIReKVGIVFQNpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 ALFPHLNVADNIAWGLD--GTRHEKRQRV--EALMEMVSLDRQLAThwPHEISGGQQQRVALARALAQRPSLMLLDEPFS 162
Cdd:PRK13640 95 NQFVGATVGDDVAFGLEnrAVPRPEMIKIvrDVLADVGMLDYIDSE--PANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 163 ALDTGLRAMTRKATADLLAEAGVASILVTHDQNEAlSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
1.00e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.48 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 8 SKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRI----------------------VMQGRTL 65
Cdd:PRK13651 14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvlekLVIQKTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 66 FDENSFVPAHLRRIGFVPQ--EGALFPHlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQ 140
Cdd:PRK13651 94 FKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGpvsMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 141 RVALARALAQRPSLMLLDEPFSALD-TGLRAMTRkaTADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPY 219
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDpQGVKEILE--IFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
250 260
....*....|....*....|....*
gi 697052228 220 DVYTrpvDEEtalFLGDAVILPAQL 244
Cdd:PRK13651 251 DILS---DNK---FLIENNMEPPKL 269
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-229 |
1.21e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 109.88 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAG------FEtpdtGRIVMQGRtlfdensfvPA 74
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGE---------VC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HLRRI------GFV--PQEGALFPHLNVADNIAWGLDGTR------HEKRQRVEALMEMVSLDRQLATHWPHeISGGQQQ 140
Cdd:NF040905 68 RFKDIrdsealGIViiHQELALIPYLSIAENIFLGNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTD-IGVGKQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 141 RVALARALAQRPSLMLLDEPFSAL---DTglramtrKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGRftQ 214
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALneeDS-------AALLDLLLElkaQGITSIIISHKLNEIRRVADSITVLRDGR--T 217
|
250
....*....|....*
gi 697052228 215 VGTpYDVYTRPVDEE 229
Cdd:NF040905 218 IET-LDCRADEVTED 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-217 |
2.84e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.42 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensFVPAHLRR-IGFVPQEGALFPH 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD---YTLASLRRqVALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 lNVADNIAWGldGTRHEKRQRVEALMEMVSL----DR-QLATHWP-----HEISGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:TIGR02203 421 -TIANNIAYG--RTEQADRAEIERALAAAYAqdfvDKlPLGLDTPigengVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 162 SALDTGLRAMTRKATADLLaeAGVASILVTHdQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:TIGR02203 498 SALDNESERLVQAALERLM--QGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGT 550
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-212 |
3.68e-26 |
|
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: 102.51 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAIS--KSFSDVqvldslNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR 78
Cdd:cd03215 4 VLEVRGLSvkGAVRDV------SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV---TRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 --IGFVP---QEGALFPHLNVADNIAwgldgtrhekrqrvealmemvsLDRQLathwpheiSGGQQQRVALARALAQRPS 153
Cdd:cd03215 75 agIAYVPedrKREGLVLDLSVAENIA----------------------LSSLL--------SGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 154 LMLLDEPFSALDTGlramtrkATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRF 212
Cdd:cd03215 125 VLILDEPTRGVDVG-------AKAEIyrlireLADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-223 |
5.98e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.30 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAhlRRIGFVPQEGALFPHLNVA 95
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWG-------LDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGL 168
Cdd:PRK10253 100 ELVARGryphqplFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 169 RAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-210 |
1.07e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.55 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDT---GRIVMQGRTLFDENSF---VPA 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLardIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HLRRIGFVPQEGALFPHLNVADNIAWGLDG------------TRHEKRQRVEALMemvsldRQLATHWPHE----ISGGQ 138
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcfswfTREQKQRALQALT------RVGMVHFAHQrvstLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 139 QQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSG 210
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-192 |
1.22e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.87 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlfdENSFVPAHLRRIGFVPQEGALFPHL 92
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-----GDIDDPDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 93 NVADNIA-W-GLDGTRhekRQRVEALMEMVSLdrQLATHWP-HEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLR 169
Cdd:PRK13539 89 TVAENLEfWaAFLGGE---ELDIAAALEAVGL--APLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|...
gi 697052228 170 AMTRKATADLLAEAGVAsILVTH 192
Cdd:PRK13539 164 ALFAELIRAHLAQGGIV-IAATH 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-225 |
1.49e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIGFV---PQEGAL 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRKFVGLVfqnPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FPhlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK13652 93 SP--TVEQDIAFGpinLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 166 TGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-196 |
1.64e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR-I 79
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE---DISTLKPEIYRQqV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPHlNVADNIA--WGLDGTRHEkRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIfpWQIRNQQPD-PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNE 196
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-230 |
1.72e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.33 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF---------SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL-FDENS 70
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 71 FVPAHLRRIgFVPQEGALFPHLNVADNIAWGL----DGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALAR 146
Cdd:PRK15112 84 YRSQRIRMI-FQDPSTSLNPRQRISQILDFPLrlntDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 147 ALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
....
gi 697052228 227 DEET 230
Cdd:PRK15112 243 HELT 246
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-205 |
2.43e-25 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 99.06 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGrIVMQGRTLfdensfvpahlrRIGF 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTV------------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQegalfphlnvadniawgldgtrhekrqrvealmemvsldrqlathwpheISGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:cd03221 68 FEQ-------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 697052228 162 SALDTGlramTRKATADLLAEAGVASILVTHDQnealSFATQVA 205
Cdd:cd03221 99 NHLDLE----SIEALEEALKEYPGTVILVSHDR----YFLDQVA 134
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-211 |
2.47e-25 |
|
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: 101.78 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD-ENSFVpaHlRRIGFVPQEGALFP 90
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYL--H-SKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HlNVADNIAWGLDGTRHEK----RQRVEA---LMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:cd03248 102 R-SLQDNIAYGLQSCSFECvkeaAQKAHAhsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVasILVTHDQNeALSFATQVAVMRSGR 211
Cdd:cd03248 181 LDAESEQQVQQALYDWPERRTV--LVIAHRLS-TVERADQILVLDGGR 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-217 |
2.48e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.47 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPDTGRIVMQGRTLfdeNSFVPAHLRR-IGFVPQEGAL 88
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIEL---RELDPESWRKhLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FpHLNVADNIawgLDGTRHEKRQRVEALMEMVSLD---RQLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLD 158
Cdd:PRK11174 435 P-HGTLRDNV---LLGNPDASDEQLQQALENAWVSeflPLLPQGLDTPIgdqaaglSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 159 EPFSALD--------TGLRAMTRKATAdllaeagvasILVTHdQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:PRK11174 511 EPTASLDahseqlvmQALNAASRRQTT----------LMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-223 |
2.78e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.16 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 5 TAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQgrtlfdeNSFVPAHLRRI----- 79
Cdd:PRK13645 15 TYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG-------DYAIPANLKKIkevkr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 -----GFVPQ--EGALFPHlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALA 149
Cdd:PRK13645 88 lrkeiGLVFQfpEYQLFQE-TIEKDIAFGpvnLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 150 QRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-166 |
3.04e-25 |
|
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: 106.44 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR-IGFVPQEGALFphlN 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ---DIRDVTQASLRAaIGIVPQDTVLF---N 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 --VADNIAWG-LDGTRHEkrqrVEALMEMVSLD----------------RQLathwphEISGGQQQRVALARALAQRPSL 154
Cdd:COG5265 446 dtIAYNIAYGrPDASEEE----VEAAARAAQIHdfieslpdgydtrvgeRGL------KLSGGEKQRVAIARTLLKNPPI 515
|
170
....*....|..
gi 697052228 155 MLLDEPFSALDT 166
Cdd:COG5265 516 LIFDEATSALDS 527
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-211 |
3.30e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 101.64 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRRIGFV-PQEGALF 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR---KKFLRRIGVVfGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHLNVADNIA-----WGLDGTRHekRQRVEALMEMVSLDRQLAThwP-HEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:cd03267 108 WDLPVIDSFYllaaiYDLPPARF--KKRLDELSELLDLEELLDT--PvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-230 |
3.97e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF-----ETPDTGRIVMQGRTLFDENSFVPAH 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 LRRIGFVPQEGALFPhLNVADNIAWGLdgtRHEKRQRVEALMEMVSLDRQLATHWP------HE----ISGGQQQRVALA 145
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGL---RLKGIKDKQVLDEAVEKSLKGASIWDevkdrlHDsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 146 RALAQRPSLMLLDEPFSALDTgLRAMTRKATADLLAEAgVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
....*
gi 697052228 226 VDEET 230
Cdd:PRK14239 239 KHKET 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-227 |
4.68e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFvpaHLRR-IGFVPQE-GALF 89
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW---NLRRkIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHLNVADNIAWGLDGT---RHEKRQRV-EALMEMVSLDrqLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK13642 95 VGATVEDDVAFGMENQgipREEMIKRVdEALLAVNMLD--FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 166 TGLRAMTRKATADLLAEAGVASILVTHDQNEALSfATQVAVMRSGRFTQVGTPYDVYTRPVD 227
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-238 |
6.26e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.46 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF-----ETPDTGRIVMQGRTLFDENsFVPAHLRR-IGFVPQ 84
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPD-VDPIEVRReVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 85 EGALFPHLNVADNIAWGLD-----GTRHEKRQRVEALMEMVSL-----DRqlATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKlnglvKSKKELDERVEWALKKAALwdevkDR--LNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALDTGLRAMTRKATADLLAEAGVasILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL 234
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
....
gi 697052228 235 GDAV 238
Cdd:PRK14267 249 TGAL 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-213 |
8.54e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.33 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSF-SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFD-ENSFVPAHLRR 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAWGL---DGTRHEKRQRVEALMEMVSL-DRqlATHWPHEISGGQQQRVALARALAQRPSL 154
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLiiaGASGDDIRRRVSAALDKVGLlDK--AKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 155 MLLDEPFSALDTGLramtRKATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGRFT 213
Cdd:PRK10908 159 LLADEPTGNLDDAL----SEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-221 |
1.13e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.16 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 9 KSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRT--LFDENSfvpahlrriGFVPQeg 86
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsaLLELGA---------GFHPE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 alfphLNVADNI-----AWGLdgTRHEKRQRVEalmEMVS-------LDRQLAThwpheISGGQQQRVALARALAQRPSL 154
Cdd:COG1134 103 -----LTGRENIylngrLLGL--SRKEIDEKFD---EIVEfaelgdfIDQPVKT-----YSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 155 MLLDEpfsALDTGLRAMTRKATADL--LAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:COG1134 168 LLVDE---VLAVGDAAFQKKCLARIreLRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
12-250 |
1.33e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 100.30 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQV---LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPDTGRIVMQGRTLfdeNSFVPAHLRRI-GFVPQEGA 87
Cdd:COG4138 4 NDVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPL---SDWSAAELARHrAYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 88 LFPHLNVADNIAWGLDGTRHEkrQRVEALMEMVSLDRQLAT--HWP-HEISGGQQQRVALARALAQ-------RPSLMLL 157
Cdd:COG4138 80 PPFAMPVFQYLALHQPAGASS--EAVEQLLAQLAEALGLEDklSRPlTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 158 DEPFSALDTGLRAmtrkATADLLAE---AGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTrpvdeetalfl 234
Cdd:COG4138 158 DEPMNSLDVAQQA----ALDRLLRElcqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT----------- 222
|
250
....*....|....*.
gi 697052228 235 gdavilPAQLAAGYAV 250
Cdd:COG4138 223 ------PENLSEVFGV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-222 |
1.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.35 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQG---RTLFDENSFVPAHlRRIGFVPQ--EGALF 89
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVR-KKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHlNVADNIAWGLD--GTRHEKRQRVEA-LMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:PRK13643 99 EE-TVLKDVAFGPQnfGIPKEKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 167 GLRAMTRKaTADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13643 178 KARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-235 |
1.61e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 100.94 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 7 ISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRIL-------AGFETpdTGRIVMQGRTLFDENSfVPAHLRRI 79
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRY--SGDVLLGGRSIFNYRD-VLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGALFPhLNVADNIAWGLDG----TRHEKRQRVEALMEMVSL-----DRqlATHWPHEISGGQQQRVALARALAQ 150
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAhklvPRKEFRGVAQARLTEVGLwdavkDR--LSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVasILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEET 230
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
....*
gi 697052228 231 ALFLG 235
Cdd:PRK14271 259 ARYVA 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-225 |
3.11e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.40 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRR-IGFVPQE--GALF 89
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRdIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHLNVADNIAWGL------DGtrHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:PRK10261 416 PRQTVGDSIMEPLrvhgllPG--KAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-192 |
4.19e-24 |
|
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: 97.43 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIGFVPqegALFPHLNVA 95
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP---GLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWGLDGTRHEKRQRVEALMEMVSLDRqlaTHWP-HEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRK 174
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRTIEDALAAVGLTGF---EDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*...
gi 697052228 175 ATADLLAEAGVAsILVTH 192
Cdd:TIGR01189 169 LLRAHLARGGIV-LLTTH 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-204 |
5.73e-24 |
|
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: 96.07 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqgrtLFDENSFvpahlrrigFVPQEgalfPHLNva 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----PEGEDLL---------FLPQR----PYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 dniawglDGTrhekrqrvealmemvsLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTG-LRAMtrk 174
Cdd:cd03223 77 -------LGT----------------LREQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEEsEDRL--- 130
|
170 180 190
....*....|....*....|....*....|
gi 697052228 175 atADLLAEAGVASILVTHdQNEALSFATQV 204
Cdd:cd03223 131 --YQLLKELGITVISVGH-RPSLWKFHDRV 157
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
6.21e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.96 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF-----ETPDTGRIVMQGRTLFDENSFVPAHL 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPhLNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHWPH-------EISGGQQQRVALARALA 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHkihksalDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 150 QRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRS-----GRFTQVGTPYDVYTR 224
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
....*.
gi 697052228 225 PVDEET 230
Cdd:PRK14258 247 PHDSRT 252
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-221 |
9.66e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 101.66 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL--FDENSFVPahlrRIGFVPQEGALFPHlN 93
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLkqWDRETFGK----HIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 VADNIAWGLDGTrhEKRQRVEA-----LMEMVSldrQLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:TIGR01842 408 VAENIARFGENA--DPEKIIEAaklagVHELIL---RLPDGYDTVIgpggatlSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 162 SALDTGLRAMTRKATADLLAeAGVASILVTHDQNeALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKA-RGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
1.13e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 101.67 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQ-VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIG 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD--QDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFpHLNVADNIAWGL-DGTRHEkrqrVEALMEMVSLDRQLA------THWPHE----ISGGQQQRVALARALA 149
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLARpDATDEE----LWAALERVGLADWLRalpdglDTVLGEggarLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 697052228 150 QRPSLMLLDEPFSALDtglrAMTRKA-TADLL-AEAGVASILVTHD 193
Cdd:TIGR02868 488 ADAPILLLDEPTEHLD----AETADElLEDLLaALSGRTVVLITHH 529
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-225 |
3.69e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.87 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKT----TLLRILAGfetpdTGRIvmQGRTLFDENSFV--PAH----LR--RIG 80
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRI--GGSATFNGREILnlPEKelnkLRaeQIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQE--GALFPHLNVADNIAWGLdgTRHEKRQRVEALMEMVS-LD-------RQLATHWPHEISGGQQQRVALARALAQ 150
Cdd:PRK09473 101 MIFQDpmTSLNPYMRVGEQLMEVL--MLHKGMSKAEAFEESVRmLDavkmpeaRKRMKMYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-213 |
5.08e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 9 KSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSFVPAHLRRIGFVP----Q 84
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRDAIRAGIAYVPedrkG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 85 EGaLFPHLNVADNIA---------WGLDGTRHEkRQRVEALMEMV-----SLDRQLAThwpheISGGQQQRVALARALAQ 150
Cdd:COG1129 339 EG-LVLDLSIRENITlasldrlsrGGLLDRRRE-RALAEEYIKRLriktpSPEQPVGN-----LSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 151 RPSLMLLDEPFSALDTGLRA-----MTRkatadlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFT 213
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAeiyrlIRE------LAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-192 |
6.76e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.49 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRRIG 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR---DEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLatHWP-HEISGGQQQRVALARALAQRPSLMLLDE 159
Cdd:PRK13538 78 YLGHQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFE--DVPvRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 697052228 160 PFSALDTglramtrKATADLL------AEAGVASILVTH 192
Cdd:PRK13538 156 PFTAIDK-------QGVARLEallaqhAEQGGMVILTTH 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-168 |
7.34e-23 |
|
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: 95.03 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGfETPDTGRIvmQGRTLFDENSFVPAH-LRRIGFVPQEGALFP 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTT--SGQILFNGQPRKPDQfQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HLNVADNIAWG--LDGTRHeKRQRVEALMEMVSLDRQLA-THWPHE----ISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:cd03234 95 GLTVRETLTYTaiLRLPRK-SSDAIRKKRVEDVLLRDLAlTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
....*
gi 697052228 164 LDTGL 168
Cdd:cd03234 174 LDSFT 178
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-212 |
7.95e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.92 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdENSFV-PAHLRR- 78
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK----EVTFNgPKSSQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 -IGFVPQEGALFPHLNVADNIAWGLDGTRH-----EKRQRVEAlmemvslDRQLA----THWPH----EISGGQQQRVAL 144
Cdd:PRK10762 80 gIGIIHQELNLIPQLTIAENIFLGREFVNRfgridWKKMYAEA-------DKLLArlnlRFSSDklvgELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 145 ARALAQRPSLMLLDEPFSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRF 212
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDAL-------TDTETESLfrvireLKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-222 |
1.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvpaHL----RRIGFVPQ--EGALF 89
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-----NLwdirNKAGMVFQnpDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHLnVADNIAWG---LDGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:PRK13633 100 ATI-VEEDVAFGpenLGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 167 GLRAMTRKATADLLAEAGVASILVTHDQNEALSfATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-222 |
1.22e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvPAHLR----RIGFVPQ--EGAL 88
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTK--DKYIRpvrkRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FPHlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK13646 99 FED-TVEREIIFGpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 166 TGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.35e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD-VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSFVPAHLRR- 78
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLREs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQ--EGALFPhLNVADNIAWG---LDGTRHEKRQRVEALMEMVSLD--RQLATHWpheISGGQQQRVALARALAQR 151
Cdd:PRK13636 84 VGMVFQdpDNQLFS-ASVYQDVSFGavnLKLPEDEVRKRVDNALKRTGIEhlKDKPTHC---LSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 152 PSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVY 222
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-229 |
2.05e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.85 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 4 LTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvPAHLRRIGFVP 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS--KAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 84 QEGALFPHLNVADNIAWG-------LDGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLML 156
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGrypwhgaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 157 LDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEE 229
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-218 |
2.90e-22 |
|
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: 98.16 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRRIGFVPQEGALFPHLNVAD 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK---DIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 97 NIAW--GLDGTRHEKRQ-RVEALMEMVSLDRQlATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDtglrAMTR 173
Cdd:TIGR01257 1023 HILFyaQLKGRSWEEAQlEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD----PYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 697052228 174 KATADLLAE--AGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTP 218
Cdd:TIGR01257 1098 RSIWDLLLKyrSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-245 |
3.25e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKT-TLLRILAGFETPD----TGRIVMQGRTLFDENSFVPAHLR--RIGFVPQEG- 86
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRgnKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 -ALFPHLNVADNIAWGLdgTRHEKRQRVEALMEMVS-LDR----QLATH---WPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK15134 103 vSLNPLHTLEKQLYEVL--SLHRGMRREAARGEILNcLDRvgirQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 158 DEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFL--- 234
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLnse 260
|
250
....*....|...
gi 697052228 235 --GDAVILPAQLA 245
Cdd:PRK15134 261 psGDPVPLPEPAS 273
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-239 |
5.71e-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: 96.41 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFET--PDTGRIVMQ----------GRTLFD-- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyvERPSKVge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 68 -----ENSFVPAHL--------------RRIGFVPQEG-ALFPHLNVADNIAWGLDGTRHEKR---QRVEALMEMVSLDR 124
Cdd:TIGR03269 81 pcpvcGGTLEPEEVdfwnlsdklrrrirKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKeavGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 125 QLaTHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQV 204
Cdd:TIGR03269 161 RI-THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 697052228 205 AVMRSGRFTQVGTPYDVYTR------PVDEETALFLGDAVI 239
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVfmegvsEVEKECEVEVGEPII 280
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-216 |
7.69e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 7.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGR--TLFDENSfvpahlrriGFVPQegalfp 90
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGLGG---------GFNPE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 hLNVADNI-----AWGLDGTrhEKRQRVEALMEMVSL----DRQLATHwpheiSGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:cd03220 99 -LTGRENIylngrLLGLSRK--EIDEKIDEIIEFSELgdfiDLPVKTY-----SSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 162 SALDTGLRamtRKATADL--LAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03220 171 AVGDAAFQ---EKCQRRLreLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-192 |
8.43e-22 |
|
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: 91.40 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIGFVPqegALFPHLNVA 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP---GIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWGLDgtRHEKRQRVEALMEMvslDRQLATHWP-HEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRK 174
Cdd:cd03231 92 ENLRFWHA--DHSDEQVEEALARV---GLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*...
gi 697052228 175 ATADLLAEAGVAsILVTH 192
Cdd:cd03231 167 AMAGHCARGGMV-VLTTH 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-225 |
1.08e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 8 SKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL---FDENSFVPAHL-------- 76
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkKNNHELITNPYskkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 ---RRIGFVPQ--EGALFPHlNVADNIAWG---LDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARAL 148
Cdd:PRK13631 113 elrRRVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 149 AQRPSLMLLDEPFSALD-TGLRAMTrkataDLLAEA---GVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDpKGEHEMM-----QLILDAkanNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD 266
|
.
gi 697052228 225 P 225
Cdd:PRK13631 267 Q 267
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-211 |
3.37e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvpAHLRR-- 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---AKIMRea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAW-GLDGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 697052228 158 DEPFSALdTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK11614 162 DEPSLGL-APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-213 |
3.67e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.94 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRR--IGFVPQE---GAL 88
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRlgVAYIPEDrlgRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FPHLNVADNIAwgLDGTRHEK------------RQRVEALME-----MVSLD---RQLathwpheiSGGQQQRVALARAL 148
Cdd:COG3845 348 VPDMSVAENLI--LGRYRRPPfsrggfldrkaiRAFAEELIEefdvrTPGPDtpaRSL--------SGGNQQKVILAREL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 149 AQRPSLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFT 213
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-193 |
5.38e-21 |
|
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: 93.85 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtlfdensfVPAHLRRIGFVPQEGALFPHLNV 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-------------RPQPGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDGTRH-----------------------EKRQRVEALMEMV---SLDRQL-----ATHWP------HEISGG 137
Cdd:TIGR03719 86 RENVEEGVAEIKDaldrfneisakyaepdadfdklaAEQAELQEIIDAAdawDLDSQLeiamdALRCPpwdadvTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 138 QQQRVALARALAQRPSLMLLDEPFSALDTglramtrKATADL---LAEAGVASILVTHD 193
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLerhLQEYPGTVVAVTHD 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-235 |
7.26e-21 |
|
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: 89.74 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 18 DSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmQGRTLFDENSFVPAHLR--RIGFVPQE--GALFPHLN 93
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQT--SGEILLDGRPLLPLSIRgrHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 VADNIAWGLdgTRHEK-----RQRVEALMEMVSLD--RQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:TIGR02770 81 MGNHAIETL--RSLGKlskqaRALILEALEAVGLPdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 167 GLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALFLG 235
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-217 |
8.03e-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: 93.65 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensFVPAHLRR-IGFVPQEGALFPHlNV 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD---IDRHTLRQfINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGL-DGTRHEKRQRVEALMEM--------VSLDRQLATHwPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:TIGR01193 565 LENLLLGAkENVSQDEIWAACEIAEIkddienmpLGYQTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 166 TGLRamtRKATADLLAEAGVASILVTHdqneALSFATQ---VAVMRSGRFTQVGT 217
Cdd:TIGR01193 644 TITE---KKIVNNLLNLQDKTIIFVAH----RLSVAKQsdkIIVLDHGKIIEQGS 691
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-212 |
1.78e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL-FdeNSFVPAHLRRIG 80
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrF--ASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDGTRH----------EKRQRVEALMEMVSLDRQLAthwphEISGGQQQRVALARALAQ 150
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQLPHKGgivnrrllnyEAREQLEHLGVDIDPDTPLK-----YLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052228 151 RPSLMLLDEPFSALDTglRAMTR--KATADLLAEaGVASILVTHDQNEALSFATQVAVMRSGRF 212
Cdd:PRK11288 158 NARVIAFDEPTSSLSA--REIEQlfRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-244 |
2.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.28 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSD-VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDEnSFVPAHLRRI 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVPQEGAL-FPHLNVADNIAWGLDG---TRHEKRQRVEALMEMVSLDRqLATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGPENlclPPIEIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 156 LLDEPFSALD--TGLRAMTRkatADLLAEAGVASILVTHDQNEaLSFATQVAVMRSGRFTQVGTPYDVYTRPVDEETALF 233
Cdd:PRK13644 159 IFDEVTSMLDpdSGIAVLER---IKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLT 234
|
250
....*....|.
gi 697052228 234 LGDAVILPAQL 244
Cdd:PRK13644 235 PPSLIELAENL 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-193 |
2.94e-20 |
|
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: 91.54 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqGRTLfdensfvpahlrRIGF 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQE-GALFPHLNVADNIAWGLDGTRHEKRqrvealmEMVS-----------LDRQLAThwpHEISGGQQQRVALARALA 149
Cdd:TIGR03719 390 VDQSrDALDPNKTVWEEISGGLDIIKLGKR-------EIPSrayvgrfnfkgSDQQKKV---GQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 697052228 150 QRPSLMLLDEPFSALDT-GLRAMTRKatadLLAEAGVAsILVTHD 193
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVeTLRALEEA----LLNFAGCA-VVISHD 499
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
3.29e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIG 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQ--EGALFpHLNVADNIAWGLDG---TRHEKRQRVEALMEMVslDRQLATHWPHE-ISGGQQQRVALARALAQRPSL 154
Cdd:PRK13638 81 TVFQdpEQQIF-YTDIDSDIAFSLRNlgvPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALDTGLRAMTrKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQM-IAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
4.59e-20 |
|
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: 86.21 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSF--SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdENSFVPAHLRR- 78
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV----PVSDLEKALSSl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEgalfPHLnvadniawgLDGTrhekrqrveaLMEmvSLDRQLathwpheiSGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03247 77 ISVLNQR----PYL---------FDTT----------LRN--NLGRRF--------SGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 159 EPFSALDtglrAMTRKATADLLAEA--GVASILVTHdQNEALSFATQVAVMRSGRFTQVG 216
Cdd:cd03247 124 EPTVGLD----PITERQLLSLIFEVlkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-231 |
5.30e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLR-------ILAGFETpdTGRIVMQGRTLFDENSFVPA 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 75 HLRRIGFVPQEGALFPHlNVADNIAWG--LDGTRHEKRQRVE-ALMEMVSLD------RQLAThwphEISGGQQQRVALA 145
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPK-SIYDNIAYGarINGYKGDMDELVErSLRQAALWDevkdklKQSGL----SLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 146 RALAQRPSLMLLDEPFSALDtglrAMTRKATADLLAEAG--VASILVTHDQNEALSFATQVAVM---------RSGRFTQ 214
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALD----PISTLRIEELMHELKeqYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVE 239
|
250
....*....|....*..
gi 697052228 215 VGTPYDVYTRPVDEETA 231
Cdd:PRK14243 240 FDRTEKIFNSPQQQATR 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-217 |
2.29e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlFDENSFVPAHLRRIG 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDGTR----------HEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQ 150
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 151 RPSLMLLDEPFSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGrfTQVGT 217
Cdd:PRK09700 163 DAKVIIMDEPTSSL-------TNKEVDYLflimnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDG--SSVCS 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-225 |
2.43e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAHL-RRI 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI----EGLPGHQiARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 80 GFVP--QEGALF------------PHLNVADNIAWGLDGTRHEKRQRVEAL------MEMVSLdRQLATHWPHEISGGQQ 139
Cdd:PRK11300 81 GVVRtfQHVRLFremtvienllvaQHQQLKTGLFSGLLKTPAFRRAESEALdraatwLERVGL-LEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 140 QRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPY 219
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
....*.
gi 697052228 220 DVYTRP 225
Cdd:PRK11300 240 EIRNNP 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-195 |
4.35e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.62 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFE--TPDTGRIVMqgrtlfDENSFvpahlrrigfvPQEGALFPHLN 93
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV------PDNQF-----------GREASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 VADNIAwgldgtrhekrQRVEALmEMVSL-DRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMT 172
Cdd:COG2401 108 RKGDFK-----------DAVELL-NAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|...
gi 697052228 173 RKATADLLAEAGVASILVTHDQN 195
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYD 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-165 |
5.91e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 87.48 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIV-MQGRTlfdensfvpahlrrIGFVPQEGALFPHLN 93
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpAPGIK--------------VGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 VADNIAWGLDGTRhEKRQRVEALMEMVS---------------------------LDRQL-----ATHWPH------EIS 135
Cdd:PRK11819 87 VRENVEEGVAEVK-AALDRFNEIYAAYAepdadfdalaaeqgelqeiidaadawdLDSQLeiamdALRCPPwdakvtKLS 165
|
170 180 190
....*....|....*....|....*....|
gi 697052228 136 GGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-219 |
6.51e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 26 PGSRTAIVGPSGSGKTTLLRILAGFETPDT---GRIVMQGRTLfdENSFvpahLRRI-GFVPQEGALFPHLNVADNIAW- 100
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI--DAKE----MRAIsAYVQQDDLFIPTLTVREHLMFq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 101 -----GLDGTRHEKRQRVEALMEMVSLD--RQLATHWPHE---ISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRA 170
Cdd:TIGR00955 124 ahlrmPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 697052228 171 MTRKATADlLAEAGVASILVTHD-QNEALSFATQVAVMRSGRFTQVGTPY 219
Cdd:TIGR00955 204 SVVQVLKG-LAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
2.03e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQ--VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTL--FDEnsfvpAHLR 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSE-----AALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 R-IGFVPQEGALFPHlNVADNIAWGLDGTRHEKR----QRV--EALMEMVS-LD-------RQLathwpheiSGGQQQRV 142
Cdd:PRK11160 414 QaISVVSQRVHLFSA-TLRDNLLLAAPNASDEALievlQQVglEKLLEDDKgLNawlgeggRQL--------SGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 143 ALARALAQRPSLMLLDEPFSALDtglrAMTRKATADLLAE--AGVASILVTHDQNeALSFATQVAVMRSGRFTQVGT 217
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLD----AETERQILELLAEhaQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGT 556
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-218 |
2.59e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFE--TPDTGRIVMQGRTLFDEnsfvPAHLR-R 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILEL----SPDERaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IG-FV----PQEgalFPHLNVAD------NIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHWPHE-ISGGQQQRVALAR 146
Cdd:COG0396 77 AGiFLafqyPVE---IPGVSVSNflrtalNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 147 ALAQRPSLMLLDEPFSALDT-GLRAMTRKATAdlLAEAGVASILVTHdQNEALSF--ATQVAVMRSGRFTQVGTP 218
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIdALRIVAEGVNK--LRSPDRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-211 |
4.92e-18 |
|
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: 81.03 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFE--TPDTGRIVMQGRTLFDensfVPAHLRR- 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITD----LPPEERAr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 --IGFVPQEGALFPHLNVAD---NIAWGLdgtrhekrqrvealmemvsldrqlathwpheiSGGQQQRVALARALAQRPS 153
Cdd:cd03217 77 lgIFLAFQYPPEIPGVKNADflrYVNEGF--------------------------------SGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 154 LMLLDEPFSALD-TGLRAMTRkaTADLLAEAGVASILVTHdQNEALSF--ATQVAVMRSGR 211
Cdd:cd03217 125 LAILDEPDSGLDiDALRLVAE--VINKLREEGKSVLIITH-YQRLLDYikPDRVHVLYDGR 182
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-193 |
5.78e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.21 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRRIGFV-PQEGALF 89
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR---KEFARRIGVVfGQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHLNVADNIA-----WGLDGTRHekRQRVEALMEMVSLD-------RQLathwpheiSGGQQQRVALARALAQRPSLMLL 157
Cdd:COG4586 109 WDLPAIDSFRllkaiYRIPDAEY--KKRLDELVELLDLGelldtpvRQL--------SLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 697052228 158 DEPfsaldT-GLRAMTRKATADLL----AEAGVASILVTHD 193
Cdd:COG4586 179 DEP-----TiGLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-193 |
5.82e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfvpahlrRIG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-------------RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNvadniawgLDGTRHEK-RQRVEALMEMVSLDRQLATH---WP-HEISGGQQQRVALARALAQRPSLM 155
Cdd:PRK09544 71 YVPQKLYLDTTLP--------LTVNRFLRlRPGTKKEDILPALKRVQAGHlidAPmQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 697052228 156 LLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHD 193
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-230 |
1.23e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.63 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 4 LTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSFVPAHLRRIGFVP 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 84 QEGALFPHLNVADNIAWGLDGTR-----HEKRQR-VEALMEMVSLD----RQLAThwpheISGGQQQRVALARALAQRPS 153
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKgmfvdQDKMYRdTKAIFDELDIDidprAKVAT-----LSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 154 LMLLDEPFSALdtglramTRKATADL------LAEAGVASILVTHDQNEALSFATQVAVMRSGRFtqvgtpydVYTRPVD 227
Cdd:PRK10982 155 IVIMDEPTSSL-------TEKEVNHLftiirkLKERGCGIVYISHKMEEIFQLCDEITILRDGQW--------IATQPLA 219
|
...
gi 697052228 228 EET 230
Cdd:PRK10982 220 GLT 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-225 |
1.72e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKT----TLLRIL--AGFETpDTGRIVMQGRT--LFDENSFVPAHLRR-----IG 80
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLV-QCDKMLLRRRSrqVIELSEQSAAQMRHvrgadMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQE--GALFPHLNVADNIAWGLdgTRHEKRQRVEALME---MVSLDR-----QLATHWPHEISGGQQQRVALARALAQ 150
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIAESI--RLHQGASREEAMVEakrMLDQVRipeaqTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 151 RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-166 |
1.77e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 83.39 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 8 SKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPD--TGRIVMQGRTLFDENsfvpahLRRIGFVPQE 85
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQI------LKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 GALFPHLNVADNIAW------GLDGTRHEKRQRVEALMEMVSLDR----QLATHWPHEISGGQQQRVALARALAQRPSLM 155
Cdd:PLN03211 149 DILYPHLTVRETLVFcsllrlPKSLTKQEKILVAESVISELGLTKcentIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170
....*....|.
gi 697052228 156 LLDEPFSALDT 166
Cdd:PLN03211 229 ILDEPTSGLDA 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-165 |
3.63e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRR-IGFVPQEGALFpHLN 93
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG---TDIRTVTRASLRRnIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 94 VADNIAWGL-DGTRHEKR---QRVEALMEMVSLDRQLATHWPH---EISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK13657 425 IEDNIRVGRpDATDEEMRaaaERAQAHDFIERKPDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-166 |
4.12e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.37 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDensFVPAHLRR-IGFVPQEGALFpH 91
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD---YTLASLRNqVALVSQNVHLF-N 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLDG--TRH--EKRQRVEALMEMVS-LDRQLATHWPHE---ISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:PRK11176 431 DTIANNIAYARTEqySREqiEEAARMAYAMDFINkMDNGLDTVIGENgvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
...
gi 697052228 164 LDT 166
Cdd:PRK11176 511 LDT 513
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
6.12e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.17 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQV----LDSLNLSVAPGSRTAIVGPSGSGKT-TLLRILAGFETPdtGRiVMQGRTLFDENSF--VP 73
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GR-VMAEKLEFNGQDLqrIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 74 AHLRR--IG------FVPQEGALFPHLNVADNIAWGLD----GTRHEKRQRVEALMEMVSLD--RQLATHWPHEISGGQQ 139
Cdd:PRK11022 80 EKERRnlVGaevamiFQDPMTSLNPCYTVGFQIMEAIKvhqgGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 140 QRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPY 219
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
....*.
gi 697052228 220 DVYTRP 225
Cdd:PRK11022 240 DIFRAP 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-218 |
1.19e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.53 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAH-LR-RIGFVPQEGALFPHlN 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI----SKIGLHdLRsRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 VADNiawgLD-GTRHEKRQRVEALmEMVSLDR---QLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLDEPFS 162
Cdd:cd03244 94 IRSN----LDpFGEYSDEELWQAL-ERVGLKEfveSLPGGLDTVVeeggenlSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 163 ALDTGLRAMTRKATADLLAEAGVasILVTHDQNEALSFAtQVAVMRSGRFTQVGTP 218
Cdd:cd03244 169 SVDPETDALIQKTIREAFKDCTV--LTIAHRLDTIIDSD-RILVLDKGRVVEFDSP 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
12-226 |
1.20e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQV---LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPDTGRIVMQGRTLFDENSFVPAHlRRIGFVPQEGAL 88
Cdd:PRK03695 4 NDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELAR-HRAYLSQQQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FP---------HLNVADNIAwgldgtrhEKRQRVEALMEMVSLDRQLATHwPHEISGGQQQRVALARALAQ-RPS----- 153
Cdd:PRK03695 82 FAmpvfqyltlHQPDKTRTE--------AVASALNEVAEALGLDDKLGRS-VNQLSGGEWQRVRLAAVVLQvWPDinpag 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 154 -LMLLDEPFSALDtglraMTRKATADLL----AEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPV 226
Cdd:PRK03695 153 qLLLLDEPMNSLD-----VAQQAALDRLlselCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-165 |
1.30e-16 |
|
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: 76.90 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPD--TGRIVMQGRTLfdensfVPAHLRRIGFVPQEGALFPHL 92
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL------DKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 93 NVadniawgldgtrhekrqrVEALMEMVSLdrqlathwpHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:cd03232 95 TV------------------REALRFSALL---------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-193 |
1.33e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.55 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqGRTLfdensfvpahlrRIGF 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQE-GALFPHLNVADNIAWGLDGTRHEKRqrvealmEMVSL-----------DRQLAThwpHEISGGQQQRVALARALA 149
Cdd:PRK11819 392 VDQSrDALDPNKTVWEEISGGLDIIKVGNR-------EIPSRayvgrfnfkggDQQKKV---GVLSGGERNRLHLAKTLK 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 697052228 150 QRPSLMLLDEPFSALDT-GLRAMtRKAtadLLAEAGVAsILVTHD 193
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVeTLRAL-EEA---LLEFPGCA-VVISHD 501
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
5.12e-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: 79.29 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQ--VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVpaHlRR 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV--H-QN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFVPQEGALFPHLNVADNIAW--GLDGTRHEKRQRV-----EALMEMVSLDRQLATHwpheiSGGQQQRVALARALAQR 151
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLyaRLRGVPAEEIEKVanwsiQSLGLSLYADRLAGTY-----SGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 152 PSLMLLDEPFSALDTGLRAMTRKATADLLAEaGVASILVTHDQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-203 |
7.22e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvpaHLRRIG 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-----RSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAW--GLDGtRHEKRQRVEALMeMVSLDRQLAThWPHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:PRK13543 86 YLGHLPGLKADLSTLENLHFlcGLHG-RRAKQMPGSALA-IVGLAGYEDT-LVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 697052228 159 EPFSALD-TGLRAMTRKATADLlaEAGVASILVTHDQNEALSFATQ 203
Cdd:PRK13543 163 EPYANLDlEGITLVNRMISAHL--RGGGAALVTTHGAYAAPPVRTR 206
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-193 |
7.28e-16 |
|
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: 75.91 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRT-----AIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtlfdensfvPAHLRRIGFVPQE-GA 87
Cdd:cd03237 7 KKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI--------------EIELDTVSYKPQYiKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 88 LFPhLNVADNIAWGLDGTRHEKRQRVEAL--MEMVSL-DRQLAthwphEISGGQQQRVALARALAQRPSLMLLDEPFSAL 164
Cdd:cd03237 73 DYE-GTVRDLLSSITKDFYTHPYFKTEIAkpLQIEQIlDREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180
....*....|....*....|....*....
gi 697052228 165 DTGLRAMTRKATADLLAEAGVASILVTHD 193
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-193 |
7.42e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSfsdvqvLDSLNLSVAPGS-RT----AIVGPSGSGKTTLLRILAGFETPDTGRIVmqgRTLfdensfvpah 75
Cdd:PRK13409 340 LVEYPDLTKK------LGDFSLEVEGGEiYEgeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PEL---------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 76 lrRIGFVPQEGALFPHLNVAD---NIAWGLDGT--RHE--KRQRVEALMemvslDRQLAthwphEISGGQQQRVALARAL 148
Cdd:PRK13409 401 --KISYKPQYIKPDYDGTVEDllrSITDDLGSSyyKSEiiKPLQLERLL-----DKNVK-----DLSGGELQRVAIAACL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 697052228 149 AQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHD 193
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-223 |
1.04e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 7 ISKSFSDVQvldSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSFVPAHLRRIGFVPQ-- 84
Cdd:PRK09700 272 TSRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI-SPRSPLDAVKKGMAYITEsr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 85 -EGALFPHLNVADNIA-------------WGLDGTRHEKR----QRVEALMEMVSLDRQLAthwphEISGGQQQRVALAR 146
Cdd:PRK09700 348 rDNGFFPNFSIAQNMAisrslkdggykgaMGLFHEVDEQRtaenQRELLALKCHSVNQNIT-----ELSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 147 ALAQRPSLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYT 223
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-218 |
1.28e-15 |
|
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: 74.37 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 15 QVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdenSFVPAH-LRR-IGFVPQEGALFphl 92
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLEdLRSsLTIIPQDPTLF--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 93 nvADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLathwpheiSGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMT 172
Cdd:cd03369 95 --SGTIRSNLDPFDEYSDEEIYGALRVSEGGLNL--------SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 697052228 173 RKATADLLAEAGVASIlvTHDQNEALSFAtQVAVMRSGRFTQVGTP 218
Cdd:cd03369 165 QKTIREEFTNSTILTI--AHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-224 |
1.56e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVmqgrtlFDENSfvpahlrRIGF 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------WSENA-------NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQE-GALFPH-LNVADNIA-WGLDGtrhEKRQRVEALmemvsLDRQL-----ATHWPHEISGGQQQRVALARALAQRPS 153
Cdd:PRK15064 387 YAQDhAYDFENdLTLFDWMSqWRQEG---DDEQAVRGT-----LGRLLfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 154 LMLLDEPFSALDT----GLRAMTRKATADLlaeagvasILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:PRK15064 459 VLVMDEPTNHMDMesieSLNMALEKYEGTL--------IFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLR 525
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-246 |
1.71e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.12 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTtlLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLR--RIGFVPQ--EGA 87
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRgrKIATIMQnpRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 88 LFPHLNVADN-IAWGLDGTRHEKRQRVEALMEMVSLD--RQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSAL 164
Cdd:PRK10418 92 FNPLHTMHTHaRETCLALGKPADDATLTAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 165 DTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEET-ALFLGDAVILPAQ 243
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTrSLVSAHLALYGME 251
|
...
gi 697052228 244 LAA 246
Cdd:PRK10418 252 LAS 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-165 |
1.80e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGfETPDT--GRIVMQGRtlfdensfvpahlrrIGFVPQEGALFpHLNV 94
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRsdASVVIRGT---------------VAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGL--DGTRHEKRQRVEALMEMVSLdrqLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PLN03130 696 RDNILFGSpfDPERYERAIDVTALQHDLDL---LPGGDLTEIgergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-165 |
2.03e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.30 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGR----------------TLFDensFVP 73
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegTVYD---FVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 74 A------------H--LRRIGFVPQEGAL---------FPHLNvadniAWGLDgtrhekrQRVEALMEMVSL--DRQLAt 128
Cdd:PRK11147 89 EgieeqaeylkryHdiSHLVETDPSEKNLnelaklqeqLDHHN-----LWQLE-------NRINEVLAQLGLdpDAALS- 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 697052228 129 hwphEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PRK11147 156 ----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-223 |
2.99e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.86 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPD--------TGRIVMQGRTLFDENSFVPAHLRRIgfVPQEG- 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAV--LPQAAq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 -------------ALFPHLNVAdniawglDGTRHEKRQ---RVEALMEMVSLDRQLAThwphEISGGQQQRVALARALAQ 150
Cdd:PRK13547 94 pafafsareivllGRYPHARRA-------GALTHRDGEiawQALALAGATALVGRDVT----TLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 151 ---------RPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDV 221
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
..
gi 697052228 222 YT 223
Cdd:PRK13547 243 LT 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-193 |
3.33e-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: 76.36 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFsdvqvlDSLNLSVAPGS-----RTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdenSFVPAHL 76
Cdd:COG1245 342 VEYPDLTKSY------GGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI-----SYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 RRIGFVPQEGALFPHLNVAdniawgLDGT--RHE--KRQRVEALMemvslDRQLAthwphEISGGQQQRVALARALAQRP 152
Cdd:COG1245 411 SPDYDGTVEEFLRSANTDD------FGSSyyKTEiiKPLGLEKLL-----DKNVK-----DLSGGELQRVAIAACLSRDA 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHD 193
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-210 |
3.79e-15 |
|
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: 73.52 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRiVMQGRTLFDENSFVPAHLRR---IGFVPQEGAL 88
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK-VHWSNKNESEPSFEATRSRNrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FpHLNVADNIAWGldgtRHEKRQRVEALMEMVSL--DRQLATHWPH--------EISGGQQQRVALARALAQRPSLMLLD 158
Cdd:cd03290 91 L-NATVEENITFG----SPFNKQRYKAVTDACSLqpDIDLLPFGDQteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 159 EPFSALDTGLR-AMTRKATADLLAEAGVASILVTHdQNEALSFATQVAVMRSG 210
Cdd:cd03290 166 DPFSALDIHLSdHLMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-219 |
3.94e-15 |
|
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: 76.52 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfdensfvpahlrrIGFVPQEgALFPH 91
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------VAYVPQQ-AWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LNVADNIAWGLDGTRHEKRQRVEAL-----MEMV-SLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:TIGR00957 713 DSLRENILFGKALNEKYYQQVLEACallpdLEILpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 166 TGL-RAMTRKATADLLAEAGVASILVTHdqneALSFATQV---AVMRSGRFTQVGtPY 219
Cdd:TIGR00957 793 AHVgKHIFEHVIGPEGVLKNKTRILVTH----GISYLPQVdviIVMSGGKISEMG-SY 845
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-200 |
7.61e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 7.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfVPAHLRR--IGFVPQEGAL---FPH 91
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-------TRQALQKnlVAYVPQSEEVdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 LnVADNIAWGLDG-------TRHEKRQRVEALMEMVSL----DRQLAthwphEISGGQQQRVALARALAQRPSLMLLDEP 160
Cdd:PRK15056 96 L-VEDVVMMGRYGhmgwlrrAKKRDRQIVTAALARVDMvefrHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 697052228 161 FSALDTGLRAMTRKATADLLAEaGVASILVTHDQNEALSF 200
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEF 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-165 |
2.92e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 74.18 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtlfdensfvpAHLRRIGFVPQEGALFPHlNVA 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------------KHSGRISFSPQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 96 DNIAWGLDGTRHEKRQRVEA--LMEMVSL----DRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIKAcqLEEDIALfpekDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-211 |
5.29e-14 |
|
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: 72.55 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAG-FETPDTGRIVMQGRTLFDEN---------SFVPAHLRRIGFVPQEG 86
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNpaqairagiAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 87 alfphlnVADNIAWG-LDgtRHEKRQRVEALMEMVSLDR-----QLATHWPH----EISGGQQQRVALARALAQRPSLML 156
Cdd:TIGR02633 356 -------VGKNITLSvLK--SFCFKMRIDAAAELQIIGSaiqrlKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 157 LDEPFSALDTGLRAMTRKATaDLLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLI-NQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-217 |
7.27e-14 |
|
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: 71.04 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtlfdensfvpAHLRRIGFVPQEGALFPHlNVA 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------------KHSGRISFSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 DNIAWGLDGTRHEKRQRVEA------LMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGL- 168
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKAcqleedITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTe 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 697052228 169 RAMTRKATADLLAEAgvASILVThDQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:cd03291 196 KEIFESCVCKLMANK--TRILVT-SKMEHLKKADKILILHEGSSYFYGT 241
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-197 |
9.57e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.97 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGfETPDT--------GRIVMQGRTLFDENsfvpahlRRIGF 81
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGETIWDIK-------KHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VpqEGALfpHL------NVADNIAWGL-------DGTRHEKRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARAL 148
Cdd:PRK10938 341 V--SSSL--HLdyrvstSVRNVILSGFfdsigiyQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRAL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 697052228 149 AQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEA 197
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-160 |
1.29e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.69 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 3 ELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGfetpdtGRIVMQGR-TLFDENSFVPAHLR---- 77
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG------ARKIQQGRvEVLGGDMADARHRRavcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 78 RIGFVPQ--EGALFPHLNVADNIA-----WGLDgtRHEKRQRVEALMEMVSL----DRQLAthwphEISGGQQQRVALAR 146
Cdd:NF033858 77 RIAYMPQglGKNLYPTLSVFENLDffgrlFGQD--AAERRRRIDELLRATGLapfaDRPAG-----KLSGGMKQKLGLCC 149
|
170
....*....|....
gi 697052228 147 ALAQRPSLMLLDEP 160
Cdd:NF033858 150 ALIHDPDLLILDEP 163
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-225 |
1.59e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 70.32 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPDTGRI-----VMQGRTLFDensfVPAHLRR------IGFV 82
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLK----LSPRERRkiigreIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 83 PQE--GALFPHLNVADNI-----AWGLDGT----RHEKRQRVEALMEMVSL--DRQLATHWPHEISGGQQQRVALARALA 149
Cdd:COG4170 95 FQEpsSCLDPSAKIGDQLieaipSWTFKGKwwqrFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 150 QRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-192 |
2.26e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.90 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFS---DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRR-IGFVPQE 85
Cdd:PRK10790 347 SFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL---SSLSHSVLRQgVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 GALFPHlNVADNIAWGldgtRHEKRQRVEALMEMVSLdRQLATHWPHEI-----------SGGQQQRVALARALAQRPSL 154
Cdd:PRK10790 424 PVVLAD-TFLANVTLG----RDISEEQVWQALETVQL-AELARSLPDGLytplgeqgnnlSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 155 MLLDEPFSALDTG--------LRAMTRKATADLLA-------EAGvaSILVTH 192
Cdd:PRK10790 498 LILDEATANIDSGteqaiqqaLAAVREHTTLVVIAhrlstivEAD--TILVLH 548
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-214 |
2.51e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGF--------------ETPDTGRIVMQ-------------- 61
Cdd:PTZ00265 1177 SRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneHTNDMTNEQDYqgdeeqnvgmknvn 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 62 --------------------GRTLFDENSFVPAHLRRI----GFVPQEGALFpHLNVADNIAWGLDGTRHEKRQRV---E 114
Cdd:PTZ00265 1257 efsltkeggsgedstvfknsGKILLDGVDICDYNLKDLrnlfSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRAckfA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 115 ALMEMV-SLDRQLATH---WPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILV 190
Cdd:PTZ00265 1336 AIDEFIeSLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
250 260
....*....|....*....|....*...
gi 697052228 191 THdQNEALSFATQVAVM----RSGRFTQ 214
Cdd:PTZ00265 1416 AH-RIASIKRSDKIVVFnnpdRTGSFVQ 1442
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-165 |
3.08e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 17 LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETP-DTGRIVMQGRtlfdensfvpahlrrIGFVPQEGALFpHLNVA 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGS---------------VAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052228 96 DNIAWGLD--GTRHEKRQRVEALMEMVSL----DRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:PLN03232 697 ENILFGSDfeSERYWRAIDVTALQHDLDLlpgrDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-272 |
5.11e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.66 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtlfdENSFvpAHLRRIG 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER---------QSQF--SHITRLS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 F------VPQEgalFPHLNvADNIAWGLDGT----------RHEKRQRVEALMEMVSLDRQLATHWPHeISGGQQQRVAL 144
Cdd:PRK10938 72 FeqlqklVSDE---WQRNN-TDMLSPGEDDTgrttaeiiqdEVKDPARCEQLAQQFGITALLDRRFKY-LSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 145 ARALAQRPSLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVytr 224
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLAS-LHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI--- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 225 pvdeetalfLGDAVIlpAQLA-----AGYAVCALGEVPTDNAQATGQGRVMMR 272
Cdd:PRK10938 223 ---------LQQALV--AQLAhseqlEGVQLPEPDEPSARHALPANEPRIVLN 264
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-165 |
1.03e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSfvpAHLRRIG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC---TYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHLNVADNIAWGLDGTrhEKRQRVEALMEMVSLDRQLatHWP-HEISGGQQQRVALARALAQRPSLMLLDE 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIHFS--PGAVGITELCRLFSLEHLI--DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
....*.
gi 697052228 160 PFSALD 165
Cdd:PRK13540 154 PLVALD 159
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-193 |
1.10e-12 |
|
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: 67.01 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 23 SVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRivMQGRTLFDE--NSFVPAHLR-----------RIGFVPQEGALF 89
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEilDEFRGSELQnyftkllegdvKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHL---NVADNIawgldgTRHEKRQRVEALMEMVSLDRQLATHWPHeISGGQQQRVALARALAQRPSLMLLDEPFSALDT 166
Cdd:cd03236 100 PKAvkgKVGELL------KKKDERGKLDELVDQLELRHVLDRNIDQ-LSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 697052228 167 GLRaMTRKATADLLAEAGVASILVTHD 193
Cdd:cd03236 173 KQR-LNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-211 |
1.53e-12 |
|
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: 65.75 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 7 ISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGfETPDTGRIvmQGRTLFDENSFVPAHL---RRIGFVP 83
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSV--EGDIHYNGIPYKEFAEkypGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 84 QEGALFPHLNVADNIAWGLDGTRHekrqrvealmEMVSldrqlathwphEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCKGN----------EFVR-----------GISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 697052228 164 LD--TGLR-AMTRKATADLLAEAGVASILVTHDqnEALSFATQVAVMRSGR 211
Cdd:cd03233 149 LDssTALEiLKCIRTMADVLKTTTFVSLYQASD--EIYDLFDKVLVLYEGR 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-194 |
1.82e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVM----------QGRTLF---D 67
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgiklgyfaQHQLEFlraD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 68 ENSFvpAHLRRIGFVPQEGALFPHLNvadniAWGLDGTRhekrqrvealmemvsldrqlATHWPHEISGGQQQRVALARA 147
Cdd:PRK10636 392 ESPL--QHLARLAPQELEQKLRDYLG-----GFGFQGDK--------------------VTEETRRFSGGEKARLVLALI 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 697052228 148 LAQRPSLMLLDEPFSALDTGLramtRKATADLLAEAGVASILVTHDQ 194
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDM----RQALTEALIDFEGALVVVSHDR 487
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-202 |
2.05e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.93 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 26 PGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqgrtlfdensfvpahlrrigfvpqegalfphlnvadniawgLDGT 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 106 RHEKRQRVEALMEMVsldrqlaTHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRK-----ATADLL 180
Cdd:smart00382 40 DILEEVLDQLLLIIV-------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLK 112
|
170 180
....*....|....*....|..
gi 697052228 181 AEAGVASILVTHDQNEALSFAT 202
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALL 134
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-214 |
3.49e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 20 LNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRRIGFV--P---QEGALFphlnV 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI---NALSTAQRLARGLVylPedrQSSGLY----L 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDGTRHE------KRQRVEALMEmvSLDRQLATHWPHE------ISGGQQQRVALARALAQRPSLMLLDEPFS 162
Cdd:PRK15439 355 DAPLAWNVCALTHNrrgfwiKPARENAVLE--RYRRALNIKFNHAeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 697052228 163 ALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQ 214
Cdd:PRK15439 433 GVDVSARNDIYQLIRS-IAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-211 |
5.91e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAG-FEtpdtgriVMQGRTLFDensfvpahlRRIGFVPQEgALFPHLNV 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFE-------ISEGRVWAE---------RSIAYVPQQ-AWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWgLDGTRHEKRQRVEALMEMVSLDRQLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLDEPFSALD-- 165
Cdd:PTZ00243 738 RGNILF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIgekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALDah 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 697052228 166 TGLRAMTRkatADLLAEAGVASILVTHdQNEALSFATQVAVMRSGR 211
Cdd:PTZ00243 817 VGERVVEE---CFLGALAGKTRVLATH-QVHVVPRADYVVALGDGR 858
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-193 |
6.06e-12 |
|
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: 66.35 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 26 PGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVM-----------QGRTLFDensfvpaHLRRIgfvpQEGALfphlNV 94
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfRGTELQD-------YFKKL----ANGEI----KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 A------DNIAWGLDGT------RHEKRQRVEALMEMVSL----DRQLAthwphEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:COG1245 163 AhkpqyvDLIPKVFKGTvrelleKVDERGKLDELAEKLGLenilDRDIS-----ELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 697052228 159 EPFSALDTGLRAMTRKATADlLAEAGVASILVTHD 193
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRE-LAEEGKYVLVVEHD 271
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-217 |
1.25e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFetPD----TGRIVMQGRTLFDENSFVPAHL 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 77 R-RIGF-VPQEgalFPHLNVAD--NIAWgldGTRHEKRQRVEA-----------LMEMVSLDRQLATHWPHE-ISGGQQQ 140
Cdd:CHL00131 85 GiFLAFqYPIE---IPGVSNADflRLAY---NSKRKFQGLPELdplefleiineKLKLVGMDPSFLSRNVNEgFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 141 RVALARALAQRPSLMLLDEPFSALDT-GLRAMTRkaTADLLAEAGVASILVTHDQNeALSFATQ--VAVMRSGRFTQVGT 217
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIdALKIIAE--GINKLMTSENSIILITHYQR-LLDYIKPdyVHVMQNGKIIKTGD 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-217 |
1.40e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 12 SDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIGFVPQEGALFPH 91
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--LDSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 lNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHWPHEI-------SGGQQQRVALARALAQRPSLMLLDEPFSAL 164
Cdd:PRK10789 404 -TVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVgergvmlSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 165 D--------TGLRAMTRKATadllaeagvasILVTHDQNEALSFATQVAVMRSGRFTQVGT 217
Cdd:PRK10789 483 DgrtehqilHNLRQWGEGRT-----------VIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-224 |
1.87e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLlRILAGFETPDTGRIVMQGRTLFDENSfvpAHLRRIGF 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRR---ALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 -VPQEGALFPHLNVADN---IAWGLDGTRHEKRQRVEALMEMVSLDrQLATHWPHEISGGQQQRVALARALAQRPSLMLL 157
Cdd:NF000106 90 hRPVR*GRRESFSGRENlymIGR*LDLSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 158 DEPfsalDTGLRAMTRKATAD---LLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTR 224
Cdd:NF000106 169 DEP----TTGLDPRTRNEVWDevrSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-211 |
1.96e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 4 LTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAG-FETPDTGRIVMQGRTLFDENS---------FVP 73
Cdd:PRK13549 265 LTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPqqaiaqgiaMVP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 74 AHLRRIGFVPQegalfphLNVADNIAWG-LDgtRHEKRQRVEALMEMVSLDRQLA-----THWPH----EISGGQQQRVA 143
Cdd:PRK13549 345 EDRKRDGIVPV-------MGVGKNITLAaLD--RFTGGSRIDDAAELKTILESIQrlkvkTASPElaiaRLSGGNQQKAV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 144 LARALAQRPSLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQ-LVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-211 |
2.67e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 21 NLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSfvPAHLRRIGFV------PQEGaLFPHLNV 94
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRS--PRDAIRAGIMlcpedrKAEG-IIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAwgLDGTRHEKRQR--VEALMEMVSLDRQLA-----THWPHE----ISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:PRK11288 349 ADNIN--ISARRHHLRAGclINNRWEAENADRFIRslnikTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 697052228 164 LDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK11288 427 IDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-201 |
4.79e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETpdTGRI-----VMQGRTLfdENSFVpahlRRIGFVPQEGA 87
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVItggdrLVNGRPL--DSSFQ----RSIGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 88 LFPHLNVADNIAWGL------DGTRHEKRQRVEALMEMVSLdRQLATHWPHEISGG----QQQRVALARALAQRPSLML- 156
Cdd:TIGR00956 847 HLPTSTVRESLRFSAylrqpkSVSKSEKMEYVEEVIKLLEM-ESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 697052228 157 LDEPFSALDtglrAMTRKATADL---LAEAGVAsILVTHDQNEALSFA 201
Cdd:TIGR00956 926 LDEPTSGLD----SQTAWSICKLmrkLADHGQA-ILCTIHQPSAILFE 968
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-192 |
5.50e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 13 DVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQgrtlfDENSFVPAHLR----RIGFVPQEGAL 88
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-----DSHNLKDINLKwwrsKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 FPHlNVADNIAWGL---------------DG--------TRHEKRQRVEALM-------------------------EMV 120
Cdd:PTZ00265 472 FSN-SIKNNIKYSLyslkdlealsnyyneDGndsqenknKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsEVV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 121 SLDRQLATH-----WP-----------HEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAG 184
Cdd:PTZ00265 551 DVSKKVLIHdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
....*...
gi 697052228 185 VASILVTH 192
Cdd:PTZ00265 631 RITIIIAH 638
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-192 |
1.32e-10 |
|
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: 62.46 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPdtgriVMQGRTLFDENSfvpahlrRIGFVPQEgalfPHLNVA 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WP-----VYGGRLTKPAKG-------KLFYVPQR----PYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 96 ---DNIAWGlDGTRHEKR-----QRVEALMEMVSLDRQL--------ATHWPHEISGGQQQRVALARALAQRPSLMLLDE 159
Cdd:TIGR00954 530 tlrDQIIYP-DSSEDMKRrglsdKDLEQILDNVQLTHILereggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....
gi 697052228 160 PFSALDTGLR-AMTRkatadLLAEAGVASILVTH 192
Cdd:TIGR00954 609 CTSAVSVDVEgYMYR-----LCREFGITLFSVSH 637
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-225 |
1.33e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPDTGRIVMQgRTLFDENSFV---PAHLRR-----IGFVPQE 85
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTAD-RMRFDDIDLLrlsPRERRKlvghnVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 --GALFPHLNVADNI-----AWGLDGT-----RHEKRQRVEALMEMVSLDRQLATH-WPHEISGGQQQRVALARALAQRP 152
Cdd:PRK15093 98 pqSCLDPSERVGRQLmqnipGWTYKGRwwqrfGWRKRRAIELLHRVGIKDHKDAMRsFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 153 SLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASILVTHDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRP 225
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-213 |
2.02e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQ--------VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIvmqgrtlfdensFVPAHLRRigf 81
Cdd:PLN03073 510 SFSDASfgypggplLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------------FRSAKVRM--- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 vpqegALFPHLNVAdniawGLDGTRHE-----------KRQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQ 150
Cdd:PLN03073 575 -----AVFSQHHVD-----GLDLSSNPllymmrcfpgvPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052228 151 RPSLMLLDEPFSALDtgLRAMTRKATADLLAEAGVasILVTHDQNEALSFATQVAVMRSGRFT 213
Cdd:PLN03073 645 KPHILLLDEPSNHLD--LDAVEALIQGLVLFQGGV--LMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-233 |
3.54e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRRI-GFVPQEGALFphlnv 94
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAKFGLTDLRRVlSIIPQSPVLF----- 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDG-TRHEKRQRVEAL-----MEMVS-----LDRQLaTHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:PLN03232 1323 SGTVRFNIDPfSEHNDADLWEALerahiKDVIDrnpfgLDAEV-SEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVasILVTHDQNEALSfATQVAVMRSGRFTQVGTPYDVYTRpvdEETALF 233
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR---DTSAFF 1465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-193 |
4.68e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 3 ELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMqGRTL----FDEnsfvpahlrr 78
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLevayFDQ---------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 igfvpQEGALFPHLNVADNIAWG-----LDG-TRH-----------EKRQR--VEALmemvsldrqlathwpheiSGGQQ 139
Cdd:PRK11147 390 -----HRAELDPEKTVMDNLAEGkqevmVNGrPRHvlgylqdflfhPKRAMtpVKAL------------------SGGER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 140 QRVALARaLAQRPS-LMLLDEPFSALDTglramtrkATADLLAEAgVAS-----ILVTHD 193
Cdd:PRK11147 447 NRLLLAR-LFLKPSnLLILDEPTNDLDV--------ETLELLEEL-LDSyqgtvLLVSHD 496
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-159 |
6.19e-10 |
|
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: 60.20 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 20 LNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfVPAHLRRIGFVPQEGALFPHLnvadnia 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN--REAYRQLFSAVFSDFHLFDRL------- 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 100 WGLDGTrhEKRQRVEALMEMVSLDRQLA--------ThwphEISGGQQQRVALARALA-QRPsLMLLDE 159
Cdd:COG4615 422 LGLDGE--ADPARARELLERLELDHKVSvedgrfstT----DLSQGQRKRLALLVALLeDRP-ILVFDE 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
10-165 |
6.38e-10 |
|
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: 57.72 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 10 SFSDVQV--LDSLNLSVAPGSRTAIVGPSGSGKTTLLriLAGFETPDTGRIVmQGRTLFDENSFVpahlrrigFVPQEGA 87
Cdd:cd03238 2 TVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLI-SFLPKFSRNKLI--------FIDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 88 LfphlnvadnIAWGLdgtrhekrqrvealmEMVSLDRQLAThwpheISGGQQQRVALARALAQRP--SLMLLDEPFSALD 165
Cdd:cd03238 71 L---------IDVGL---------------GYLTLGQKLST-----LSGGELQRVKLASELFSEPpgTLFILDEPSTGLH 121
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-218 |
6.67e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 58.77 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLlrILAGFETPDT--GRIVMQGRTLfdenSFVPAH-LR-RIGFVPQEGALFph 91
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIfdGKIVIDGIDI----SKLPLHtLRsRLSIILQDPILF-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 92 lnvADNIAWGLDGTRHEKRQRVEALMEMVSLDRQ----------LATHWPHEISGGQQQRVALARALAQRPSLMLLDEPF 161
Cdd:cd03288 108 ---SGSIRFNLDPECKCTDDRLWEALEIAQLKNMvkslpggldaVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 162 SALDTGLRAMTRKATADLLAEAGVASIlvTHDQNEALSfATQVAVMRSGRFTQVGTP 218
Cdd:cd03288 185 ASIDMATENILQKVVMTAFADRTVVTI--AHRVSTILD-ADLVLVLSRGILVECDTP 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-211 |
2.02e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 32 IVGPSG---SGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvpahlrrigfvPQEG---------------ALFPHLN 93
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS-------------PQDGlangivyisedrkrdGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 94 VADNI----------AWGldGTRH-EKRQRVEALMEMV-----SLDRQLAthwphEISGGQQQRVALARALAQRPSLMLL 157
Cdd:PRK10762 347 VKENMsltalryfsrAGG--SLKHaDEQQAVSDFIRLFniktpSMEQAIG-----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 158 DEPFSALDTGlramTRKATADLL---AEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK10762 420 DEPTRGVDVG----AKKEIYQLInqfKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-215 |
3.67e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFE--TPDTGRIVMQGRTLFD--------ENS 70
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLElspedragEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 71 FVP-AHLRRIGFVPQEGALFPHLNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHWPHE-ISGGQQQRVALARAL 148
Cdd:PRK09580 81 FMAfQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052228 149 AQRPSLMLLDEPFSALDT-GLRAMTRKATAdlLAEAGVASILVTHDQN-------EALSFATQVAVMRSGRFTQV 215
Cdd:PRK09580 161 VLEPELCILDESDSGLDIdALKIVADGVNS--LRDGKRSFIIVTHYQRildyikpDYVHVLYQGRIVKSGDFTLV 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-174 |
4.79e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGrtlFDENSFVPAHLRRI-GFVPQEGALFphlnv 94
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG---CDISKFGLMDLRKVlGIIPQAPVLF----- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 95 ADNIAWGLDG-TRHEKRQRVEALMEM----------VSLDRQLAtHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:PLN03130 1326 SGTVRFNLDPfNEHNDADLWESLERAhlkdvirrnsLGLDAEVS-EAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170
....*....|.
gi 697052228 164 LDTGLRAMTRK 174
Cdd:PLN03130 1405 VDVRTDALIQK 1415
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-165 |
5.06e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPD--TGRIVMQGRTLFDENsfvpahLRRI-GFVPQEGALFP 90
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQET------FARIsGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 91 HLNVADNIAWGL------DGTRHEKRQRVEALMEMVSLD--RQLATHWP--HEISGGQQQRVALARALAQRPSLMLLDEP 160
Cdd:PLN03140 967 QVTVRESLIYSAflrlpkEVSKEEKMMFVDEVMELVELDnlKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 697052228 161 FSALD 165
Cdd:PLN03140 1047 TSGLD 1051
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-193 |
6.21e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 26 PGSRTAIVGPSGSGKTTLLRILAGFETPDTGRI--------VMQ---GRTLFD------ENSFVPAHlrrigfVPQEgal 88
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKrfrGTELQNyfkklyNGEIKVVH------KPQY--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 89 fphlnvADNIAWGLDGT------RHEKRQRVEALMEMVSL----DRQLathwpHEISGGQQQRVALARALAQRPSLMLLD 158
Cdd:PRK13409 169 ------VDLIPKVFKGKvrellkKVDERGKLDEVVERLGLenilDRDI-----SELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 697052228 159 EPFSALDTGLRAMTRKATADLLAEAGVasILVTHD 193
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHD 270
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
6-193 |
6.35e-09 |
|
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: 54.89 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 6 AISKSFSDVQVLDSLNlSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTlfdensfvpahlrrIGFVPQE 85
Cdd:cd03222 5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT--------------PVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 86 galfphlnvadniawgldgtrhekrqrvealmemVSLdrqlathwpheiSGGQQQRVALARALAQRPSLMLLDEPFSALD 165
Cdd:cd03222 70 ----------------------------------IDL------------SGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180
....*....|....*....|....*...
gi 697052228 166 TGLRAMTRKATADLLAEAGVASILVTHD 193
Cdd:cd03222 104 IEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-221 |
1.08e-08 |
|
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: 56.88 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTT----LLRILAGFEtpdtGRIVMQGRTLFDensfVPAH-LR-RIGFVPQEGALF 89
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAE----GEIIIDGLNIAK----IGLHdLRfKITIIPQDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 ---------PHLNVADNIAWGLDGTRHEKrQRVEALMEmvSLDRQLAtHWPHEISGGQQQRVALARALAQRPSLMLLDEP 160
Cdd:TIGR00957 1373 sgslrmnldPFSQYSDEEVWWALELAHLK-TFVSALPD--KLDHECA-EGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 161 FSALDTGLRAMTRKATADLLAEAGVASIlvTHDQNEALSFaTQVAVMRSGRFTQVGTPYDV 221
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTI--AHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-234 |
1.04e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 14 VQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILA----GFETPDTGRIVMQGRTLFDENSFVPAHLRRIGfvpQEGALF 89
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNA---ETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 PHLNVADNIAW----------GLDGTRHEKRQRVEAL-MEMVSLDRQLATHWPHE----ISGGQQQRVALARALAQRPSL 154
Cdd:TIGR00956 151 PHLTVGETLDFaarcktpqnrPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNDfvrgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 155 MLLDEPFSALD--TGL---RAMtrKATADLLAeagvASILVTHDQ--NEALSFATQVAVMRSGrftqvgtpYDVYTRPVD 227
Cdd:TIGR00956 231 QCWDNATRGLDsaTALefiRAL--KTSANILD----TTPLVAIYQcsQDAYELFDKVIVLYEG--------YQIYFGPAD 296
|
....*..
gi 697052228 228 EETALFL 234
Cdd:TIGR00956 297 KAKQYFE 303
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
1.06e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 1 MLELTAISKSFSDVQVLDsLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfdeNSFVPAHLRRIG 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI---NNIAKPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 fvpQEGALFPHLNVADNIA-WGldgtrhEKRQRVEALMEMVS-------LDRQLAThwpheISGGQQQRVALARALAQRP 152
Cdd:PRK13541 77 ---HNLGLKLEMTVFENLKfWS------EIYNSAETLYAAIHyfklhdlLDEKCYS-----LSSGMQKIVAIARLIACQS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 697052228 153 SLMLLDEpfsaLDTGLRAMTRKATADLL---AEAGVASILVTHDQN 195
Cdd:PRK13541 143 DLWLLDE----VETNLSKENRDLLNNLIvmkANSGGIVLLSSHLES 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-192 |
1.25e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDtGRIVMQGRTLfdeNSFVPAHLRR-IGFVPQEGALF----- 89
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSW---NSVTLQTWRKaFGVIPQKVFIFsgtfr 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 90 ----PHLNVADNIAWgldgtRHEKRQRVEALMEMV--SLDRQLATHwPHEISGGQQQRVALARALAQRPSLMLLDEPFSA 163
Cdd:TIGR01271 1310 knldPYEQWSDEEIW-----KVAEEVGLKSVIEQFpdKLDFVLVDG-GYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180
....*....|....*....|....*....
gi 697052228 164 LDTGLRAMTRKATADLLAEAGVasILVTH 192
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQSFSNCTV--ILSEH 1410
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-195 |
1.31e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 30 TAIVGPSGSGKTTLLR-ILAGF--ETPDTGRIVMQGRTLFDENSfvpahlrRIGFVpqegalfpHLNVadniaWGLDGTR 106
Cdd:cd03240 25 TLIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGE-------VRAQV--------KLAF-----ENANGKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 107 HEKRQRVEALMEMVSLdRQLATHWPHEI-----SGGQQQ------RVALARALAQRPSLMLLDEPFSALDTGLRamtRKA 175
Cdd:cd03240 85 YTITRSLAILENVIFC-HQGESNWPLLDmrgrcSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI---EES 160
|
170 180
....*....|....*....|....
gi 697052228 176 TADLLAEAGVAS----ILVTHDQN 195
Cdd:cd03240 161 LAEIIEERKSQKnfqlIVITHDEE 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-214 |
4.04e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 20 LNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENsfvPAHLRR-IGFVPQEGALFPHLnvadni 98
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ---PEDYRKlFSAVFTDFHLFDQL------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 99 aWGLDGTRHEKrQRVEALMEMVSLDRQLaTHWPHEI-----SGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTR 173
Cdd:PRK10522 413 -LGPEGKPANP-ALVEKWLERLKMAHKL-ELEDGRIsnlklSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 697052228 174 KATADLLAEAGVASILVTHDqNEALSFATQVAVMRSGRFTQ 214
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-168 |
2.08e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDVQ---------VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRtlfDENSFVPAHLRR-IG 80
Cdd:PTZ00243 1311 FEGVQmryreglplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR---EIGAYGLRELRRqFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 81 FVPQEGALFPHlNVADNIAWGLDGTRHEkrqrVEALMEMVSLDRQLAThwphEISG--------------GQQQRVALAR 146
Cdd:PTZ00243 1388 MIPQDPVLFDG-TVRQNVDPFLEASSAE----VWAALELVGLRERVAS----ESEGidsrvleggsnysvGQRQLMCMAR 1458
|
170 180
....*....|....*....|...
gi 697052228 147 ALAQRPS-LMLLDEPFSALDTGL 168
Cdd:PTZ00243 1459 ALLKKGSgFILMDEATANIDPAL 1481
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-166 |
2.96e-06 |
|
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: 46.58 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 25 APGSRTAIVGPSGSGKTTLLR---ILAGFETPDTGRivmqgRTLFDENSFVPA-HLRRIGFVPQegalfphlnvadniaw 100
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDaigLALGGAQSATRR-----RSGVKAGCIVAAvSAELIFTRLQ---------------- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 101 gldgtrhekrqrvealmemvsldrqlathwpheISGGQQQRVALARALA----QRPSLMLLDEPFSALDT 166
Cdd:cd03227 78 ---------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-165 |
5.14e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 11 FSDVQV-------LDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGR-TLFDENSFVPA-HLRRIGF 81
Cdd:PRK10636 4 FSSLQIrrgvrvlLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPAlPQPALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 82 VPQEGALFPHLNVADNIAWGL-DG----TRHEK---------RQRVEALMEMVSLDRQLATHWPHEISGGQQQRVALARA 147
Cdd:PRK10636 84 VIDGDREYRQLEAQLHDANERnDGhaiaTIHGKldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
|
170
....*....|....*...
gi 697052228 148 LAQRPSLMLLDEPFSALD 165
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLD 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-211 |
4.60e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 4.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 134 ISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADlLAEAGVASILVTHDQNEALSFATQVAVMRSGR 211
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE-LAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-218 |
5.04e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 34 GPSGSGKTTLLRILAGFETPDTGRIVMQGRTLfDENSFvpAHLRRIGFVPQEGALFPHLNVADNIA-----WGLdgTRHE 108
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDI--ATRRRVGYMSQAFSLYGELTVRQNLElharlFHL--PAAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 109 KRQRVEALMEMVSLdRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDTGLRAMTRKATADLLAEAGVASI 188
Cdd:NF033858 374 IAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIF 452
|
170 180 190
....*....|....*....|....*....|....*
gi 697052228 189 LVTHDQNEAL-----SFatqvavMRSGRFTQVGTP 218
Cdd:NF033858 453 ISTHFMNEAErcdriSL------MHAGRVLASDTP 481
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-193 |
5.46e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 2 LELTAIsKSFSDVQVLDsLNLSVapgsrTAIVGPSGSGKTTLLR-ILAGF--ETPDTGRIVMQGRTLFDENSFVPAHLRR 78
Cdd:COG0419 5 LRLENF-RSYRDTETID-FDDGL-----NLIVGPNGAGKSTILEaIRYALygKARSRSKLRSDLINVGSEEASVELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 79 IGFV-----PQ-EGALFPH---------------LNVADNIAWGLDGTRHEKRQRVEALMEMVSLDRQLATHW-----PH 132
Cdd:COG0419 78 GGKRyrierRQgEFAEFLEakpserkealkrllgLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052228 133 EISGGQQQRVALARALAqrpslMLLDepFSALDTGlramTRKATADLLAEAGVasilVTHD 193
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEE----RLERLLDALEELAI----ITHV 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
112-229 |
1.03e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 112 RVEALMEMVSLDRQLATHWPHEISGGQQQRVALARALAQRPSLMLLDEPFSALDtgLRAMTRKATadLLAEAGVASILVT 191
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLET--YLLKWPKTFIVVS 398
|
90 100 110
....*....|....*....|....*....|....*...
gi 697052228 192 HDQNEALSFATQVAVMRSGRFTQVGTPYDVYTRPVDEE 229
Cdd:PLN03073 399 HAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQ 436
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
16-60 |
8.54e-04 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 39.83 E-value: 8.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFeTPDTGRIVM 60
Cdd:cd01130 1 MAAFLRLAVRARKNILISGGTGSGKTTLLNALLSF-IPPDERIVT 44
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
31-58 |
8.70e-04 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 39.01 E-value: 8.70e-04
10 20 30
....*....|....*....|....*....|.
gi 697052228 31 AIVGPSGSGKTTLLRILA---GFETPDTGRI 58
Cdd:cd02020 3 AIDGPAGSGKSTVAKLLAkklGLPYLDTGGI 33
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
24-192 |
1.53e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 39.29 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 24 VAPGSRTAIVGPSGSGKTTLLRILAgfetpdtgRIVMQGRTLFDENsfvpahlrrigFVPQEGA-LFphlnvadniaWGL 102
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLA--------AAVATGKPWLGGP-----------RVPEQGKvLY----------VSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 103 DGTRHEKRQRVEALMEMVSLDRQLATHW-------PHEISGGQ---QQRVALARALAQR--PSLMLLDePFSAL----DT 166
Cdd:pfam13481 81 EGPADELRRRLRAAGADLDLPARLLFLSlveslplFFLDRGGPlldADVDALEAALEEVedPDLVVID-PLARAlggdEN 159
|
170 180
....*....|....*....|....*...
gi 697052228 167 GLRAMTR--KATADLLAEAGVASILVTH 192
Cdd:pfam13481 160 SNSDVGRlvKALDRLARRTGATVLLVHH 187
|
|
| cmk |
TIGR00017 |
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ... |
31-96 |
3.11e-03 |
|
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 129128 [Multi-domain] Cd Length: 217 Bit Score: 38.56 E-value: 3.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052228 31 AIVGPSGSGKTTLLRILA---GFETPDTGRI--------VMQGRTLFDENSFVPAHLR-RIGFVPQEGALFPHLNVAD 96
Cdd:TIGR00017 6 AIDGPSGAGKSTVAKAVAeklGYAYLDSGAMyraialaaLQNRVDLTSEDALAELISHlDIRFIPTNGEVEVFLNGED 83
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
9-58 |
3.16e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 3.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 697052228 9 KSFSDVqvldSLNLSVAPGsRTAIVGPSGSGKTTLLRILAGFETPDTGRI 58
Cdd:COG3950 12 RGFEDL----EIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-73 |
3.98e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 3.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 697052228 24 VAPGSRTAIVGPSGSGKTTLLRILAGFETPD---TGRIVMQGRTLfdeNSFVP 73
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRL---NEFVP 237
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-48 |
4.19e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.49 E-value: 4.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 697052228 9 KSFSDVQVLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILA 48
Cdd:COG1106 11 RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALY 50
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
29-81 |
5.58e-03 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 37.24 E-value: 5.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 697052228 29 RTAIVGPSGSGKTTLLRILA---GFET-PDTGRIVMQGRtLFDENSFVPAHLRRIGF 81
Cdd:pfam13521 1 RIVITGGPSTGKTTLAEALAarfGYPVvPEAAREILEEL-GADGGDALPWVEDLLAF 56
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
16-72 |
5.84e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 37.73 E-value: 5.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 697052228 16 VLDSLNLSVAPGSRTAIVGPSGSGKTTLLRILAGFETPDTGRIV-MQGRTL-FDENSFV 72
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIgLRGDALpLGANSFI 60
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-118 |
6.40e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 30 TAIVGPSGSGKTTLLRILAGFETPDTGRIVMQGRTLFDENSFVPAHLRRIGFVPQEGALFPHLNVADNIAWGLdGTRHEK 109
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRY-GLDLER 80
|
....*....
gi 697052228 110 RQRVEALME 118
Cdd:pfam13304 81 EDVEEKLSS 89
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
32-59 |
6.68e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 38.22 E-value: 6.68e-03
10 20
....*....|....*....|....*...
gi 697052228 32 IVGPSGSGKTTLLRILAGFeTPDTGRIV 59
Cdd:COG4962 187 VSGGTGSGKTTLLNALSGF-IPPDERIV 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-213 |
8.59e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052228 135 SGGQQQRVALARALAQRPSLMLLDEPFSALDTGlramtrkatA--------DLLAEAGVASILVTHDQNEALSFATQVAV 206
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVG---------AkyeiytiiNELAAEGKGVIVISSELPELLGMCDRIYV 476
|
....*..
gi 697052228 207 MRSGRFT 213
Cdd:NF040905 477 MNEGRIT 483
|
|
|