|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-242 |
5.40e-86 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 255.78 E-value: 5.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLH----VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG---R 73
Cdd:COG1116 3 AAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV-DGKPVTGpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 LAWMGQKDLLYPWLSVRDNVALGARLRGE--KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVpkAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSAADGDIDDSHHLAGTPPRAPD---APDL 226
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRElrtSPEF 241
|
250
....*....|....*.
gi 488994816 227 LIGQAALLQQLMRAQP 242
Cdd:COG1116 242 AALRAEILDLLREEAE 257
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-207 |
7.21e-73 |
|
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: 221.19 E-value: 7.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRL----FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG---RLAWMG 78
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV-DGEPVTGpgpDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QKDLLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPF 156
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 157 SALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSAADGDI 207
Cdd:cd03293 160 SALDALTREQLQEELLDIWRetGKTVLLVTHDIDEAVFLADRVVVLSARPGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-201 |
2.67e-62 |
|
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: 193.89 E-value: 2.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVaSDGQ------PIQGRLAWMGQ 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL-IDGRdvtgvpPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488994816 158 ALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:cd03259 160 ALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMN 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-203 |
3.97e-57 |
|
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: 180.75 E-value: 3.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWM 77
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 158 ALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEAcrLSHRLLVLSAA 203
Cdd:COG4133 161 ALDAAGVALLAELIAAHLArGGAVLLTTHQPLEL--AAARVLDLGDF 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-202 |
1.71e-56 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 183.76 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAW---M 77
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-DGRDVTGLPPEkrnV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 G---QKDLLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:COG3842 80 GmvfQDYALFPHLTVAENVAFGLRMRGVPKAeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488994816 153 DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEEALALADRIAVMND 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-209 |
1.05e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.95 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQ 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 158 ALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:COG1131 161 GLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERLCDRVAIIDKgrivADGTPDE 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
1.85e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 178.13 E-value: 1.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLH----VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAWMG- 78
Cdd:COG4525 2 SMLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-DGVPVTGPGADRGv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 --QKDLLYPWLSVRDNVALGARLRG-EKVDR-ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDE 154
Cdd:COG4525 81 vfQKDALLPWLNVLDNVAFGLRLRGvPKAERrARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 155 PFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSAADGDIDDSHHL-------AGTPPRA 220
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQrtGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELdfsrrflAGEDARA 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-209 |
2.70e-51 |
|
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: 166.96 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQ 79
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 158 ALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLS----AADGDIDD 209
Cdd:COG4555 162 GLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHkgkvVAQGSLDE 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-201 |
4.27e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 169.56 E-value: 4.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCG------EVVASDGQPIQGRLAWMG 78
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlngRDLFTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPF 156
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPpsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 157 SALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDelGGTTVFVTHDQEEALELADRVVVMN 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-209 |
6.44e-49 |
|
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: 160.53 E-value: 6.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMGQK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DGQDITG----LSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DL---------------LYPWLSVRDNVALGARLRG---EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALART 142
Cdd:COG1127 76 ELyelrrrigmlfqggaLFDSLTVFENVAFPLREHTdlsEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTR----IQTLAATLlaGRTVVLITHDPQEACRLSHRLLVLS----AADGDIDD 209
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVidelIRELRDEL--GLTSVVVTHDLDSAFAIADRVAVLAdgkiIAEGTPEE 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-202 |
3.15e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.06 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAWMGQKDLLY- 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL-DGKPLSAMPPPEWRRQVAYv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 ----PWL--SVRDNVALGARLRGEKVDRARVAALLEQVELS-SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:COG4619 80 pqepALWggTVRDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 158 ALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:COG4619 160 ALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-209 |
3.57e-48 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 159.05 E-value: 3.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWM 77
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL-DGRDLASlsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALG-----ARLRGE-KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphlGLFGRPsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 152 MDEPFSALD------TLtrTRIQTLAATllAGRTVVLITHDPQEACRLSHRLLVLS----AADGDIDD 209
Cdd:COG1120 161 LDEPTSHLDlahqleVL--ELLRRLARE--RGRTVVMVLHDLNLAARYADRLVLLKdgriVAQGPPEE 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-223 |
4.69e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 158.38 E-value: 4.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLfdNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGR------LAWMGQ 79
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTALppaerpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALG--ARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlrPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 158 ALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLS----AADGDIDDShhLAGTPPRAPDA 223
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARIADRVLLVAdgriAADGPTAAL--LDGEPPPALAA 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-209 |
1.65e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.17 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQPIQ---GRLAWM 77
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-RLFGKPPRrarRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQK---DLLYPwLSVRDNVALG------ARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP 148
Cdd:COG1121 81 PQRaevDWDFP-ITVRDVVLMGrygrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 149 IVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLS---AADGDIDD 209
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVLLLNrglVAHGPPEE 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-207 |
1.71e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.74 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLS--LHVGDRRL--FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMG 78
Cdd:COG1136 2 SPLLELRNLTksYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI-DGQDISS----LS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QKDL----------------LYPWLSVRDNVALGARLRGE--KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALA 140
Cdd:COG1136 77 ERELarlrrrhigfvfqffnLLPELTALENVALPLLLAGVsrKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 141 RTLYEDRPIVLMDEPFSALDTLTRTRI----QTLAATLlaGRTVVLITHDPqEACRLSHRLLVLSaaDGDI 207
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVlellRELNREL--GTTIVMVTHDP-ELAARADRVIRLR--DGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-207 |
1.10e-46 |
|
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: 154.18 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSL--HVGDRRLF--DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVaSDGQPIQG--------- 72
Cdd:cd03255 1 IELKNLSKtyGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR-VDGTDISKlsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 RLAWMG---QKDLLYPWLSVRDNVALGARLRGEKV--DRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDR 147
Cdd:cd03255 80 RRRHIGfvfQSFNLLPDLTALENVELPLLLAGVPKkeRRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 148 PIVLMDEPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEAcRLSHRLLVLSaaDGDI 207
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELA-EYADRIIELR--DGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-207 |
2.30e-46 |
|
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: 154.20 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMGQKDL--- 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-DGEDISG----LSEAELyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 ------------LYPWLSVRDNVALGARLRG---EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDR 147
Cdd:cd03261 76 rrrmgmlfqsgaLFDSLTVFENVAFPLREHTrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 148 PIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLsaADGDI 207
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVL--YDGKI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-217 |
5.18e-46 |
|
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: 153.16 E-value: 5.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAW------MGQ 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-DGKDITNLPPHkrpvntVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKlpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 158 ALDTLTRTRIQ----TLAATLlaGRTVVLITHDPQEACRLSHRLLVLSAadGDIDDShhlaGTP 217
Cdd:cd03300 160 ALDLKLRKDMQlelkRLQKEL--GITFVFVTHDQEEALTMSDRIAVMNK--GKIQQI----GTP 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-224 |
1.04e-44 |
|
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: 149.80 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASD----GQPIQGR-LAWMGQ 79
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatDVPVQERnVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGEKVD------RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994816 154 EPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVLSAadGDIDDshhlAGTPPRAPDAP 224
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEALEVADRVVVMNK--GRIEQ----VGTPDEVYDHP 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-200 |
4.86e-44 |
|
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: 146.00 E-value: 4.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQ 79
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNValgarlrgekvdrarvaalleqvelsscadarpaTLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:cd03230 81 EPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488994816 160 DTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03230 127 DPESRREFWELLRELKKeGKTILLSSHILEEAERLCDRVAIL 168
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-207 |
1.08e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.22 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAwmGQKDL--- 82
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRDVTDLPP--KDRNIamv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 -----LYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:COG3839 81 fqsyaLYPHMTVYENIAFPLKLRKVPKAeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 156 FSALD----TLTRTRIQTLAATLlaGRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:COG3839 161 LSNLDaklrVEMRAEIKRLHRRL--GTTTIYVTHDQVEAMTLADRIAVMN--DGRI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-202 |
2.91e-43 |
|
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: 144.25 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG----------RLA 75
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDLTDledelpplrrRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWLSVRDNVALGarlrgekvdrarvaalleqvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488994816 156 FSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-201 |
1.34e-42 |
|
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: 143.38 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLHVGD--RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQPIQGRLAWMGQKD--- 81
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV-LVDGKDLTKLSLKELRRKvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 --------LLYPwlSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:cd03225 80 vfqnpddqFFGP--TVEEEVAFGLENLGlpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-207 |
2.40e-42 |
|
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: 144.71 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG------------RLAWMGQKDLLYPWLSVR 90
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-DGQDIAAmsrkelrelrrkKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQ 168
Cdd:cd03294 121 ENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488994816 169 TLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:cd03294 201 DELLRLQAelQKTIVFITHDLDEALRLGDRIAIMK--DGRL 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-200 |
2.65e-42 |
|
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: 143.06 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQPI---QGRLAWMGQK--- 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-RVFGKPLekeRKRIGYVPQRrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DLLYPwLSVRDNVALGARLRGE------KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDE 154
Cdd:cd03235 80 DRDFP-ISVRDVVLMGLYGHKGlfrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 155 PFSALDTLTRTRIQTLAATL-LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-200 |
2.68e-42 |
|
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: 142.82 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGgQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ------------PIQGRLAWMGQKDLLYPWLSVR 90
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTvlfdsrkkinlpPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVALGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTL 170
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|..
gi 488994816 171 AATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03297 174 LKQIKKnlNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-202 |
2.17e-41 |
|
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: 140.72 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLF--DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWM 77
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 156 FSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-200 |
2.24e-41 |
|
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: 141.28 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR-LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAW 76
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI-DGEDIREqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVEL--SSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKwpKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 153 DEPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-220 |
2.55e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 141.76 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGeVVASDGQPIQGRLAWMG---QKDL 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHG-SITLDGKPVEGPGAERGvvfQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 LYPWLSVRDNVALGARLRG-EKVDRARVA-ALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGvEKMQRLEIAhQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 161 TLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSAADGDIDDSHHL-------AGTPPRA 220
Cdd:PRK11248 161 AFTREQMQTLLLKLWQetGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLnfarrfvAGESSRS 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-202 |
1.63e-40 |
|
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: 138.72 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRR----LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI------ 70
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL-AGQDLfalded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 71 ------QGRLAWMGQKDLLYPWLSVRDNVALGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:COG4181 83 ararlrARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRlSHRLLVLSA 202
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAAR-CDRVLRLRA 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-200 |
5.07e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 143.89 E-value: 5.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLH-----VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI----Q 71
Cdd:COG1123 256 AAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF-DGKDLtklsR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 72 GRLAWMGQK---------DLLYPWLSVRDNVALGARLRG---EKVDRARVAALLEQVELS-SCADARPATLSGGMRQRAA 138
Cdd:COG1123 335 RSLRELRRRvqmvfqdpySSLNPRMTVGDIIAEPLRLHGllsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 139 LARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVM 478
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-207 |
5.09e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 138.27 E-value: 5.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 8 VRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDG--QPIQGRLAWMGQKDLLYP 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 WLSVRDNVALGarLRGEKVDRARVAalLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRT 165
Cdd:PRK11247 95 WKKVIDNVGLG--LKGQWRDAALQA--LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488994816 166 RIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:PRK11247 171 EMQDLIESLWQqhGFTVLLVTHDVSEAVAMADRVLLIE--EGKI 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-200 |
5.43e-40 |
|
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: 138.01 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVG----DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAWMGQKD 81
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF-DGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 L----------LYPWLSVRDNVALGARLRGEKVDRARVAALLEQVEL-SSCADARPATLSGGMRQRAALARTLYEDRPIV 150
Cdd:COG1124 81 VqmvfqdpyasLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488994816 151 LMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-200 |
8.92e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.68 E-value: 8.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgqpiqgrlaWMGQKDLLYPW 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL------------IDGKDIAKLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 87 LSVRDNVALgarlrgekvdrarvaalLEQvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR 166
Cdd:cd00267 69 EELRRRIGY-----------------VPQ-------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*
gi 488994816 167 IQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd00267 119 LLELLRELAEeGRTVIIVTHDPELAELAADRVIVL 153
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-202 |
1.16e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 143.75 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSL-HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI--------QG 72
Cdd:COG4988 333 GPPSIELEDVSFsYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI-NGVDLsdldpaswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 RLAWMGQKDLLYPWlSVRDNVALGARlrgeKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALAR 141
Cdd:COG4988 412 QIAWVPQNPYLFAG-TIRENLRLGRP----DASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 142 TLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPqEACRLSHRLLVLSA 202
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRL-ALLAQADRILVLDD 546
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-200 |
1.29e-39 |
|
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: 136.48 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLF----DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAWMgQKD 81
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF-DGKDLLKLSRRL-RKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 L--------------LYPWLSVRDNVALGARLRGEKVD----RARVAALLEQVELSS-CADARPATLSGGMRQRAALART 142
Cdd:cd03257 80 RrkeiqmvfqdpmssLNPRMTIGEQIAEPLRIHGKLSKkearKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-196 |
2.14e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 139.85 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIqgrlAWMGQKDL----------------LYPW 86
Cdd:COG4175 45 DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLI-DGEDI----TKLSKKELrelrrkkmsmvfqhfaLLPH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 87 LSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTR 164
Cdd:COG4175 120 RTVLENVAFGLEIQGVPKAerRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 488994816 165 TRIQ----TLAATLlaGRTVVLITHDPQEACRLSHR 196
Cdd:COG4175 200 REMQdellELQAKL--KKTIVFITHDLDEALRLGDR 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-190 |
2.88e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 134.92 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG-LAPA--TCGEVVAsDGQPIQG------RLA 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLL-NGRRLTAlpaeqrRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWLSVRDNVALG--ARLRGEKvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFAlpPTIGRAQ-RRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 154 EPFSALDTLTRTRIQTLAATLLAGRT--VVLITHDPQEA 190
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGipALLVTHDEEDA 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-207 |
8.89e-39 |
|
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: 133.92 E-value: 8.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV-----ASDGQPIQGRLAWMGQK 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DLLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSA 158
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 159 LDTL----TRTRIQTLAATLlaGRTVVLITHDPQEACRLSHRLLVLsaADGDI 207
Cdd:cd03301 161 LDAKlrvqMRAELKRLQQRL--GTTTIYVTHDQVEAMTMADRIAVM--NDGQI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-217 |
1.29e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.77 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAwmGQK 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML-DGQDITHVPA--ENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DL--------LYPWLSVRDNVALGarLRGEKVDRA----RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYeDRP 148
Cdd:PRK09452 87 HVntvfqsyaLFPHMTVFENVAFG--LRMQKTPAAeitpRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV-NKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 149 IVLM-DEPFSALDTLTRTRIQT----LAATLlaGRTVVLITHDPQEACRLSHRLLVLSaaDGDIDDShhlaGTP 217
Cdd:PRK09452 164 KVLLlDESLSALDYKLRKQMQNelkaLQRKL--GITFVFVTHDQEEALTMSDRIVVMR--DGRIEQD----GTP 229
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-207 |
2.57e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 135.22 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRL-FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG----RLAW-MG- 78
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILI-DGEDIRDldpvELRRrIGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 --QKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVEL--SSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:COG1125 81 viQQIGLFPHMTVAENIATVPRLLGwdKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 153 DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRelGKTIVFVTHDIDEALKLGDRIAVMR--EGRI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-205 |
2.82e-38 |
|
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: 132.62 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 24 LSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ------PIQGRLAWMGQKDLLYPWLSVRDNVALG- 96
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-NGVdvtaapPADRPVSMLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 97 -ARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLL 175
Cdd:cd03298 96 sPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 488994816 176 AGR--TVVLITHDPQEACRLSHRLLVLS----AADG 205
Cdd:cd03298 176 AETkmTVLMVTHQPEDAKRLAQRVVFLDngriAAQG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-201 |
3.91e-38 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 131.93 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVsLLGASGAGKTSLLRVMAGLAPAT------CGEVVASDGQPIQGRLAWMGQ 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSsgtiriDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488994816 158 ALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLN 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-157 |
5.16e-38 |
|
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: 129.69 E-value: 5.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 21 FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ--------GRLAWMGQKDLLYPWLSVRDN 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL-DGQDLTdderkslrKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 93 VALGARLRG--EKVDRARVAALLEQVELSSCAD----ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:pfam00005 80 LRLGLLLKGlsKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-202 |
1.87e-37 |
|
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: 130.76 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGE----VVASDGQPIQG--------- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegEVLLDGKDIYDldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 -RLAWMGQKDLLYPwLSVRDNVALGARLRGEKVDR---ARVAALLEQVELSSCADAR--PATLSGGMRQRAALARTLYED 146
Cdd:cd03260 81 rRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEeldERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 147 RPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLN 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-217 |
2.41e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 134.06 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPIQG------RLAWMGQ 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-GTDVSRlhardrKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARL--RGEKVDRA----RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlpRRERPNAAaikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 154 EPFSALDTLTRTR----IQTLAATLlaGRTVVLITHDPQEACRLSHRLLVLSaaDGDIDDshhlAGTP 217
Cdd:PRK10851 162 EPFGALDAQVRKElrrwLRQLHEEL--KFTSVFVTHDQEEAMEVADRVVVMS--QGNIEQ----AGTP 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-200 |
3.33e-37 |
|
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: 128.27 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDR--RLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLA 75
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDLRDldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPwLSVRDNValgarlrgekvdrarvaalleqvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 156 FSALDTLTRTRIQTLAATLLAGRTVVLITHDPqEACRLSHRLLVL 200
Cdd:cd03228 124 TSALDPETEALILEALRALAKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-201 |
1.48e-36 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 127.61 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ-------GRLAWMG 78
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW-QGEPIRrqrdeyhQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QKDLLYPWLSVRDNVALGARLRGEkVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSA 158
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRLHGP-GDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 159 LDT-----LTrtriQTLAATLLAGRTVVLITHdpQEACRLSHRLLVLS 201
Cdd:PRK13538 160 IDKqgvarLE----ALLAQHAEQGGMVILTTH--QDLPVASDKVRKLR 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-207 |
2.13e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.78 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMGQKDLlypw 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-DGKDLAS----LSPKEL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 87 lsvrdnvalgARLrgekvdRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR 166
Cdd:cd03214 72 ----------ARK------IAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488994816 167 IQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVLsaADGDI 207
Cdd:cd03214 136 LLELLRRLarERGKTVVMVLHDLNLAARYADRVILL--KDGRI 176
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-201 |
3.98e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.11 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ------PIQGRL 74
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVdlshvpPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPWLSVRDNVALGarLRGEKVDRA----RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIV 150
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFG--LKQDKLPKAeiasRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 151 LMDEPFSALDTLTRTRIQTLAATLL--AGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILerVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
4.66e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.54 E-value: 4.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLA-PAT-----CGEVVASDGQPIQGRL 74
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDAgsislCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGlsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 153 DEPFSALDTLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVlsaadgdIDDSHHLAGTPPRA 220
Cdd:PRK13537 163 DEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDRLCV-------IEEGRKIAEGAPHA 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-200 |
4.87e-36 |
|
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: 134.58 E-value: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR--LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLA 75
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGIDLRQidpaslrrQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPwLSVRDNVALGArlrgEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLY 144
Cdd:COG2274 553 VVLQDVFLFS-GTIRENITLGD----PDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPqEACRLSHRLLVL 200
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL-STIRLADRIIVL 682
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-201 |
8.64e-36 |
|
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: 126.81 E-value: 8.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ----GRLAwMGQKDLLYPWLSVRDNVALGA 97
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITepgpDRMV-VFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 98 ------RLRGEKvdRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLA 171
Cdd:TIGR01184 80 drvlpdLSKSER--RAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|..
gi 488994816 172 ATLL--AGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:TIGR01184 158 MQIWeeHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-200 |
1.06e-35 |
|
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: 126.68 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLfDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ------PIQGRLAWMGQ 79
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL-NGKditnlpPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGE--KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVdkKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 158 ALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03299 159 ALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-187 |
1.60e-35 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 125.37 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLA----WMGQKD 81
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 LLYPWLSVRDNVALGARLRGEkvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:PRK13539 83 AMKPALTVAENLEFWAAFLGG--EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 488994816 162 LTRTRIQTLAATLLA-GRTVVLITHDP 187
Cdd:PRK13539 161 AAVALFAELIRAHLAqGGIVIAATHIP 187
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-200 |
5.18e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.70 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSL-HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMGQKDLLY 84
Cdd:COG2884 2 IRFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV-NGQDLSR----LKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 ---------------PWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDR 147
Cdd:COG2884 77 lrrrigvvfqdfrllPDRTVYENVALPLRVTGksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488994816 148 PIVLMDEPFSALDTLTRTRIQTLAATL-LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-200 |
1.19e-33 |
|
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: 120.59 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG----RLAW----MG---QKDLLYPWLSVR 90
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV-NGQDVSDlrgrAIPYlrrkIGvvfQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVALGARLRGE--KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQ 168
Cdd:cd03292 97 ENVAFALEVTGVppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|...
gi 488994816 169 TLAATL-LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03292 177 NLLKKInKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-200 |
2.21e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 119.69 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ----GRLAWMGQKD 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDiaarNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 LLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEeaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 160 D----TLTRTRIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03269 160 DpvnvELLKDVIRELAR---AGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-207 |
3.43e-33 |
|
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: 119.17 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRL-------AWMG 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKLTDDKkninelrQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 ---QKDLLYPWLSVRDNVALGAR-LRGEKVDRARVAA--LLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:cd03262 80 mvfQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERAleLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 153 DEPFSALDTLTRTR----IQTLAATllaGRTVVLITHDPQEACRLSHRLLVLsaADGDI 207
Cdd:cd03262 160 DEPTSALDPELVGEvldvMKDLAEE---GMTMVVVTHEMGFAREVADRVIFM--DDGRI 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-207 |
5.63e-33 |
|
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: 118.81 E-value: 5.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 25 SFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQ-----PIQGRLAWMGQKDLLYPWLSVRDNVALGAR- 98
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtglaPYQRPVSMLFQENNLFAHLTVRQNIGLGLHp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 99 -LRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAG 177
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|..
gi 488994816 178 R--TVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:TIGR01277 178 RqrTLLMVTHHLSDARAIASQIAVVS--QGKI 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-190 |
7.08e-33 |
|
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: 124.88 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLH--VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ-------- 71
Cdd:COG4987 330 GGPSLELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL-GGVDLRdldeddlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 72 GRLAWMGQKdllyPWL---SVRDNVALGArlrgEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRA 137
Cdd:COG4987 409 RRIAVVPQR----PHLfdtTLRENLRLAR----PDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 138 ALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEA 190
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-209 |
9.38e-33 |
|
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: 118.69 E-value: 9.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG----RLAWMG--- 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF-DGEDITGlpphEIARLGigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 --QKDLLYPWLSVRDNVALGARLRG------------EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:cd03219 80 tfQIPRLFPELTVLENVMVAAQARTgsglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994816 145 EDRPIVLMDEPFSAldtLTRTRIQTLAATLLA----GRTVVLITHDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:cd03219 160 TDPKLLLLDEPAAG---LNPEETEELAELIRElrerGITVLLVEHDMDVVMSLADRVTVLDQgrviAEGTPDE 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-200 |
9.56e-33 |
|
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: 117.96 E-value: 9.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR-----LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgqpIQGRLAWMGQK 80
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS------VPGSIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 dllyPWL---SVRDNVALGARLRGEKVDRA-RVAALLEQVELSSCADA-----RPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:cd03250 75 ----PWIqngTIRENILFGKPFDEERYEKViKACALEPDLEILPDGDLteigeKGINLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 152 MDEPFSALDTLTRTRI--QTLAATLLAGRTVVLITHDPQeACRLSHRLLVL 200
Cdd:cd03250 151 LDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQ-LLPHADQIVVL 200
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-202 |
1.23e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.09 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQ-PIQGRLAWMG- 78
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvPARARLARARi 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 ----QKDLLYPWLSVRDNVALGARLRGEKVDR--ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:PRK13536 117 gvvpQFDNLDLEFTVRENLLVFGRYFGMSTREieAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 153 DEPFSALDTLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:PRK13536 197 DEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
1.41e-32 |
|
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: 123.86 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHV--GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATC---GEVVASDGQPIQGRLAWM 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQK---------DLLYPwLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYED 146
Cdd:COG1123 82 GRRigmvfqdpmTQLNP-VTVGDQIAEALENLGLSRAeaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 147 RPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDIDDShhlaGTPPRAPDAP 224
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIADRVVVMD--DGRIVED----GPPEEILAAP 234
|
...
gi 488994816 225 DLL 227
Cdd:COG1123 235 QAL 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-207 |
2.21e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 117.76 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNL----SFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ------PIQGRLAWMGQKDLLYPWLSV 89
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL-NGQdhtttpPSRRPVSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGAR--LRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI 167
Cdd:PRK10771 89 AQNIGLGLNpgLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488994816 168 QTLAATLLAGR--TVVLITHDPQEACRLSHRLLVLsaADGDI 207
Cdd:PRK10771 169 LTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVV--ADGRI 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-201 |
2.26e-32 |
|
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: 120.29 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 36 LLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAW------MGQKDLLYPWLSVRDNVALGARLRgeKVDRA-- 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIML-DGEDVTNVPPHlrhinmVFQSYALFPHMTVEENVAFGLKMR--KVPRAei 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 108 --RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLL--AGRTVVLI 183
Cdd:TIGR01187 78 kpRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeqLGITFVFV 157
|
170
....*....|....*...
gi 488994816 184 THDPQEACRLSHRLLVLS 201
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMR 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-207 |
2.68e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 123.35 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLH-VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ--------GRLA 75
Cdd:COG1132 339 EIEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-DGVDIRdltleslrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPwLSVRDNVALGArlrgEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLY 144
Cdd:COG1132 418 VVPQDTFLFS-GTIRENIRYGR----PDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS-----HRLLVLSaaDGDI 207
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLD--DGRI 552
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-200 |
3.17e-32 |
|
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: 117.08 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQKDLLYPWLSVRDNVAL 95
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdVVKEPAEARRRLGFVSDSTGLYDRLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 96 GARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL-TRTRIQTLAA 172
Cdd:cd03266 102 FAGLYGLKGDelTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMaTRALREFIRQ 181
|
170 180
....*....|....*....|....*...
gi 488994816 173 TLLAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03266 182 LRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-201 |
1.06e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVaSDGQPIQG--------RLAWM 77
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-LGDKPISMlssrqlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALG--------ARLRGEkvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPI 149
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspwlslwGRLSAE--DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 150 VLMDEPFSALDTLTRTRIQTLAATL-LAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-207 |
1.56e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 114.66 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVaSDGQPIQG----RLAWMGQKDLLYPWL--SV 89
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-LNGKPIKAkerrKSIGYVMQDVDYQLFtdSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGARLRGEkvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQT 169
Cdd:cd03226 90 REELLLGLKELDA--GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 170 LAATLLA-GRTVVLITHDPQEACRLSHRLLVLsaADGDI 207
Cdd:cd03226 168 LIRELAAqGKAVIVITHDYEFLAKVCDRVLLL--ANGAI 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-185 |
2.05e-31 |
|
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: 114.62 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV-----ASDGQPIQGRLAWMGQK 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DLLYPWLSVRDNVALGARLRGekVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLG--IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180
....*....|....*....|....*....
gi 488994816 161 TL----TRTRIQTLAATllaGRTVVLITH 185
Cdd:cd03268 159 PDgikeLRELILSLRDQ---GITVLISSH 184
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-187 |
2.20e-31 |
|
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: 120.47 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHVGDRR-LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------R 73
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV-NGVPLADadadswrdQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 LAWMGQKDLLYPWlSVRDNVALGARlrgeKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALART 142
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLARP----DASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDP 187
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL 517
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-201 |
2.96e-31 |
|
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: 114.39 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQ 79
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGEKVDRA--RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERreRIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 158 ALDTLTRT----RIQTLAATLlaGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:cd03265 161 GLDPQTRAhvweYIEKLKEEF--GMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-205 |
5.03e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEvVASDGQPIQG--------RLAWM 77
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE-VRLNGRPLADwspaelarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQK-DLLYPWlSVRDNVALGA--RLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTL------YEDRP 148
Cdd:PRK13548 82 PQHsSLSFPF-TVEEVVAMGRapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994816 149 IVLMDEPFSALDTLTRTRIQTLAATLL--AGRTVVLITHDPQEACRLSHRLLVLS----AADG 205
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDLNLAARYADRIVLLHqgrlVADG 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
4-209 |
7.71e-31 |
|
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: 116.74 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRgLSLHVGDRRLfdNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG----------- 72
Cdd:COG4148 1 MMLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-GGEVLQDsargiflpphr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 -RLAWMGQKDLLYPWLSVRDNVALGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:COG4148 77 rRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 152 MDEPFSALDTLTRTRI----QTLAATLlaGRTVVLITHDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:COG4148 157 MDEPLAALDLARKAEIlpylERLRDEL--DIPILYVSHSLDEVARLADHVVLLEQgrvvASGPLAE 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-202 |
8.30e-31 |
|
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: 113.82 E-value: 8.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLH-VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDG----------QPIQGRL 74
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPWLSVRDNV---ALGAR--LRG-----EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRstWRSlfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKD 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-209 |
1.57e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.44 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV-VasDGQPIQ----GRLAWM--- 77
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlW--DGEPLDpedrRRIGYLpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 -GqkdlLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDE 154
Cdd:COG4152 80 rG----LYPKMKVGEQLVYLARLKGlsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994816 155 PFSALD----TLTRTRIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:COG4152 156 PFSGLDpvnvELLKDVIRELAA---KGTTVIFSSHQMELVEELCDRIVIINKgrkvLSGSVDE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-202 |
1.68e-30 |
|
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: 113.06 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLS----LHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMGQKD 81
Cdd:cd03258 2 IELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDLTL----LSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 L---------------LYPWLSVRDNVALGARLRG-EKVDR-ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:cd03258 77 LrkarrrigmifqhfnLLSSRTVFENVALPLEIAGvPKAEIeERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-207 |
4.14e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ-----PIQGRLAWM-GQ 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEdvthrSIQQRDICMvFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488994816 158 ALD-TLTRT---RIQTLAATLlaGRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:PRK11432 166 NLDaNLRRSmreKIRELQQQF--NITSLYVTHDQSEAFAVSDTVIVMN--KGKI 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-217 |
1.40e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.98 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQPIQG--------RLAWM 77
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV-RLNGRPLAAwspwelarRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQK-DLLYPWlSVRDNVALG--ARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTL-------YEDR 147
Cdd:COG4559 81 PQHsSLAFPF-TVEEVVALGraPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 148 PIVLMDEPFSALDTLTRTRIQTLAATLL-AGRTVVLITHDPQEACRLSHRLLVLsaADGDIddshHLAGTP 217
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLArRGGGVVAVLHDLNLAAQYADRILLL--HQGRL----VAQGTP 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-200 |
1.84e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 108.46 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR--LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQgrlawmgqkdll 83
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADIS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 yPWlsvrdnvalgarlrGEKVDRARVAALLEQVEL--SSCADArpaTLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:cd03246 68 -QW--------------DPNELGDHVGYLPQDDELfsGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 162 LTRTRI-QTLAATLLAGRTVVLITHDPqEACRLSHRLLVL 200
Cdd:cd03246 130 EGERALnQAIAALKAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-230 |
2.52e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.01 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI-----------QGRL 74
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-DGENIpamsrsrlytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPWLSVRDNVALGARLRG---EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTqlpAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEacrlshrllVLSAADGD--IDDSHHLA-GTPPRAPDAPDL 226
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPE---------VLSIADHAyiVADKKIVAhGSAQALQANPDP 237
|
....
gi 488994816 227 LIGQ 230
Cdd:PRK11831 238 RVRQ 241
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
17-200 |
8.12e-29 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 108.21 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI----QGRLAWMGQKDL--------LY 84
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLF-NGQSLsklsSNERAKLRNKKLgfiyqfhhLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 PWLSVRDNVALGARLRGEKVDRA--RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL 162
Cdd:TIGR02211 96 PDFTALENVAMPLLIGKKSVKEAkeRAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 163 TRTRIQTLAATL--LAGRTVVLITHDPQEACRLShRLLVL 200
Cdd:TIGR02211 176 NAKIIFDLMLELnrELNTSFLVVTHDLELAKKLD-RVLEM 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-218 |
1.30e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG---------RLAW 76
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-DGLKVNDpkvderlirQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 M-GQKDLLYPWLSVRDNVALGA-RLRGEKVDRARVAA--LLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:PRK09493 81 MvFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQAreLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 153 DEPFSALDTLTR----TRIQTLAATllaGRTVVLITHDPQEACRLSHRLLVLS----AADGDIDDshhLAGTPP 218
Cdd:PRK09493 161 DEPTSALDPELRhevlKVMQDLAEE---GMTMVIVTHEIGFAEKVASRLIFIDkgriAEDGDPQV---LIKNPP 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-187 |
1.37e-28 |
|
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: 107.06 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGR------LAWMGQ 79
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephenILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGEkvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGG--AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 488994816 160 DTLTRTRIQTL-AATLLAGRTVVLITHDP 187
Cdd:TIGR01189 159 DKAGVALLAGLlRAHLARGGIVLLTTHQD 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-196 |
1.41e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRV---MAGLAP--ATCGEVVAsDGQPIQG---- 72
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPgaRVEGEILL-DGEDIYDpdvd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 ------RLAWMGQKDLLYPwLSVRDNVALGARLRG--------EKVDRA-RVAALLEQVE--LSscadaRPAT-LSGGMR 134
Cdd:COG1117 87 vvelrrRVGMVFQKPNPFP-KSIYDNVAYGLRLHGikskseldEIVEESlRKAALWDEVKdrLK-----KSALgLSGGQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 135 QRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHR 196
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDY 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-201 |
2.21e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 109.02 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 14 HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQKDLLYPWL 87
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTArvagydVVREPRKVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRT 165
Cdd:TIGR01188 82 TGRENLEMMGRLYGlpKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 488994816 166 RIQTLAATLL-AGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:TIGR01188 162 AIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIID 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-205 |
2.28e-28 |
|
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: 106.91 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD--RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ--------GRLA 75
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRqldpadlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKdllyPWL---SVRDNVALGARLrgekVDRARVaalLEQVELSSCAD--------------ARPATLSGGMRQRAA 138
Cdd:cd03245 82 YVPQD----VTLfygTLRDNITLGAPL----ADDERI---LRAAELAGVTDfvnkhpngldlqigERGRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 139 LARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQeACRLSHRLLVLSA----ADG 205
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS-LLDLVDRIIVMDSgrivADG 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-202 |
4.03e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 109.73 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV-----ASDGQPIQGRLAWMGQ 79
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRG-EKVDRA-RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGaKKEEINqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 158 ALDTLTRT--RIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:PRK11000 163 NLDAALRVqmRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-187 |
4.07e-28 |
|
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: 106.04 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQ 79
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGekvdRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS----DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*....
gi 488994816 160 DTLTRTRIQT-LAATLLAGRTVVLITHDP 187
Cdd:cd03231 157 DKAGVARFAEaMAGHCARGGMVVLTTHQD 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-198 |
8.68e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGqpiqGRLAWMGQKDLLyPW---LSVRDN 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----ARVAYVPQRSEV-PDslpLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 93 VALGA--------RLRGEkvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTR 164
Cdd:NF040873 78 VAMGRwarrglwrRLTRD--DRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*
gi 488994816 165 TRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLL 198
Cdd:NF040873 156 ERIIALLAEEHArGATVVVVTHDLELVRRADPCVL 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-186 |
1.01e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWM 77
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-DGLDVATtpsrelakRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALG------ARLRGEkvDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpyskGRLTAE--DREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488994816 152 MDEPFSALD---------TLTRtriqtLAATLlaGRTVVLITHD 186
Cdd:COG4604 159 LDEPLNNLDmkhsvqmmkLLRR-----LADEL--GKTVVIVLHD 195
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-209 |
1.43e-27 |
|
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: 107.89 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 24 LSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV------ASDGQPI-----QGRLAWMGQKDLLYPWLSVRDN 92
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 93 VALGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI----Q 168
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIlpylE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 169 TLAATLlaGRTVVLITHDPQEACRLSHRLLVLS----AADGDIDD 209
Cdd:TIGR02142 176 RLHAEF--GIPILYVSHSLQEVLRLADRVVVLEdgrvAAAGPIAE 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-200 |
1.79e-27 |
|
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: 104.82 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGR---------LAW 76
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDITGLppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPWLSVRDNVALGARLRGEKVDRARVAALLEQV-ELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 156 FSAL-----DTLTRTrIQTLAATllaGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03224 160 SEGLapkivEEIFEA-IRELRDE---GVTILLVEQNARFALEIADRAYVL 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-186 |
2.37e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 8 VRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQpiqgRLAWMGQKDLLYPWL 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL----RIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALGARLRGEKVDR----------------------------------ARVAALLEQVELSSC-ADARPATLSGG 132
Cdd:COG0488 77 TVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggweaeARAEEILSGLGFPEEdLDRPVSELSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 133 MRQRAALARTLYEDRPIVLMDEPFSALDtltrtrIQTLA--ATLLAGR--TVVLITHD 186
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD------LESIEwlEEFLKNYpgTVLVVSHD 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-187 |
4.19e-27 |
|
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: 108.60 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSL-HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV-------ASDGQPIQGR 73
Cdd:TIGR02868 331 GKPTLELRDLSAgYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvsSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 LAWMGQKDLLYPwLSVRDNVALGArlrgEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALART 142
Cdd:TIGR02868 411 VSVCAQDAHLFD-TTVRENLRLAR----PDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDP 187
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-200 |
6.77e-27 |
|
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: 103.38 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 15 VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgqpIQGRLAWM-----GqkdlLYPWLSV 89
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT------VRGRVSSLlglggG----FNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGARLRGekVDRARVAALLEQV----ELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRT 165
Cdd:cd03220 102 RENIYLNGRLLG--LSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 488994816 166 R-IQTLAATLLAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03220 180 KcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-197 |
1.13e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.93 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR----LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPI-----QGRLA- 75
Cdd:PRK10584 7 VEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLhqmdeEARAKl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 ------WMGQKDLLYPWLSVRDNVALGARLRGE--KVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTlYEDR 147
Cdd:PRK10584 86 rakhvgFVFQSFMLIPTLNALENVELPALLRGEssRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA-FNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 148 PIVLM-DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRL 197
Cdd:PRK10584 165 PDVLFaDEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRL 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-202 |
2.17e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLH--VGDRRL--FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQpiqgRLAWMGQKD 81
Cdd:PRK11153 2 IELKNISKVfpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV-DGQ----DLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 LL------------YPWLSVR---DNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:PRK11153 77 LRkarrqigmifqhFNLLSSRtvfDNVALPLELAGTPKAeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 145 EDRPIVLMDEPFSALDTLTrTRiQTLAatLLA------GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:PRK11153 157 SNPKVLLCDEATSALDPAT-TR-SILE--LLKdinrelGLTIVLITHEMDVVKRICDRVAVIDA 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-186 |
2.47e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.39 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLH----VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawMGQKD 81
Cdd:COG1135 2 IELENLSKTfptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV-DGVDLTA----LSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 82 L---------------LYPWLSVRDNVALGarLRGEKVDRA----RVAALLEQVELSSCADARPATLSGGMRQRAALART 142
Cdd:COG1135 77 LraarrkigmifqhfnLLSSRTVAENVALP--LEIAGVPKAeirkRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTrTRiQTLAatLLA------GRTVVLITHD 186
Cdd:COG1135 155 LANNPKVLLCDEATSALDPET-TR-SILD--LLKdinrelGLTIVLITHE 200
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-194 |
2.89e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.30 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGL-----APATCGEVVAsDGQPI--------QG 72
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYL-DGQDIfkmdvielRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 RLAWMGQKDLLYPWLSVRDNVALGARL----RGEKVDRARVAALLEQVEL----SSCADARPATLSGGMRQRAALARTLY 144
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLS 194
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIS 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-200 |
6.59e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.96 E-value: 6.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRrlfdnlSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI------------QGR 73
Cdd:PRK10070 35 LEKTGLSLGVKDA------SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIakisdaelrevrRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 LAWMGQKDLLYPWLSVRDNVALGARLRGEKVDRARVAAL--LEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLAG--RTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-209 |
1.05e-25 |
|
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: 100.54 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTV-PGGQWVsLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQP--------IQGRLAW 76
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVkPGEHWA-ILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERrggedvweLRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 ----MGQKdlLYPWLSVRDNVA------LGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYED 146
Cdd:COG1119 83 vspaLQLR--FPRDETVLDVVLsgffdsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 147 RPIVLMDEPFSALDTLTR----TRIQTLAATllAGRTVVLITHDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:COG1119 161 PELLILDEPTAGLDLGARelllALLDKLAAE--GAPTLVLVTHHVEEIPPGITHVLLLKDgrvvAAGPKEE 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-201 |
1.26e-25 |
|
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: 99.16 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLA--PATCGEvVASDGQP-----IQGRLAWMGQKDLLYPWLS 88
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGE-VLINGRPldkrsFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGARLRGekvdrarvaalleqvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLT-RTRI 167
Cdd:cd03213 99 VRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSaLQVM 151
|
170 180 190
....*....|....*....|....*....|....*
gi 488994816 168 QTLAATLLAGRTVVLITHDP-QEACRLSHRLLVLS 201
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLS 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-212 |
4.18e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.23 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLAWMGQ- 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 -----------------KDLLYPWLSVRDNV-----ALGARLRGEKvdRARVAALLEQVEL-SSCADARPATLSGGMRQR 136
Cdd:PRK11701 82 errrllrtewgfvhqhpRDGLRMQVSAGGNIgerlmAVGARHYGDI--RATAGDWLERVEIdAARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 137 AALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSAA--------DGD 206
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLLAHRLLVMKQGrvvesgltDQV 239
|
....*.
gi 488994816 207 IDDSHH 212
Cdd:PRK11701 240 LDDPQH 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-209 |
4.25e-25 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 98.77 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ-----PIQGR----LAW 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-DGQditklPMHKRarlgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPWLSVRDNvaLGARLRGEKVDRA----RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:cd03218 80 LPQEASIFRKLTVEEN--ILAVLEIRGLSKKereeKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 153 DEPFSALDTLTRTRIQTLAATLLAGRTVVLIT-HDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEgkvlAEGTPEE 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-200 |
4.63e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.07 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 24 LSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV-----VASDGQPIQGRLAWMGQKDLLYPWLSVRDNVALGAR 98
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNELEPADRDIAMVFQNYALYPHMSVRENMAYGLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 99 LRG-EKVD-RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR----IQTLAA 172
Cdd:PRK11650 103 IRGmPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQmrleIQRLHR 182
|
170 180
....*....|....*....|....*...
gi 488994816 173 TLlaGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK11650 183 RL--KTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-201 |
6.35e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.11 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAP---ATCGEVVAsDGQPI-----QGRLAWMGQKDLLYPWLS 88
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILF-NGQPRkpdqfQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGARLR-GEKVDRARVAALLEQVELSSCADARPA-----TLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL 162
Cdd:cd03234 98 VRETLTYTAILRlPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488994816 163 TRTR-IQTLAATLLAGRTVVLITHDPQ-EACRLSHRLLVLS 201
Cdd:cd03234 178 TALNlVSTLSQLARRNRIVILTIHQPRsDLFRLFDRILLLS 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-201 |
7.17e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 102.43 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLAPA--TCGEVVASDGQPI-----QGRLAWMGQKDLLYPWLSVRDNVALGARLR--- 100
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGMPIdakemRAISAYVQQDDLFIPTLTVREHLMFQAHLRmpr 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 101 --GEKVDRARVAALLEQVELSSCADARPAT------LSGGMRQRAALARTLYEDRPIVLMDEPFSALD-TLTRTRIQTLA 171
Cdd:TIGR00955 131 rvTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsFMAYSVVQVLK 210
|
170 180 190
....*....|....*....|....*....|.
gi 488994816 172 ATLLAGRTVVLITHDPQ-EACRLSHRLLVLS 201
Cdd:TIGR00955 211 GLAQKGKTIICTIHQPSsELFELFDKIILMA 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-194 |
9.44e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.70 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRV---MAGLAPATCGE---------VVASDGQPIQ-- 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEgkvtfhgknLYAPDVDPVEvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 72 GRLAWMGQKDLLYPwLSVRDNVALGARLRG------EKVDRA-RVAALLEQVE--LSSCADArpatLSGGMRQRAALART 142
Cdd:PRK14243 91 RRIGMVFQKPNPFP-KSIYDNIAYGARINGykgdmdELVERSlRQAALWDEVKdkLKQSGLS----LSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLS 194
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVS 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-200 |
1.55e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGE-------------VVASDGQPIQ 71
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdfsqkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 72 GRLAWMGQKDLLYPWLSVRDN-VALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP 148
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 149 IVLMDEPFSALDTLTRTR----IQTLAATllaGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG4161 162 VLLFDEPTAALDPEITAQvveiIRELSQT---GITQVIVTHEVEFARKVASQVVYM 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-227 |
3.74e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RL 74
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEAlsaraasrRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPWLSVRDNVALG-----ARL-RGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP 148
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGrtphrSRFdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 149 IVLMDEPFSALDTLTRTRIQTLAATLL-AGRTVVLITHDPQEACRLSHRLLVLsaADGDIDDShhlagTPPRAPDAPDLL 227
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVdDGKTAVAAIHDLDLAARYCDELVLL--ADGRVRAA-----GPPADVLTADTL 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-194 |
4.87e-24 |
|
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: 100.18 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVG--DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ--------GRLA 75
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL-DGHDLAdytlaslrRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPwLSVRDNVALGarlRGEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLY 144
Cdd:TIGR02203 410 LVSQDVVLFN-DTIANNIAYG---RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH------RLS 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-194 |
1.14e-23 |
|
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: 94.99 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWMGQKDLLYPwLS 88
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREvtldslrrAIGVVPQDTVLFN-DT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGaRLRG--EKVDRARVAALLEQVELS------SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:cd03253 91 IGYNIRYG-RPDAtdEEVIEAAKAAQIHDKIMRfpdgydTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190
....*....|....*....|....*....|....
gi 488994816 161 TLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:cd03253 170 THTEREIQAALRDVSKGRTTIVIAH------RLS 197
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-205 |
1.19e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.73 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLHVGD-RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgQPIQGRLAWMGQK 80
Cdd:COG4178 359 EDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA----RPAGARVLFLPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 dlLY-PWLSVRDNVALGArlRGEKVDRARVAALLEQVELSSCAD------ARPATLSGGMRQRAALARTLYEdRP-IVLM 152
Cdd:COG4178 435 --PYlPLGTLREALLYPA--TAEAFSDAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLLLH-KPdWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 153 DEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPqEACRLSHRLLVLSAADG 205
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHRS-TLAAFHDRVLELTGDGS 561
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-209 |
1.71e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 8 VRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgqpIQGRLAWM-----Gqkdl 82
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE------VNGRVSALlelgaG---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 LYPWLSVRDNVALGARLRGekVDRARVAALLEQV----ELSSCADaRPA-TLSGGMRQR-A-ALARTLYEDrpIVLMDEP 155
Cdd:COG1134 99 FHPELTGRENIYLNGRLLG--LSRKEIDEKFDEIvefaELGDFID-QPVkTYSSGMRARlAfAVATAVDPD--ILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 156 FSALDTLTR----TRIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVLS----AADGDIDD 209
Cdd:COG1134 174 LAVGDAAFQkkclARIRELRE---SGRTVIFVSHSMGAVRRLCDRAIWLEkgrlVMDGDPEE 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-200 |
2.74e-23 |
|
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: 92.11 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRlawmgqkdllyp 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEVSFA------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 wlSVRDNVALGArlrgekvdrarvaALLEQvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRT 165
Cdd:cd03216 68 --SPRDARRAGI-------------AMVYQ-------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 166 R----IQTLAAtllAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:cd03216 120 RlfkvIRRLRA---QGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-201 |
7.50e-23 |
|
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: 97.01 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLS--LHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLA 75
Cdd:TIGR01257 927 PGVCVKNLVkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdIETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWLSVRDNVALGARLRGEKVDRARVA--ALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 154 EPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-201 |
1.09e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.40 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLAW-------MGQKDLLYPWLSVRDNVA 94
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlrrigvvFGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 95 LGARLRGEKVDRA--RVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAA 172
Cdd:cd03267 118 LLAAIYDLPPARFkkRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLK 197
|
170 180 190
....*....|....*....|....*....|.
gi 488994816 173 TLLAGR--TVVLITHDPQEACRLSHRLLVLS 201
Cdd:cd03267 198 EYNRERgtTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-207 |
1.13e-22 |
|
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: 92.29 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWMGQKDLLYPWlSVRDNV 93
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDytlaslrrQIGLVSQDVFLFND-TVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 ALGAR--LRGEKVDRARVAALLEQVE-----LSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR 166
Cdd:cd03251 97 AYGRPgaTREEVEEAARAANAHEFIMelpegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488994816 167 IQTLAATLLAGRTVVLITHdpqeacRLS-----HRLLVLSaaDGDI 207
Cdd:cd03251 177 VQAALERLMKNRTTFVIAH------RLStienaDRIVVLE--DGKI 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-196 |
1.40e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRV---MAGLAP--ATCGEVV---------ASD 66
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPevTITGSIVynghniyspRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 67 GQPIQGRLAWMGQKDLLYPwLSVRDNVALGARLRGEKvDRARVAALLEQV--------ELSSCADARPATLSGGMRQRAA 138
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIK-DKQVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 139 LARTLYEDRPIVLMDEPFSALDTLTRTRIQtlaATLLAGR---TVVLITHDPQEACRLSHR 196
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIE---ETLLGLKddyTMLLVTRSMQQASRISDR 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-217 |
1.41e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGD--RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGeVVASDGQPIQGRLAWMG 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG-TITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QK---------DLLYPWLSVRDNVALGARLRG----EKVDRARVAalLEQVELSSCADARPATLSGGMRQRAALARTLYE 145
Cdd:PRK13635 80 RRqvgmvfqnpDNQFVGATVQDDVAFGLENIGvpreEMVERVDQA--LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 146 DRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRlSHRLLVLSaaDGDIDDShhlaGTP 217
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQ-ADRVIVMN--KGEILEE----GTP 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-187 |
1.72e-22 |
|
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: 91.73 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPgIEVRGLS----LH-VGDRRL--FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV-VASDGQPIQg 72
Cdd:COG4778 1 MTTL-LEVENLSktftLHlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDGGWVD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 rLAWMGQKDLLY----------------PWLSVRDNVALGARLRGEKVD--RARVAALLEQVEL-SSCADARPATLSGGM 133
Cdd:COG4778 79 -LAQASPREILAlrrrtigyvsqflrviPRVSALDVVAEPLLERGVDREeaRARARELLARLNLpERLWDLPPATFSGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 134 RQRAALARTLYEDRPIVLMDEPFSALDTLTRTR-IQTLAATLLAGRTVVLITHDP 187
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVvVELIEEAKARGTAIIGIFHDE 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-215 |
3.42e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPIQG------------RLAWMGQKDLLYPWLSVR 90
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN-GQPMSKlssaakaelrnqKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVAL----GARLRGEKVDRARvaALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR 166
Cdd:PRK11629 106 ENVAMplliGKKKPAEINSRAL--EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 167 IQTLAATL--LAGRTVVLITHDPQEACRLSHRllvLSAADGDIDDSHHLAG 215
Cdd:PRK11629 184 IFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQ---LEMRDGRLTAELSLMG 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-194 |
4.25e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.44 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGL-----APATCGEV-------VASDGQPIQGR 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVrlfgrniYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 --LAWMGQKDLLYPWLSVRDNVALGARLRG---------EKVDRA-RVAALLEQVElsSCADARPATLSGGMRQRAALAR 141
Cdd:PRK14267 85 reVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvkskkeldERVEWAlKKAALWDEVK--DRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 142 TLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLS 194
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVS 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-200 |
4.66e-22 |
|
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: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRlawmGQK 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DGKPVRIR----SPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 D-------------LLYPWLSVRDNVALGA-RLRGEKVD----RARVAALLEQVELSSCADARPATLSGGMRQRAALART 142
Cdd:COG3845 76 DaialgigmvhqhfMLVPNLTVAENIVLGLePTKGGRLDrkaaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994816 143 LYEDRPIVLMDEPFSAL-----DTLTRTrIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG3845 156 LYRGARILILDEPTAVLtpqeaDELFEI-LRRLAA---EGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-200 |
4.72e-22 |
|
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: 94.04 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHV--GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQgrlAWMgqKDLL 83
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-DGADLS---QWD--REEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 YPWL------------SVRDNVAlgarlRGEKVDRARV--AALLEQV-------------ELsscaDARPATLSGGMRQR 136
Cdd:COG4618 405 GRHIgylpqdvelfdgTIAENIA-----RFGDADPEKVvaAAKLAGVhemilrlpdgydtRI----GEGGARLSGGQRQR 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 137 AALARTLYEDRPIVLMDEPFSALDT-----LTRTrIQTLAAtllAGRTVVLITHDPQeACRLSHRLLVL 200
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDegeaaLAAA-IRALKA---RGATVVVITHRPS-LLAAVDKLLVL 539
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-185 |
1.08e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLS-LHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATcG-------EVVASDGQPIQGRLAWM 77
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GslkingiELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLyPWLSVRDNVALGArlrgEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLYED 146
Cdd:PRK11174 429 GQNPQL-PHGTLRDNVLLGN----PDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQP 503
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 147 RPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITH 185
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTH 542
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-200 |
1.35e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.47 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI--------QGRLAWMGQKDLLYPwLSVRDNV 93
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLaladpawlRRQVGVVLQENVLFN-RSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 ALG--ARLRGEKVDRARVAALLEQV-ELSSCADA----RPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR 166
Cdd:cd03252 97 ALAdpGMSMERVIEAAKLAGAHDFIsELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHA 176
|
170 180 190
....*....|....*....|....*....|....
gi 488994816 167 IQTLAATLLAGRTVVLITHDpQEACRLSHRLLVL 200
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHR-LSTVKNADRIIVM 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-185 |
1.59e-21 |
|
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: 87.75 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 21 FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQKDLLYPwLSVRDNva 94
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpVSDLEKALSSLISVLNQRPYLFD-TTLRNN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 95 LGARLrgekvdrarvaalleqvelsscadarpatlSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATL 174
Cdd:cd03247 95 LGRRF------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV 144
|
170
....*....|.
gi 488994816 175 LAGRTVVLITH 185
Cdd:cd03247 145 LKDKTLIWITH 155
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-186 |
1.84e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR-LFDnLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV--------VASDGQPIQGRL-- 74
Cdd:PRK11124 3 IQLNGINCFYGAHQaLFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 ---AWMGQKDLLYPWLSVRDN-VALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP 148
Cdd:PRK11124 82 rnvGMVFQQYNLWPHLTVQQNlIEAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488994816 149 IVLMDEPFSALDTLTRTR----IQTLAATllaGRTVVLITHD 186
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQivsiIRELAET---GITQVIVTHE 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-201 |
2.16e-21 |
|
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: 87.49 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHvgdrRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRlawmgqkdl 82
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-DGKPVTRR--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 lypwlSVRDNVALGARLRGEkvDRARVAALLEQvelsSCAD--ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:cd03215 68 -----SPRDAIRAGIAYVPE--DRKREGLVLDL----SVAEniALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488994816 161 TLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:cd03215 137 VGAKAEIyRLIRELADAGKAVLLISSELDELLGLCDRILVMY 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-194 |
2.32e-21 |
|
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: 88.82 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWMGQKDLLYPWlSVRDNV 93
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-DGIDIRDisrkslrsMIGVVLQDTFLFSG-TIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 ALGarlrGEKVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL 162
Cdd:cd03254 98 RLG----RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190
....*....|....*....|....*....|..
gi 488994816 163 TRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:cd03254 174 TEKLIQEALEKLMKGRTSIIIAH------RLS 199
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-200 |
2.48e-21 |
|
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: 90.50 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLH--VGDRRLF--DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATC---GEVVAsDGQPIQGrlawMG 78
Cdd:COG0444 2 LEVRNLKVYfpTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILF-DGEDLLK----LS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QKDL------------------LYPWLSVRDNVALGARLRG---EKVDRARVAALLEQVELS---SCADARPATLSGGMR 134
Cdd:COG0444 77 EKELrkirgreiqmifqdpmtsLNPVMTVGDQIAEPLRIHGglsKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 135 QRAALARTLYEDRPIVLMDEPFSALDTLTRTRI----QTLAATLlaGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQIlnllKDLQREL--GLAILFITHDLGVVAEIADRVAVM 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-217 |
3.10e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ-----PIQGRlAWMG 78
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-DGEdithlPMHKR-ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 -----------QKdllypwLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYE 145
Cdd:COG1137 80 igylpqeasifRK------LTVEDNILAVLELRKlsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 146 DRPIVLMDEPFSALDTLTRTRIQTLAATlLAGRTV-VLIT-HDPQEACRLSHRLLVLSaaDGDIddshhLA-GTP 217
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRH-LKERGIgVLITdHNVRETLGICDRAYIIS--EGKV-----LAeGTP 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-200 |
3.17e-21 |
|
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: 88.30 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ--------GRLAWMGQKDLLYPwLS 88
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-DGKPISqyehkylhSKVSLVGQEPVLFA-RS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALG-ARLRGEKVDRARVAA-------LLEQvELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:cd03248 104 LQDNIAYGlQSCSFECVKEAAQKAhahsfisELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 161 TLTRTRIQTLAATLLAGRTVVLITHDPQEACRlSHRLLVL 200
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVL 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-209 |
3.76e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 87.98 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 26 FTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGR--LAWMGQKDLL---YPwLSVRDNVA------ 94
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWrhIGYVPQRHEFawdFP-ISVAHTVMsgrtgh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 95 LGARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATL 174
Cdd:TIGR03771 80 IGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 175 L-AGRTVVLITHDPQEACRLSHRLLVLSA---ADGDIDD 209
Cdd:TIGR03771 160 AgAGTAILMTTHDLAQAMATCDRVVLLNGrviADGTPQQ 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-217 |
4.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD--RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG-LAPATCGE-VVASDGQPIQGRLAW----- 76
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNsKITVDGITLTAKTVWdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 ----MGQKDLLYPWLSVRDNVALGARLRGekVDRAR----VAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP 148
Cdd:PRK13640 86 vgivFQNPDNQFVGATVGDDVAFGLENRA--VPRPEmikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 149 IVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEAcRLSHRLLVLSaaDGDIDDShhlaGTP 217
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEA-NMADQVLVLD--DGKLLAQ----GSP 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-186 |
5.33e-21 |
|
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: 85.58 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGlapatcgevvasDGQPIQGRLAWMGQKDLLYp 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG------------ELEPDEGIVTWGSTVKIGY- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 wlsvrdnvalgarlrgekvdrarvaalLEQvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTrt 165
Cdd:cd03221 68 ---------------------------FEQ-------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES-- 105
|
170 180
....*....|....*....|..
gi 488994816 166 rIQTLAATLLA-GRTVVLITHD 186
Cdd:cd03221 106 -IEALEEALKEyPGTVILVSHD 126
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-195 |
1.53e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.18 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDG--------QPIQGRLAWM 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQ---KDlLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADaRPA-TLSGGMRQRAALARTLYEDRPIVL 151
Cdd:NF033858 82 PQglgKN-LYPTLSVFENLDFFGRLFGQDAAerRRRIDELLRATGLAPFAD-RPAgKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLAGR---TVVLITHDPQEACRLSH 195
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERFDW 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-184 |
1.65e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.18 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG-LAPATCGEVVasdgqpIQGRLAWMGQkdllYPWL---SVRD 91
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVV------IRGTVAYVPQ----VSWIfnaTVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 92 NVALGARLRGEKVDRA-RVAALLEQVELSSCAD-----ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT-LTR 164
Cdd:PLN03130 698 NILFGSPFDPERYERAiDVTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGR 777
|
170 180
....*....|....*....|
gi 488994816 165 TRIQTLAATLLAGRTVVLIT 184
Cdd:PLN03130 778 QVFDKCIKDELRGKTRVLVT 797
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-186 |
2.13e-20 |
|
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: 89.48 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHV-----GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV---VASD-------GQ 68
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEwvdmtkpGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 69 PIQGRLA-WMG---QKDLLYPWLSVRDNV--ALGARLRGEKVDRARVAAL----LEQVELSSCADARPATLSGGMRQRAA 138
Cdd:TIGR03269 358 DGRGRAKrYIGilhQEYDLYPHRTVLDNLteAIGLELPDELARMKAVITLkmvgFDEEKAEEILDKYPDELSEGERHRVA 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 139 LARTLYEDRPIVLMDEPFSALDTLTRTRI--QTLAATLLAGRTVVLITHD 186
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVthSILKAREEMEQTFIIVSHD 487
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-194 |
2.40e-20 |
|
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: 86.05 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDR---RLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ--------GRL 74
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL-DGVDIRdlnlrwlrSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPwLSVRDNVALGARLRG-EKVDRA-RVAALLEQVE-----LSSCADARPATLSGGMRQRAALARTLYEDR 147
Cdd:cd03249 80 GLVSQEPVLFD-GTIAENIRYGKPDATdEEVEEAaKKANIHDFIMslpdgYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 148 PIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH------RLS 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-209 |
2.99e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQpiqgRLAWMGQK-DLLY 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV----KIGYFDQHqEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 PWLSVRDNVALGARLRGEKVDRARVAALL---EQVelsscaDARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDt 161
Cdd:COG0488 392 PDKTVLDELRDGAPGGTEQEVRGYLGRFLfsgDDA------FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD- 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 162 ltrtrIQTLAATLLA-----GrTVVLITHDPQEACRLSHRLLVLsaADGDIDD 209
Cdd:COG0488 465 -----IETLEALEEAlddfpG-TVLLVSHDRYFLDRVATRILEF--EDGGVRE 509
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-187 |
3.56e-20 |
|
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: 84.13 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD-RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvasdGQPIQGRLAWMGQK---- 80
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGEDLLFLPQRpylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 ------DLLYPWLSVrdnvalgarlrgekvdrarvaalleqvelsscadarpatLSGGMRQRAALARTLYEdRP-IVLMD 153
Cdd:cd03223 77 lgtlreQLIYPWDDV---------------------------------------LSGGEQQRLAFARLLLH-KPkFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 488994816 154 EPFSALDTLTRTRIQTLAATLLAgrTVVLITHDP 187
Cdd:cd03223 117 EATSALDEESEDRLYQLLKELGI--TVISVGHRP 148
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-210 |
3.57e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVG---DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAW-MGQK- 80
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-DGDLLTEENVWdIRHKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 -------DLLYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:PRK13650 84 gmvfqnpDNQFVGATVEDDVAFGLENKGIPHEemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 152 MDEPFSALDTLTRTR-IQTLAATLLA-GRTVVLITHDPQEACrLSHRLLVLSaaDGDIDDS 210
Cdd:PRK13650 164 LDEATSMLDPEGRLElIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMK--NGQVEST 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-212 |
3.59e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 86.04 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV--VASDGQPIQ--------- 71
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyIMRSGAELElyqlseaer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 72 ---GRLAW----MGQKDLLYPWLSVRDNV-----ALGARLRGEKvdRARVAALLEQVELSSC-ADARPATLSGGMRQRAA 138
Cdd:TIGR02323 81 rrlMRTEWgfvhQNPRDGLRMRVSAGANIgerlmAIGARHYGNI--RATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 139 LARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLL--AGRTVVLITHDPQEACRLSHRLLVLSAA--------DGDID 208
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVrdLGLAVIIVTHDLGVARLLAQRLLVMQQGrvvesgltDQVLD 238
|
....
gi 488994816 209 DSHH 212
Cdd:TIGR02323 239 DPQH 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-196 |
6.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASD----GQPI-------- 70
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllgGRSIfnyrdvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 71 -QGRLAWMGQKDLLYPwLSVRDNVALGAR---LRGEKVDRARVAALLEQVELSSCADAR----PATLSGGMRQRAALART 142
Cdd:PRK14271 99 fRRRVGMLFQRPNPFP-MSIMDNVLAGVRahkLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLART 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHR 196
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDR 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-187 |
7.64e-20 |
|
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: 87.79 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGeVVASDGQPIQ-------GR-LAWMGQKDLLYPWl 87
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSG-SVRLDGADLKqwdretfGKhIGYLPQDVELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVA-LGARLRGEKVDRARVAALLEQVELS------SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:TIGR01842 407 TVAENIArFGENADPEKIIEAAKLAGVHELILRlpdgydTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190
....*....|....*....|....*....|.
gi 488994816 161 TLTRtriQTLAATLLA----GRTVVLITHDP 187
Cdd:TIGR01842 487 EEGE---QALANAIKAlkarGITVVVITHRP 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-207 |
7.88e-20 |
|
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: 87.82 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLH-----------VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATcGEVVAsDGQPIQGrl 74
Cdd:COG4172 276 LEARDLKVWfpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRF-DGQDLDG-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 awMGQKDL-----------------LYPWLSVRDNVALGARLRGEKVD----RARVAALLEQVELSscADAR---PATLS 130
Cdd:COG4172 352 --LSRRALrplrrrmqvvfqdpfgsLSPRMTVGQIIAEGLRVHGPGLSaaerRARVAEALEEVGLD--PAARhryPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 131 GGMRQRAALARTL-YEDRPIVLmDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:COG4172 428 GGQRQRIAIARALiLEPKLLVL-DEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRALAHRVMVMK--DGKV 504
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
8-200 |
8.25e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.22 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 8 VRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWMGQ 79
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL-DAQPLESwsskafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALG------ARLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488994816 154 EPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-207 |
1.21e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRG--LSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG------ 72
Cdd:PRK10253 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGEHIQHyaskev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 --RLAWMGQKDLLYPWLSVRDNVALGAR------LRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:PRK10253 80 arRIGLLAQNATTPGDITVQELVARGRYphqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALR--EGKI 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-212 |
1.33e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.00 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI--------QGRLA 75
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDIstlkpeiyRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPwLSVRDNVALGARLRGEKVDRARVAALLEQVEL-SSCADARPATLSGGMRQRAALARTLYEDRPIVLMDE 154
Cdd:PRK10247 85 YCAQTPTLFG-DTVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 155 PFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEacrLSH--RLLVLSAADGDIDDSHH 212
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDE---INHadKVITLQPHAGEMQEARY 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-186 |
1.48e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.93 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSL-----HVGDRrlfdNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQPI----- 70
Cdd:PRK15056 2 MQQAGIVVNDVTVtwrngHTALR----DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-SILGQPTrqalq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 71 QGRLAWMGQK---DLLYPWLsVRDNVALGAR------LRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALAR 141
Cdd:PRK15056 77 KNLVAYVPQSeevDWSFPVL-VEDVVMMGRYghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488994816 142 TLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHD 186
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHN 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-186 |
1.62e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQpIQGRLAWMGQKDL--- 82
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDIT-IDTARSLSQQKGLirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 -------------LYPWLSVRDNVALGARL-----RGEKVDRARvaALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:PRK11264 83 lrqhvgfvfqnfnLFPHRTVLENIIEGPVIvkgepKEEATARAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488994816 145 EDRPIVLMDEPFSALD-TLTRTRIQTLAATLLAGRTVVLITHD 186
Cdd:PRK11264 161 MRPEVILFDEPTSALDpELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-200 |
2.41e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG---RLAW-M 77
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL-DGEPVRFrspRDAQaA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 G-----QKDLLYPWLSVRDNVALGA-RLRGEKVD----RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDR 147
Cdd:COG1129 80 GiaiihQELNLVPNLSVAENIFLGRePRRGGLIDwramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 148 PIVLMDEPFSAL-----DTLTRtRIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:COG1129 160 RVLILDEPTASLterevERLFR-IIRRLKA---QGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-185 |
4.14e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.18 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAG-LAPATCGEVVasdgqpIQGRLAWMGQkdllYPWL---SVRDNVALGAR 98
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVV------IRGSVAYVPQ----VSWIfnaTVRENILFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 99 LRGEKVDRA-RVAALLEQVELSSCAD-----ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT-LTRTRIQTLA 171
Cdd:PLN03232 705 FESERYWRAiDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCM 784
|
170
....*....|....
gi 488994816 172 ATLLAGRTVVLITH 185
Cdd:PLN03232 785 KDELKGKTRVLVTN 798
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-201 |
5.02e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 18 RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQ----PIQGR----LAWMGQKDLLYPWLSV 89
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllPLHARarrgIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGARLRG-----EKVDRARvaALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTR 164
Cdd:PRK10895 96 YDNLMAVLQIRDdlsaeQREDRAN--ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488994816 165 TRIQTLAATLLAGRTVVLIT-HDPQEACRLSHRLLVLS 201
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVS 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-194 |
5.64e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 11 LSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLApatcgEVVASDGQpIQGRLAWMGqKDLL------- 83
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI-----EIYDSKIK-VDGKVLYFG-KDIFqidaikl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 -------------YPWLSVRDNVALGARLRGEKvDRARVAALLEQV--------ELSSCADARPATLSGGMRQRAALART 142
Cdd:PRK14246 89 rkevgmvfqqpnpFPHLSIYDNIAYPLKSHGIK-EKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHDPQEACRLS 194
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVA 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-205 |
5.85e-19 |
|
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: 81.99 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPI-----------QGRLAWMGQKdllyPWL---S 88
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESepsfeatrsrnRYSVAYAAQK----PWLlnaT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGARLrgekvDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:cd03290 95 VEENITFGSPF-----NKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 158 ALDT-LTRTRIQTLAATLLAG--RTVVLITHDPQeacRLSHRLLVLSAADG 205
Cdd:cd03290 170 ALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQ---YLPHADWIIAMKDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
9.21e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 9.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV--------ASDGQPIQGRLA 75
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcarLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWLSVRDNVALGarLRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFG--LPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 156 FSALDTL-TRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRL-------LVLSAADGDIDDSHHLAGTPPRAPDAP 224
Cdd:PRK15439 168 TASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQLADRIsvmrdgtIALSGKTADLSTDDIIQAITPAAREKS 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-186 |
1.14e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLH--VGdRRLF----------DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQ 68
Cdd:COG4608 3 MAEPLLEVRDLKKHfpVR-GGLFgrtvgvvkavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-DGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 69 PIQGrlawMGQKDL-----------------LYPWLSVRDNVALGARL-----RGEKvdRARVAALLEQVELS-SCADAR 125
Cdd:COG4608 81 DITG----LSGRELrplrrrmqmvfqdpyasLNPRMTVGDIIAEPLRIhglasKAER--RERVAELLELVGLRpEHADRY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 126 PATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDtltrTRIQTLAATLLA------GRTVVLITHD 186
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD----VSIQAQVLNLLEdlqdelGLTYLFISHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-184 |
1.18e-18 |
|
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: 84.58 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 11 LSLHVGDrrLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGlapatcgEVVASDGQ-PIQGRLAWMGQkdllYPWL-- 87
Cdd:TIGR01271 434 FSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-------ELEPSEGKiKHSGRISFSPQ----TSWImp 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 -SVRDNVALGA---RLRGEKVDRArvAALLEQVELSSCADARP-----ATLSGGMRQRAALARTLYEDRPIVLMDEPFSA 158
Cdd:TIGR01271 501 gTIKDNIIFGLsydEYRYTSVIKA--CQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180
....*....|....*....|....*..
gi 488994816 159 LDTLTRTRI-QTLAATLLAGRTVVLIT 184
Cdd:TIGR01271 579 LDVVTEKEIfESCLCKLMSNKTRILVT 605
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-201 |
1.51e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLhvgdRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGR------LAWMG-- 78
Cdd:COG1129 258 EVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL-DGKPVRIRsprdaiRAGIAyv 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 ----QKDLLYPWLSVRDNV---ALGARLRGEKVDRARVAALLEQV--ELS---SCADARPATLSGGMRQRAALARTLYED 146
Cdd:COG1129 333 pedrKGEGLVLDLSIRENItlaSLDRLSRGGLLDRRRERALAEEYikRLRiktPSPEQPVGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 147 RPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAeGKAVIVISSELPELLGLSDRILVMR 468
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-164 |
1.71e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPAT------CGEVVASDGQPIQGRLAW 76
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASegeawlFGQPVDAGDIATRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDE 154
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170
....*....|
gi 488994816 155 PFSALDTLTR 164
Cdd:NF033858 424 PTSGVDPVAR 433
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-201 |
2.58e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 83.39 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLAPATC--GEVVASDGQP---IQGRLAWMGQKDLLYPWLSVRDNVALGARLRG---- 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPtkqILKRTGFVTQDDILYPHLTVRETLVFCSLLRLpksl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 102 EKVDRARVA-ALLEQVELSSCADARPAT-----LSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR-IQTLAATL 174
Cdd:PLN03211 174 TKQEKILVAeSVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRlVLTLGSLA 253
|
170 180
....*....|....*....|....*...
gi 488994816 175 LAGRTVVLITHDPQEAC-RLSHRLLVLS 201
Cdd:PLN03211 254 QKGKTIVTSMHQPSSRVyQMFDSVLVLS 281
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-190 |
3.62e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGE-------VVASDGQPI-QGRLAWMG---QKDLLYPWLSVR 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALaQLRREHFGfifQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQ 168
Cdd:PRK10535 105 QNVEVPAVYAGleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180
....*....|....*....|...
gi 488994816 169 TLAATLLA-GRTVVLITHDPQEA 190
Cdd:PRK10535 185 AILHQLRDrGHTVIIVTHDPQVA 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-200 |
4.59e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 10 GLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEvVASDGQPIqGRLAWMGQKDL------- 82
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN-VSWRGEPL-AKLNRAQRKAFrrdiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 -------LYPWLSVRDNVALGAR--LRGEKVDR-ARVAALLEQVELS-SCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:PRK10419 95 fqdsisaVNPRKTVREIIREPLRhlLSLDKAERlARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVM 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-187 |
6.48e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 10 GLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAP--ATCGEVVASDGQpiqgrlawmgqkdlLYPWL 87
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ--------------FGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALgarlrgeKVDRARVAALLEQVELSSCAD--ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRT 165
Cdd:COG2401 101 SLIDAIGR-------KGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....*..
gi 488994816 166 RiqtLAATLL-----AGRTVVLITHDP 187
Cdd:COG2401 174 R---VARNLQklarrAGITLVVATHHY 197
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-229 |
1.64e-17 |
|
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: 79.52 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHVGDrrLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGlapatcgEVVASDGQ-PIQGRLAWMGQKDL 82
Cdd:cd03291 38 NNLFFSNLCLVGAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-------ELEPSEGKiKHSGRISFSSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 LYPWlSVRDNVALGArlrgeKVDRARVAALLEQVELSSCADARPA-----------TLSGGMRQRAALARTLYEDRPIVL 151
Cdd:cd03291 109 IMPG-TIKENIIFGV-----SYDEYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 152 MDEPFSALDTLTRTRI-QTLAATLLAGRTVVLIThDPQEACRLSHRLLVLSaadgdiDDSHHLAGTPPR----APDAPDL 226
Cdd:cd03291 183 LDSPFGYLDVFTEKEIfESCVCKLMANKTRILVT-SKMEHLKKADKILILH------EGSSYFYGTFSElqslRPDFSSK 255
|
...
gi 488994816 227 LIG 229
Cdd:cd03291 256 LMG 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-227 |
1.81e-17 |
|
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: 81.02 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATC--GEVVAsDGQPIQGR---------L 74
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYW-SGSPLKASnirdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPWLSVRDNVALGAR--LRGEKVDRA----RVAALLEQVELSSCADARPAT-LSGGMRQRAALARTLYEDR 147
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEitLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 148 PIVLMDEPFSAldtLTRTRIQTLAATL--LAGRTV--VLITHDPQEACRLSHRLLVlsaadgdIDDSHHLAGTPPRAPDA 223
Cdd:TIGR02633 161 RLLILDEPSSS---LTEKETEILLDIIrdLKAHGVacVYISHKLNEVKAVCDTICV-------IRDGQHVATKDMSTMSE 230
|
....
gi 488994816 224 PDLL 227
Cdd:TIGR02633 231 DDII 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-202 |
2.72e-17 |
|
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: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLAWMGQKdllyPWL---SVR 90
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDISKiglhdlrsRISIIPQD----PVLfsgTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVALgarlRGEKVDRARVAALlEQVELSSCADARP-----------ATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:cd03244 96 SNLDP----FGEYSDEELWQAL-ERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 160 DTLTRTRIQTLAATLLAGRTVVLITHdpqeacRL-----SHRLLVLSA 202
Cdd:cd03244 171 DPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDK 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-206 |
2.74e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.62 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD-RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCG-------EVVASDGQPIQGRLAWM 77
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvkvmgrEVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQK--DLLYPwLSVRDNVALGAR---LRGEKVDRaRVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:PRK13647 85 FQDpdDQVFS-STVWDDVAFGPVnmgLDKDEVER-RVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 153 DEPFSALDTLTRTRIQTLAATL-LAGRTVVLITHDPQEACRLSHRLLVLSA----ADGD 206
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEgrvlAEGD 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-185 |
3.28e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLHVGDRRL--FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQgrlAWmgQ 79
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIA---DY--S 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSV------------RDNVALGArlrgEKVDRARVAALLEQVELSSCADA------------RPatLSGGMRQ 135
Cdd:PRK11160 409 EAALRQAISVvsqrvhlfsatlRDNLLLAA----PNASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 136 RAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITH 185
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
6-167 |
3.86e-17 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 79.99 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSL--HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQP--------IQGRLA 75
Cdd:TIGR03796 478 VELRNITFgySPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI-LFDGIPreeiprevLANSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWlSVRDNVALGARLRGEK--VDRARVAALLEQVElsscadARP-----------ATLSGGMRQRAALART 142
Cdd:TIGR03796 557 MVDQDIFLFEG-TVRDNLTLWDPTIPDAdlVRACKDAAIHDVIT------SRPggydaelaeggANLSGGQRQRLEIARA 629
|
170 180
....*....|....*....|....*
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRI 167
Cdd:TIGR03796 630 LVRNPSILILDEATSALDPETEKII 654
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-200 |
4.86e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGL--APATCGEVVASDGQPIQ--GRLA------ 75
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIELLGRTVQreGRLArdirks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 -----WMGQKDLLYPWLSVRDNVALGAR---------LRG-EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALA 140
Cdd:PRK09984 85 rantgYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 141 RTLYEDRPIVLMDEPFSALDTLT-RTRIQTLA-ATLLAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESaRIVMDTLRdINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-204 |
5.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGeVVASDGQPIQGRLAWMGQK---------DLLYPWL 87
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTAENVWNLRRkigmvfqnpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALGARLRG-------EKVDRARVAalleqVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PRK13642 98 TVEDDVAFGMENQGipreemiKRVDEALLA-----VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488994816 161 TLTRTRIQTLAATLLAGR--TVVLITHDPQEACRlSHRLLVLSAAD 204
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGE 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-186 |
5.27e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.59 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsdGQPIQgrLAWMGQ-KDLLY 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GETVK--LAYVDQsRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 PWLSVRDNVALGA---RLRGEKVD-RARVAAL----LEQvelsscaDARPATLSGGMRQRAALARTLYEDRPIVLMDEPF 156
Cdd:TIGR03719 399 PNKTVWEEISGGLdiiKLGKREIPsRAYVGRFnfkgSDQ-------QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170 180 190
....*....|....*....|....*....|..
gi 488994816 157 SALDTLTrtrIQTLAATLL--AGRTVVlITHD 186
Cdd:TIGR03719 472 NDLDVET---LRALEEALLnfAGCAVV-ISHD 499
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-190 |
7.54e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.48 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgQPIQGRLAWMGQKDL---------LYPWLSVRDN 92
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN-QAITDDNFEKLRKHIgivfqnpdnQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 93 VALGAR---LRGEKVDRaRVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQT 169
Cdd:PRK13648 105 VAFGLEnhaVPYDEMHR-RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180
....*....|....*....|...
gi 488994816 170 LAATLLAGR--TVVLITHDPQEA 190
Cdd:PRK13648 184 LVRKVKSEHniTIISITHDLSEA 206
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-204 |
8.44e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQ 79
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 KDLLYPWLSVRDNVALGARLRGEKVDrarVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVG---ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 160 DTLTRTRIQTLAATLLAGRTVVLIThdpqeacrlSHRLLVLSAAD 204
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLT---------SHQDLPLNKAD 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-201 |
8.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSL--HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQP-IQGRL 74
Cdd:PRK13632 6 VMIKVENVSFsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitISKENLKeIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQK-DLLYPWLSVRDNVALGarLRGEKVDR----ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPI 149
Cdd:PRK13632 86 GIIFQNpDNQFIGATVEDDIAFG--LENKKVPPkkmkDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488994816 150 VLMDEPFSALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACrLSHRLLVLS 201
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAI-LADKVIVFS 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-202 |
8.59e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVgDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPA----TCGEVVAsDGQPI-----QGRL- 74
Cdd:PRK10418 4 QIELRNIALQA-AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLL-DGKPVapcalRGRKi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQ--KDLLYPWLSVRDNVALGARLRGEKVDRARVAALLEQVELSSCA---DARPATLSGGMRQRAALARTLYEDRPI 149
Cdd:PRK10418 82 ATIMQnpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 150 VLMDEPFSALDTLTRTRIQTLAATLLAGRT--VVLITHDPQEACRLSHRLLVLSA 202
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSH 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-194 |
1.08e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.52 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGrlawmgqkdllYPWLSVRDNVALG----- 96
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHDLRD-----------YTLASLRNQVALVsqnvh 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 97 ----------ARLRGEKVDR------ARVAALLEQVE-----LSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:PRK11176 428 lfndtianniAYARTEQYSReqieeaARMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 156 FSALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:PRK11176 508 TSALDTESERAIQAALDELQKNRTSLVIAH------RLS 540
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-185 |
1.99e-16 |
|
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: 78.06 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 21 FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgqpIQGRLAWMGQKdllyPWL---SVRDNVALGA 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH------MKGSVAYVPQQ----AWIqndSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 98 RLRgEKVDRA--RVAALLEQVELSSCAD-----ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI--Q 168
Cdd:TIGR00957 724 ALN-EKYYQQvlEACALLPDLEILPSGDrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfeH 802
|
170
....*....|....*...
gi 488994816 169 TLAAT-LLAGRTVVLITH 185
Cdd:TIGR00957 803 VIGPEgVLKNKTRILVTH 820
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-200 |
1.99e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 36 LLGASGAGKTSLLRVMAGLAPATCGEV-----VASDGQ------PIQGRLAWMGQKDLLYPWLSVRDNVALGARlrgeKV 104
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIvlngrVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----KS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 105 DRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDtLTRTR-----IQTLAATLlagRT 179
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKRellpyLERLAREI---NI 180
|
170 180
....*....|....*....|..
gi 488994816 180 VVL-ITHDPQEACRLSHRLLVL 200
Cdd:PRK11144 181 PILyVSHSLDEILRLADRVVVL 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-194 |
2.02e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 4 PGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATcGEVvasdgqPIQGRLAWMGQ---- 79
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEV------RVEGRVEFFNQniye 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 -----------------KDLLYPwLSVRDNVALGARLRGEK--------VDRARVAALLEQvELSSCADARPATLSGGMR 134
Cdd:PRK14258 79 rrvnlnrlrrqvsmvhpKPNLFP-MSVYDNVAYGVKIVGWRpkleiddiVESALKDADLWD-EIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 135 QRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTL--AATLLAGRTVVLITHDPQEACRLS 194
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLiqSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-202 |
2.54e-16 |
|
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: 77.55 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI----QGRL-AWMG---QKDLLYPwL 87
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-DGQDIrdvtQASLrAAIGivpQDTVLFN-D 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALGaRL---RGEKVDRARVAALLEQVElsSCADA-------RPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:COG5265 447 TIAYNIAYG-RPdasEEEVEAAARAAQIHDFIE--SLPDGydtrvgeRGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488994816 158 ALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS-----HRLLVLSA 202
Cdd:COG5265 524 ALDSRTERAIQAALREVARGRTTLVIAH------RLStivdaDEILVLEA 567
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-186 |
3.46e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.28 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDN--LSFtVPGGQwVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIqGRLAwmgQKDLLYPWLSVRDNV 93
Cdd:TIGR03719 16 PKKEILKDisLSF-FPGAK-IGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV-GYLP---QEPQLDPTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 ALGARLRGEKVDR------------ARVAALLE-------------------QVELSSCA------DARPATLSGGMRQR 136
Cdd:TIGR03719 90 EEGVAEIKDALDRfneisakyaepdADFDKLAAeqaelqeiidaadawdldsQLEIAMDAlrcppwDADVTKLSGGERRR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488994816 137 AALARTLYEDRPIVLMDEPFSALDTLTrtrIQTLAATL--LAGrTVVLITHD 186
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLqeYPG-TVVAVTHD 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-200 |
3.98e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG----RLAW 76
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL-RGQHIEGlpghQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MG-----QKDLLYPWLSVRDN--VA----LGARL-------------RGEKVDRArvAALLEQVELSSCADARPATLSGG 132
Cdd:PRK11300 80 MGvvrtfQHVRLFREMTVIENllVAqhqqLKTGLfsgllktpafrraESEALDRA--ATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 133 MRQRAALARTLYEdRPIVLM-DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK11300 158 QQRRLEIARCMVT-QPEILMlDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-200 |
5.77e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.68 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI--------QGRLAWMGQKDLLYPWlS 88
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLvqydhhylHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGarLRGEKVDRARVAALLeqvelsSCAD---------------ARPATLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:TIGR00958 571 VRENIAYG--LTDTPDEEIMAAAKA------ANAHdfimefpngydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 154 EPFSALDTLTRTRIQTLAAtlLAGRTVVLITHDPQeACRLSHRLLVL 200
Cdd:TIGR00958 643 EATSALDAECEQLLQESRS--RASRTVLLIAHRLS-TVERADQILVL 686
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-194 |
6.15e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSL-HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG-------RLAWM 77
Cdd:PRK10790 341 IDIDNVSFaYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSlshsvlrQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALGARLRGEKVDRArvaalLEQVELSSCADARPA-----------TLSGGMRQRAALARTLYED 146
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQVWQA-----LETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 147 RPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH------RLS 536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-187 |
7.90e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.30 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG---LAPATCGEVVaSDGQPI----QGRLAWMGQKDLLYPWLS 88
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRL-VNGRPLdssfQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGARLR-------GEKVDraRVAALLEQVELSSCADARPATLSGGM----RQRAALARTLYEdRP--IVLMDEP 155
Cdd:TIGR00956 853 VRESLRFSAYLRqpksvskSEKME--YVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVA-KPklLLFLDEP 929
|
170 180 190
....*....|....*....|....*....|...
gi 488994816 156 FSALDTLTRTRI-QTLAATLLAGRTVVLITHDP 187
Cdd:TIGR00956 930 TSGLDSQTAWSIcKLMRKLADHGQAILCTIHQP 962
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-200 |
8.60e-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: 76.21 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAWMGQKDLLYPWLSVRDNVAL 95
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAtvagksILTNISDVHQNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 96 GARLRG---EKVDRARVAALlEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI-QTLA 171
Cdd:TIGR01257 2036 YARLRGvpaEEIEKVANWSI-QSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIV 2114
|
170 180
....*....|....*....|....*....
gi 488994816 172 ATLLAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-186 |
1.43e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsdGQPIQgrLAWMGQ-KDLLY 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--GETVK--LAYVDQsRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 P----WLSV---RDNVALGARlrgEKVDRARVAAL----LEQVELSScadarpaTLSGGMRQRAALARTLYEDRPIVLMD 153
Cdd:PRK11819 401 PnktvWEEIsggLDIIKVGNR---EIPSRAYVGRFnfkgGDQQKKVG-------VLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 488994816 154 EPFSALDtltrtrIQTLAA---TLL--AGrTVVLITHD 186
Cdd:PRK11819 471 EPTNDLD------VETLRAleeALLefPG-CAVVISHD 501
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-194 |
1.45e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.38 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGeVVASDGQPIQG--------RLAWMGQKDLLYPwL 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG-RILIDGTDIRTvtraslrrNIAVVFQDAGLFN-R 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALG------ARLRgEKVDRARVAALLEQVE--LSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL 159
Cdd:PRK13657 424 SIEDNIRVGrpdatdEEMR-AAAERAQAHDFIERKPdgYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190
....*....|....*....|....*....|....*
gi 488994816 160 DTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS 194
Cdd:PRK13657 503 DVETEAKVKAALDELMKGRTTFIIAH------RLS 531
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-207 |
1.64e-15 |
|
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: 75.22 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGL--APATCGEVV---------------ASDGQ 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 69 P-------------------------IQGRLAWMGQKDL-LYPWLSVRDNVALGARLRGEKVDRA--RVAALLEQVELSS 120
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsdklrrrIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAvgRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 121 CADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQT--LAATLLAGRTVVLITHDPQEACRLSHRLL 198
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNalEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....*....
gi 488994816 199 VLSaaDGDI 207
Cdd:TIGR03269 241 WLE--NGEI 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-209 |
3.70e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLS----LHVGD-------RRLF----------DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVA 64
Cdd:COG4586 2 IEVENLSktyrVYEKEpglkgalKGLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 65 SDGQPIQGRLAW-------MGQKDLLYPWLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADaRPA-TLSGGMR 134
Cdd:COG4586 82 LGYVPFKRRKEFarrigvvFGQRSQLWWDLPAIDSFRLLKAIYRipDAEYKKRLDELVELLDLGELLD-TPVrQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 135 QRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLS----AADGDID 208
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDhgriIYDGSLE 240
|
.
gi 488994816 209 D 209
Cdd:COG4586 241 E 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-239 |
4.37e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAS----------DGQ-- 68
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkDGQlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 69 --------PIQGRLAWMGQKDLLYPWLSVRDNV------ALGArlrGEKVDRARVAALLEQVELSSCADAR-PATLSGGM 133
Cdd:PRK10619 81 vadknqlrLLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGL---SKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 134 RQRAALARTLYEDRPIVLMDEPFSALD-TLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSaaDGDIDDSHH 212
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDpELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH--QGKIEEEGA 235
|
250 260
....*....|....*....|....*....
gi 488994816 213 lagtpprapdaPDLLIG--QAALLQQLMR 239
Cdd:PRK10619 236 -----------PEQLFGnpQSPRLQQFLK 253
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-212 |
4.78e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.44 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 14 HVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPI-----------QGRLAWMGQKDL 82
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS-GHDItrlknrevpflRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 LYPWLSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIAGASGDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488994816 161 -TLTRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSaaDGDIDDSHH 212
Cdd:PRK10908 170 dALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS--DGHLHGGVG 220
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-207 |
5.33e-15 |
|
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: 71.63 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNLSFTVPGGQWVSLLGASGAGKT----SLLRVMAGLAPATCGEVVAsDGQP-----IQGRLAWM---GQKDLLYPWL 87
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSltclAILGLLPPGLTQTSGEILL-DGRPllplsIRGRHIATimqNPRTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNV--ALGARLRGEKVDRARVAALLEQVELSSCA---DARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL 162
Cdd:TIGR02770 80 TMGNHAieTLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 163 TRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:TIGR02770 160 NQARVLKLLRELrqLFGTGILLITHDLGVVARIADEVAVMD--DGRI 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-217 |
6.62e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.03 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD-RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQ---GRLAWMGQK- 80
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKydkKSLLEVRKTv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 ---------DLLYPwlSVRDNVALGA---RLRGEKVDRaRVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP 148
Cdd:PRK13639 81 givfqnpddQLFAP--TVEEDVAFGPlnlGLSKEEVEK-RVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 149 IVLMDEPFSALDTLTRTRIQTLAATL-LAGRTVVLITHDPQEACRLSHRLLVLSaaDGDIDDShhlaGTP 217
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMS--DGKIIKE----GTP 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-186 |
6.71e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 14 HVGDRRLFDN--LSFtVPGGQwVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIqGRLAwmgQKDLLYPWLSVRD 91
Cdd:PRK11819 16 VPPKKQILKDisLSF-FPGAK-IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKV-GYLP---QEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 92 NVALGARLRGEKVDR-------------------ARVAALLE------------QVELSSCA------DARPATLSGGMR 134
Cdd:PRK11819 90 NVEEGVAEVKAALDRfneiyaayaepdadfdalaAEQGELQEiidaadawdldsQLEIAMDAlrcppwDAKVTKLSGGER 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488994816 135 QRAALARTLYEDRPIVLMDEPFSALDTLTrtrIQTLAATL--LAGrTVVLITHD 186
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLhdYPG-TVVAVTHD 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-186 |
1.08e-14 |
|
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: 72.79 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGD----RRLFDNLSFTVPGGQWVSLLGASGAGKT----SLLRVMAGlAPATCGEVVASDGQPIQG 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPD-PAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 rlawMGQKDL------------------LYPWLSVRDNVA----LGARLRGEKVdRARVAALLEQVEL---SSCADARPA 127
Cdd:COG4172 81 ----LSERELrrirgnriamifqepmtsLNPLHTIGKQIAevlrLHRGLSGAAA-RARALELLERVGIpdpERRLDAYPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488994816 128 TLSGGMRQRA----ALArtlyeDRPIVLM-DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHD 186
Cdd:COG4172 156 QLSGGQRQRVmiamALA-----NEPDLLIaDEPTTALDVTVQAQILDLLKDLQRelGMALLLITHD 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-209 |
1.49e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.69 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSllrvmaGLAPAtcgEVVASDGQPIQGRL-AWMGQKDLL 83
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPA---HV*GPDAGRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 YPWLSVRDNVALGAR----------LRGEKVD------RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYeDR 147
Cdd:NF000106 84 RRTIG*HRPVR*GRResfsgrenlyMIGR*LDlsrkdaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI-GR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 148 PIVL-MDEPFSALDTLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVLS----AADGDIDD 209
Cdd:NF000106 163 PAVLyLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDrgrvIADGKVDE 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-209 |
1.64e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQ--PIQGRLAWMG 78
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 QKDLLYPWLSVRD------NVALGaRLRGEKV------D----RARVAALLEQVELSSCADARPATLSGGMRQRAALART 142
Cdd:PRK09700 81 GIGIIYQELSVIDeltvleNLYIG-RHLTKKVcgvniiDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 143 LYEDRPIVLMDEPFSaldTLTRTRIQTLAATL----LAGRTVVLITHDPQEACRLSHRLLVL----SAADGDIDD 209
Cdd:PRK09700 160 LMLDAKVIIMDEPTS---SLTNKEVDYLFLIMnqlrKEGTAIVYISHKLAEIRRICDRYTVMkdgsSVCSGMVSD 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-197 |
5.48e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATC--GEVVAsDGQPIQGR----- 73
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIF-EGEELQASnirdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 ----LAWMGQKDLLYPWLSVRDNVALGARL-RGEKVD----RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLY 144
Cdd:PRK13549 80 eragIAIIHQELALVKELSVLENIFLGNEItPGGIMDydamYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 145 EDRPIVLMDEPFSALdtltrTRIQTlaATLLAgrtvvlITHDPQE---AC-RLSHRL 197
Cdd:PRK13549 160 KQARLLILDEPTASL-----TESET--AVLLD------IIRDLKAhgiACiYISHKL 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-200 |
5.52e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APG--IEVRGLslhvgdrrlfDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPIQGRLAWMGQK 80
Cdd:PRK13641 13 SPGtpMEKKGL----------DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA-GYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DL--------LYPWL-----SVRDNVALGARLRGEKVDRARVAAL--LEQVELS-SCADARPATLSGGMRQRAALARTLY 144
Cdd:PRK13641 82 KLrkkvslvfQFPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALkwLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488994816 145 EDRPIVLMDEPFSALDTLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-204 |
6.05e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEvVASDGQPIQG-----RLAW 76
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ-IQIDGKTATRgdrsrFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPWLSVRDNVALGARLRGEKVDRARVAAlLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPF 156
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSA-LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488994816 157 SALDTLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVLSAAD 204
Cdd:PRK13543 166 ANLDLEGITLVnRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-187 |
9.77e-14 |
|
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: 67.27 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG--LAPATCGEVVAsDGQPI----QGRLAWMGQKDLLYPWLSV 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILI-NGRPLdknfQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGARLRGEKV-DRARVAAlleQVELSscadARPAtlsggmrqraalartlyedrpIVLMDEPFSALDT----LTR 164
Cdd:cd03232 97 REALRFSALLRGLSVeQRKRLTI---GVELA----AKPS---------------------ILFLDEPTSGLDSqaayNIV 148
|
170 180
....*....|....*....|...
gi 488994816 165 TRIQTLAATllaGRTVVLITHDP 187
Cdd:cd03232 149 RFLKKLADS---GQAILCTIHQP 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-200 |
1.10e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 15 VGDRRLFDNLSFTVPGGQWVSLLGASGAGKTS----LLRVMAglapaTCGEVVAsDGQPIQG-------------RLAWM 77
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWF-DGQPLHNlnrrqllpvrhriQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 78 GQKDLLYPWLSVRDNVALGAR-----LRGEKVDrARVAALLEQVELSSCADAR-PATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:PRK15134 370 DPNSSLNPRLNVLQIIEEGLRvhqptLSAAQRE-QQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLAGRTV--VLITHDPQEACRLSHRLLVL 200
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVL 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-186 |
1.26e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGlapatcgEVVASDGQPIQgrlawmgQKDLLYP 85
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-------EVLLDDGRIIY-------EQDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 WL----------SVRDNVALGARLRGEKVDR------------------------------------ARVAALLEQVELS 119
Cdd:PRK11147 70 RLqqdpprnvegTVYDFVAEGIEEQAEYLKRyhdishlvetdpseknlnelaklqeqldhhnlwqleNRINEVLAQLGLD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 120 scADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTrtrIQTLAATLLAGR-TVVLITHD 186
Cdd:PRK11147 150 --PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQgSIIFISHD 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-185 |
2.48e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsdgqpiQGRLAWMGQKdllyPWL---SVRDNVAL- 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA------ERSIAYVPQQ----AWImnaTVRGNILFf 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 96 ----GARLRgekvDRARVAALLEQVE-----LSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR 166
Cdd:PTZ00243 745 deedAARLA----DAVRVSQLEADLAqlgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180
....*....|....*....|
gi 488994816 167 I-QTLAATLLAGRTVVLITH 185
Cdd:PTZ00243 821 VvEECFLGALAGKTRVLATH 840
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-185 |
2.51e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 18 RRLFDnLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDG-----------QPIQGRLAWMGQ--KDLLY 84
Cdd:PRK13643 20 RALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeiKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 PWLSVRDnVALGARLRG-EKVDRARVAA-LLEQVELS-SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:PRK13643 99 EETVLKD-VAFGPQNFGiPKEKAEKIAAeKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180
....*....|....*....|....*
gi 488994816 162 LTRTRIQTLAATL-LAGRTVVLITH 185
Cdd:PRK13643 178 KARIEMMQLFESIhQSGQTVVLVTH 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-200 |
2.79e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG-------- 72
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF-DGKDITDwqtakimr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 -RLAWMGQKDLLYPWLSVRDNVALGARLRGEKVDRARVAALLEQV-ELSSCADARPATLSGGMRQRAALARTLYEDRPIV 150
Cdd:PRK11614 80 eAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488994816 151 LMDEPFSALDTLTRTRI-QTLAATLLAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIfDTIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-235 |
2.81e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 5 GIEVRGLSlhvgDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvASDGQPIQGR------LAWMG 78
Cdd:PRK11288 257 RLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-YLDGKPIDIRsprdaiRAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 ------QKDLLYPWLSVRDNVALGARLR----GEKVDRARVAALLEQ------VELSScADARPATLSGGMRQRAALART 142
Cdd:PRK11288 332 lcpedrKAEGIIPVHSVADNINISARRHhlraGCLINNRWEAENADRfirslnIKTPS-REQLIMNLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLSaaDGDIddshhlAGTPPRAP 221
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGVADRIVVMR--EGRI------AGELAREQ 482
|
250
....*....|....
gi 488994816 222 DAPDLLIgQAALLQ 235
Cdd:PRK11288 483 ATERQAL-SLALPR 495
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-200 |
4.29e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 2 TAPGIEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGR-------- 73
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI-DGQEMRFAsttaalaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 74 -LAWMGQKDLLYPWLSVRDNVALGaRL--RGEKVDR----ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYED 146
Cdd:PRK11288 80 gVAIIYQELHLVPEMTVAENLYLG-QLphKGGIVNRrllnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 147 RPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAeGRVILYVSHRMEEIFALCDAITVF 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-186 |
6.31e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLS-LHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPIQGR----------L 74
Cdd:PRK13652 4 IETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-GEPITKEnirevrkfvgL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMGQKDLLYPwLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLM 152
Cdd:PRK13652 83 VFQNPDDQIFS-PTVEQDIAFGPINLGldEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 488994816 153 DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHD 186
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQ 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-160 |
1.55e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgQPIQGRLAWMGQKDLLYP 85
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----RNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 86 WLSVrdNVALGARLRGeKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PRK09544 81 TLPL--TVNRFLRLRP-GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-215 |
2.54e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 21 FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGR------------LAWMGQKDLLYPWLS 88
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIML-NGKEINALstaqrlarglvyLPEDRQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNV-ALGARLRGEKVDRARVAALLEQVELS---SCADARPA--TLSGGMRQRAALARTLyEDRPIVL-MDEPFSALDT 161
Cdd:PRK15439 358 LAWNVcALTHNRRGFWIKPARENAVLERYRRAlniKFNHAEQAarTLSGGNQQKVLIAKCL-EASPQLLiVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 162 LTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLsaADGDIddSHHLAG 215
Cdd:PRK15439 437 SARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMADRVLVM--HQGEI--SGALTG 487
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-209 |
2.77e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 13 LHVGDRrlFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATcGEVVAsDGQPIQG--------RLAWMGQKDLLY 84
Cdd:COG4138 6 VAVAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILL-NGRPLSDwsaaelarHRAYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 PWLSVRDNVALG--ARLRGEKVDRArVAALLEQVELsSCADARPAT-LSGGMRQRAALARTLYEDRP-------IVLMDE 154
Cdd:COG4138 82 FAMPVFQYLALHqpAGASSEAVEQL-LAQLAEALGL-EDKLSRPLTqLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994816 155 PFSALD----TLTRTRIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVLSA----ADGDIDD 209
Cdd:COG4138 160 PMNSLDvaqqAALDRLLRELCQ---QGITVVMSSHDLNHTLRHADRVWLLKQgklvASGETAE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-201 |
2.97e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHvGDRRL--FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG------RL 74
Cdd:COG3845 255 EVVLEVENLSVR-DDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL-DGEDITGlsprerRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 75 AWMG------QKDLLYPWLSVRDNVALGAR-----LRGEKVDRARVAALLEQ------VELSScADARPATLSGGMRQRA 137
Cdd:COG3845 333 LGVAyipedrLGRGLVPDMSVAENLILGRYrrppfSRGGFLDRKAIRAFAEElieefdVRTPG-PDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 138 ALARTLYEDRPIVLMDEPFSALD----TLTRTRIQTLAAtllAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRD---AGAAVLLISEDLDEILALSDRIAVMY 476
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-200 |
3.95e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV----------ASDGQPIQGRLAWMGQKDL--LYPWLSV 89
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlsPGKLQALRRDIQFIFQDPYasLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGARLRG---EKVDRARVAALLEQVELSSCADAR-PATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRT 165
Cdd:PRK10261 421 GDSIMEPLRVHGllpGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180 190
....*....|....*....|....*....|....*..
gi 488994816 166 RIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10261 501 QIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVM 537
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-200 |
7.49e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHV---GDRRLF----------DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgqpiqg 72
Cdd:PRK15079 9 LEVADLKVHFdikDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 73 rlaWMGqKDLL----YPWLSVRDNV---------ALGARLR-GE-----------KVDRA----RVAALLEQVELSSCAD 123
Cdd:PRK15079 80 ---WLG-KDLLgmkdDEWRAVRSDIqmifqdplaSLNPRMTiGEiiaeplrtyhpKLSRQevkdRVKAMMLKVGLLPNLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 124 AR-PATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDtltrTRIQTLAATLLA------GRTVVLITHDPQEACRLSHR 196
Cdd:PRK15079 156 NRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD----VSIQAQVVNLLQqlqremGLSLIFIAHDLAVVKHISDR 231
|
....
gi 488994816 197 LLVL 200
Cdd:PRK15079 232 VLVM 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-202 |
1.03e-11 |
|
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: 62.04 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDR--RLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQG--------RLA 75
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWlSVRDNValgarlrgEKVDRARVAALLEQVELSSCADarpaTLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL--------DPFDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488994816 156 FSALDTLTRTRIQTLAATLLAGRTVVLITHdpqeacRLS-----HRLLVLSA 202
Cdd:cd03369 153 TASIDYATDALIQKTIREEFTNSTILTIAH------RLRtiidyDKILVMDA 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-217 |
1.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.14 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGR---LAWMGQKDLL---YPWL--- 87
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-DGVDITDKkvkLSDIRKKVGLvfqYPEYqlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 --SVRDNVALGARLRGEKVD--RARVAALLEQVELS--SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:PRK13637 98 eeTIEKDIAFGPINLGLSEEeiENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488994816 162 LTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDIDdshhLAGTP 217
Cdd:PRK13637 178 KGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMN--KGKCE----LQGTP 229
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-187 |
1.21e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.10 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLAPATC--GEVVASDGQPIQGRLA----WMGQKDLLYPWLSVRDNVALGARLR---- 100
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGFPKKQETFArisgYCEQNDIHSPQVTVRESLIYSAFLRlpke 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 101 GEKVDRAR-VAALLEQVELSSCADA---RPAT--LSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI-QTLAAT 173
Cdd:PLN03140 986 VSKEEKMMfVDEVMELVELDNLKDAivgLPGVtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVmRTVRNT 1065
|
170
....*....|....
gi 488994816 174 LLAGRTVVLITHDP 187
Cdd:PLN03140 1066 VDTGRTVVCTIHQP 1079
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-200 |
1.40e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD---RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLAWMG---- 78
Cdd:TIGR02633 258 LEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNPAQAirag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 --------QKDLLYPWLSVRDNVALGARLRGEKVDR----ARVAALLEQVELSSCADARP----ATLSGGMRQRAALART 142
Cdd:TIGR02633 338 iamvpedrKRHGIVPILGVGKNITLSVLKSFCFKMRidaaAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKM 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 143 LYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-201 |
5.64e-11 |
|
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: 60.50 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGQPIQGRLAwMGQKDLLYpwlSVRDNVALGARLRGEKV 104
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeieldtVSYKPQYIKADYE-GTVRDLLS---SITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 105 DRARVAALLEQvelsscadaRPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR----IQTLAatLLAGRTV 180
Cdd:cd03237 101 KPLQIEQILDR---------EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMaskvIRRFA--ENNEKTA 169
|
170 180
....*....|....*....|.
gi 488994816 181 VLITHDPQEACRLSHRLLVLS 201
Cdd:cd03237 170 FVVEHDIIMIDYLADRLIVFE 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-185 |
6.01e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLApATCGEV----VASDGQPIQG-RLAW--MGQKDLLYPWlS 88
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIqidgVSWNSVTLQTwRKAFgvIPQKVFIFSG-T 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGARLRGEKVdrARVAallEQVELSSCADARPA-----------TLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:TIGR01271 1308 FRKNLDPYEQWSDEEI--WKVA---EEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190
....*....|....*....|....*....|.
gi 488994816 158 ALDTLTrtrIQTLAATL---LAGRTVVLITH 185
Cdd:TIGR01271 1383 HLDPVT---LQIIRKTLkqsFSNCTVILSEH 1410
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-186 |
6.09e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSLHVGDRR-LF---------DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPI 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRgLFkperlvkalDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 71 QGRLAwMGQKDL--------------LYPWLSVRD--------NVALGARLRgekvdRARVAALLEQVEL-SSCADARPA 127
Cdd:PRK11308 80 LKADP-EAQKLLrqkiqivfqnpygsLNPRKKVGQileeplliNTSLSAAER-----REKALAMMAKVGLrPEHYDRYPH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994816 128 TLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHD 186
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHD 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-186 |
8.07e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGD-RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVaSDGQPI----QGRLAWMGQK 80
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-FDGKPIdysrKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DLLYP-------WLSVRDNVALGARLRG--EKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVL 151
Cdd:PRK13636 85 GMVFQdpdnqlfSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 488994816 152 MDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHD 186
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHD 201
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-217 |
8.26e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgqpiqgrlawMGQKDLLYPW--------------- 86
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG----------LDTSDEENLWdirnkagmvfqnpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 87 ----LSVRDNVALGARLRGEKVD--RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PRK13633 97 qivaTIVEEDVAFGPENLGIPPEeiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 161 TLTRTRIQTLAATL--LAGRTVVLITHDPQEACRlSHRLLVLSaaDGDIDdshhLAGTP 217
Cdd:PRK13633 177 PSGRREVVNTIKELnkKYGITIILITHYMEEAVE-ADRIIVMD--SGKVV----MEGTP 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-200 |
1.95e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAWMG------------QKDLLYPWLSV 89
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL-DGHEVVTRSPQDGlangivyisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 RDNVALGArLR-----GEKVDRARvaallEQVELSS----------CADARPATLSGGMRQRAALARTLYeDRPIVL-MD 153
Cdd:PRK10762 348 KENMSLTA-LRyfsraGGSLKHAD-----EQQAVSDfirlfniktpSMEQAIGLLSGGNQQKVAIARGLM-TRPKVLiLD 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 154 EPFSALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-188 |
2.10e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsdGQPIQgrLAWMGQ-KDLLYP 85
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC--GTKLE--VAYFDQhRAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 WLSVRDNVALGAR---LRGekVDRARVAALleQVELSSCADAR-PA-TLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PRK11147 397 EKTVMDNLAEGKQevmVNG--RPRHVLGYL--QDFLFHPKRAMtPVkALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180 190
....*....|....*....|....*....|..
gi 488994816 161 tltrtrIQTLA--ATLLAGR--TVVLITHDPQ 188
Cdd:PRK11147 473 ------VETLEllEELLDSYqgTVLLVSHDRQ 498
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-185 |
3.31e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 18 RRLFDnLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDG-----------QPIQGRLAWMGQ--KDLLY 84
Cdd:PRK13649 21 RALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdiKQIRKKVGLVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 85 PWlSVRDNVALGARLRGEKVDRARVAAL--LEQVELS-SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:PRK13649 100 EE-TVLKDVAFGPQNFGVSQEEAEALARekLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180
....*....|....*....|....*
gi 488994816 162 LTRTRIQTLAATL-LAGRTVVLITH 185
Cdd:PRK13649 179 KGRKELMTLFKKLhQSGMTIVLVTH 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-160 |
7.57e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLA----PATC------GEVVASDGQPIQ---- 71
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgiPKNCqilhveQEVVGDDTTALQcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 72 ------------GRLAwMGQKDLLYPWLSVRDNV---------ALGARL-----RGEKVD----RARVAALLEQVELSSC 121
Cdd:PLN03073 258 tdiertqlleeeAQLV-AQQRELEFETETGKGKGankdgvdkdAVSQRLeeiykRLELIDaytaEARAASILAGLSFTPE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 122 ADARPA-TLSGGMRQRAALARTLYEDRPIVLMDEPFSALD 160
Cdd:PLN03073 337 MQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-170 |
7.73e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLAWMGQK---------DLLYPW------- 86
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRirmifqdpsTSLNPRqrisqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 87 -LSVRDNVALGARLRgekvdRARVAALLEQVEL-SSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTR 164
Cdd:PRK15112 111 dFPLRLNTDLEPEQR-----EKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
....*.
gi 488994816 165 TRIQTL 170
Cdd:PRK15112 186 SQLINL 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-207 |
1.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSlHVGDRRL------FDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV----ASDGQPIQGRLA 75
Cdd:PRK13651 3 IKVKNIV-KIFNKKLptelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 76 WMGQKDLLYPWLS----------------------------VRDNVALGARLRGEKVDRA--RVAALLEQVELS-SCADA 124
Cdd:PRK13651 82 KVLEKLVIQKTRFkkikkikeirrrvgvvfqfaeyqlfeqtIEKDIIFGPVSMGVSKEEAkkRAAKYIELVGLDeSYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 125 RPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATL-LAGRTVVLITHDPQEACRLSHRLLVLSaa 203
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFK-- 239
|
....
gi 488994816 204 DGDI 207
Cdd:PRK13651 240 DGKI 243
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-202 |
1.24e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDR----RLFDNLSFTVPGGQWVSLLGASGAGKT-SLLRVMaGLAPATcGEVVAS----DGQPIQgRLAW 76
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLIDYP-GRVMAEklefNGQDLQ-RISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDL---------------LYPWLSVRDNV--ALGARLRG-EKVDRARVAALLEQVEL---SSCADARPATLSGGMRQ 135
Cdd:PRK11022 81 KERRNLvgaevamifqdpmtsLNPCYTVGFQImeAIKVHQGGnKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 136 RAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGR--TVVLITHDPQEACRLSHRLLVLSA 202
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAAHKIIVMYA 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-227 |
1.46e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 18 RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATcgevVASDGQPIQGRLAWMGQKDLLYPWL---------- 87
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG----GAPRGARVTGDVTLNGEPLAAIDAPrlarlravlp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 ---------SVRDNVALG----ARLRGEKV--DRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRP---- 148
Cdd:PRK13547 90 qaaqpafafSAREIVLLGryphARRAGALThrDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 149 -----IVLMDEPFSALDTLTRTR----IQTLAATLLAGrtVVLITHDPQEACRLSHRLLVLsaADGDIddshhLAGTPPR 219
Cdd:PRK13547 170 aqpprYLLLDEPTAALDLAHQHRlldtVRRLARDWNLG--VLAIVHDPNLAARHADRIAML--ADGAI-----VAHGAPA 240
|
....*...
gi 488994816 220 APDAPDLL 227
Cdd:PRK13547 241 DVLTPAHI 248
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-185 |
1.55e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.79 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHV--GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLApATCGEV----VASDGQPIQG-RLAW-- 76
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIqidgVSWNSVPLQKwRKAFgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPWlSVRDNVALGARLRGEKVdrARVAallEQVELSSCADARPA-----------TLSGGMRQRAALARTLYE 145
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGKWSDEEI--WKVA---EEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 146 DRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTVVLITH 185
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-185 |
1.59e-09 |
|
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: 56.00 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLapatcgevvaSDGQPIQGRLAWMGQkDLLYp 85
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----------PKYEVTEGEILFKGE-DITD- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 wLSVRDNVALGARL---RGEKVDRARVAALLEQVElsscadarpATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDtL 162
Cdd:cd03217 69 -LPPEERARLGIFLafqYPPEIPGVKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-I 137
|
170 180
....*....|....*....|....*
gi 488994816 163 TRTRI--QTLAATLLAGRTVVLITH 185
Cdd:cd03217 138 DALRLvaEVINKLREEGKSVLIITH 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-189 |
2.02e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEV------VASDGqPIQGRLAWMG---QKDLLYPWLSVRDN 92
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlylgkeVTFNG-PKSSQEAGIGiihQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 93 VALGArlrgEKVDR----------ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSAL-DT 161
Cdd:PRK10762 100 IFLGR----EFVNRfgridwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDT 175
|
170 180 190
....*....|....*....|....*....|.
gi 488994816 162 LTRTR---IQTLAAtllAGRTVVLITHDPQE 189
Cdd:PRK10762 176 ETESLfrvIRELKS---QGRGIVYISHRLKE 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-200 |
2.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 19 RLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLAWMGQKDL--------LYPWL--- 87
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLrkeiglvfQFPEYqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 --SVRDNVALGARLRGEKVDRA--RVAALLEQVEL-SSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL 162
Cdd:PRK13645 105 qeTIEKDIAFGPVNLGENKQEAykKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 163 TRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK13645 185 GEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-204 |
2.83e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 17 DRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgQPI--------QGRLAWMGQKDLLYPwLS 88
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-IPLtklqldswRSRLAVVSQTPFLFS-DT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 89 VRDNVALGarlrgekvdraRVAALLEQVE----LSSCAD--------------ARPATLSGGMRQRAALARTLYEDRPIV 150
Cdd:PRK10789 405 VANNIALG-----------RPDATQQEIEhvarLASVHDdilrlpqgydtevgERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488994816 151 LMDEPFSALDTLTRTRIQTLAATLLAGRTVVLIthdpqeacrlSHRLLVLSAAD 204
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS----------AHRLSALTEAS 517
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-200 |
4.57e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 8 VRGLSLHVGDRRLF----DNLSFTVPGGQWVSLLGASGAGKT----SLLRVM-AGLAPATCGEVV--------------- 63
Cdd:PRK10261 15 VENLNIAFMQEQQKiaavRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeQAGGLVQCDKMLlrrrsrqvielseqs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 64 ASDGQPIQGR-LAWMGQKDL--LYPWLSVRDNVALGARL-RGEKVDRARVAA--LLEQV---ELSSCADARPATLSGGMR 134
Cdd:PRK10261 95 AAQMRHVRGAdMAMIFQEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAkrMLDQVripEAQTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 135 QRAALARTLyEDRPIVLM-DEPFSALDTLTRTRIQTLAATLLAGRT--VVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10261 175 QRVMIAMAL-SCRPAVLIaDEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-208 |
5.87e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgqpiQGRLAWMGQ------ 79
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE----NANIGYYAQdhaydf 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 80 -KDL-LYPWLSvrdnvalgaRLRGEKVDRARVAALLEQVeLSSCADARPA--TLSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:PRK15064 396 eNDLtLFDWMS---------QWRQEGDDEQAVRGTLGRL-LFSQDDIKKSvkVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 156 FSALDTLTrtrIQTL--AATLLAGrTVVLITHDPQEACRLSHRLLVLSaADGDID 208
Cdd:PRK15064 466 TNHMDMES---IESLnmALEKYEG-TLIFVSHDREFVSSLATRIIEIT-PDGVVD 515
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-186 |
6.32e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG-LAPaTCGEVVASDGQpiqgRLAWMGQKDLLYPWLSVRDNVA 94
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEP-SAGNVSLDPNE----RLGKLRQDQFAFEEFTVLDTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 95 LG-ARLRGEKVDRARVAALLEQVE--------LSS--------CADARPATL-----------SGGMRQ-------RAAL 139
Cdd:PRK15064 87 MGhTELWEVKQERDRIYALPEMSEedgmkvadLEVkfaemdgyTAEARAGELllgvgipeeqhYGLMSEvapgwklRVLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488994816 140 ARTLYEDRPIVLMDEPFSALDTLTrtrIQTLAATLLAGR-TVVLITHD 186
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNsTMIIISHD 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-187 |
1.17e-08 |
|
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: 54.75 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVasdgQPIQGRLAWMGQKdllyPWLSV---RDNV--- 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT----KPAKGKLFYVPQR----PYMTLgtlRDQIiyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 --ALGARLRGekVDRARVAALLEQVEL----------SSCADARPaTLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:TIGR00954 539 dsSEDMKRRG--LSDKDLEQILDNVQLthilereggwSAVQDWMD-VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*.
gi 488994816 162 LTRTRIQTLAATllAGRTVVLITHDP 187
Cdd:TIGR00954 616 DVEGYMYRLCRE--FGITLFSVSHRK 639
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-200 |
1.29e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 18 RRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGR---------LAWMGQ---KDLLYP 85
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRnpqqaiaqgIAMVPEdrkRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 WLSVRDNVALGARLRGEKVDRARVAALLEQVELS--------SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:PRK13549 355 VMGVGKNITLAALDRFTGGSRIDDAAELKTILESiqrlkvktASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488994816 158 ALDTLTRTRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-186 |
1.35e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRRlFD--NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRlawmGQKDLL 83
Cdd:PRK10522 323 LELRNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAE----QPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 YPWLSVRDNVALGARL---RGEKVDRARVAALLEQVELS---SCADARPAT--LSGGMRQRAALARTLYEDRPIVLMDEP 155
Cdd:PRK10522 397 KLFSAVFTDFHLFDQLlgpEGKPANPALVEKWLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190
....*....|....*....|....*....|...
gi 488994816 156 FSALD-TLTRTRIQTLAATLLA-GRTVVLITHD 186
Cdd:PRK10522 477 AADQDpHFRREFYQVLLPLLQEmGKTIFAISHD 509
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-200 |
1.75e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.87 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 18 RRLFDnLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgQPIQgrlAWMGQKDL--------------- 82
Cdd:PRK13634 21 RALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE-RVIT---AGKKNKKLkplrkkvgivfqfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 83 --LYPwLSVRDNVALGARLRGEKVDRA--RVAALLEQVELSSCADAR-PATLSGGMRQRAALARTLYEDRPIVLMDEPFS 157
Cdd:PRK13634 96 hqLFE-ETVEKDICFGPMNFGVSEEDAkqKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 158 ALDTLTRTRIQTLAATL--LAGRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-184 |
2.03e-08 |
|
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: 52.65 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPAT---------CGEVVASDGQPIQGRLAWMGQKDLLYPWLSVR 90
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvegdihyNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNVALGARLRGEKVDRArvaalleqvelsscadarpatLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTR----TR 166
Cdd:cd03233 102 ETLDFALRCKGNEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAleilKC 160
|
170
....*....|....*...
gi 488994816 167 IQTLAATLlagRTVVLIT 184
Cdd:cd03233 161 IRTMADVL---KTTTFVS 175
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-200 |
2.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVV-----ASDGQPIQGRLAWMG----QKDLLYPWLSVRDNV 93
Cdd:PRK13644 20 NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidTGDFSKLQGIRKLVGivfqNPETQFVGRTVEEDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 ALGAR--------LRgEKVDRARVAALLEQVELSScadarPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLT-R 164
Cdd:PRK13644 100 AFGPEnlclppieIR-KRVDRALAEIGLEKYRHRS-----PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgI 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 488994816 165 TRIQTLAATLLAGRTVVLITHDPQEaCRLSHRLLVL 200
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVM 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-185 |
5.42e-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: 53.03 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 23 NLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIqgrlAWMGQKDLLYPWLSV-RDNVALGARLR- 100
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGLNI----AKIGLHDLRFKITIIpQDPVLFSGSLRm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 101 -----GEKVDRaRVAALLEQVELSSCADARPA-----------TLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTR 164
Cdd:TIGR00957 1379 nldpfSQYSDE-EVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
170 180
....*....|....*....|.
gi 488994816 165 TRIQTLAATLLAGRTVVLITH 185
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAH 1478
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
129-188 |
1.51e-07 |
|
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: 49.67 E-value: 1.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 129 LSGGMRQRAALARTL----YEDRPIVLMDEPFSALDTLTRTRI-QTLAATLLAGRTVVLITHDPQ 188
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALaEAILEHLVKGAQVIVITHLPE 142
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-208 |
1.56e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVgdrrlFDNLSFTVPGGQWVSLLGASGAGKTSLlrVMAGLAPATCGEVVASDGQPIQGRLAWMGQkdllyp 85
Cdd:cd03238 1 LTVSGANVHN-----LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLISFLPKFSRNKLIFIDQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 wLSVRDNVALGARLRGEKVdrarvaalleqvelsscadarpATLSGGMRQRAALARTLYEDRP--IVLMDEPFSALD-TL 162
Cdd:cd03238 68 -LQFLIDVGLGYLTLGQKL----------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHqQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488994816 163 TRTRIQTLAATLLAGRTVVLITHDPQeacrlshrllVLSAADGDID 208
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLD----------VLSSADWIID 160
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
102-186 |
1.59e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 102 EKVD-RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGRTV 180
Cdd:PRK13409 185 KKVDeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV 264
|
....*.
gi 488994816 181 VLITHD 186
Cdd:PRK13409 265 LVVEHD 270
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-207 |
1.65e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.93 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDG-----------QPIQGRLAWMGQkdllYPWL--- 87
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithktkdkyiRPVRKRIGMVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 --SVRDNVALGARLRGEKVDRARVAA--LLEQVELS-SCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTL 162
Cdd:PRK13646 100 edTVEREIIFGPKNFKMNLDEVKNYAhrLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488994816 163 TRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVLSaaDGDI 207
Cdd:PRK13646 180 SKRQVMRLLKSLQTdeNKTIILVSHDMNEVARYADEVIVMK--EGSI 224
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
20-188 |
1.69e-07 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 50.44 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQgrlawMGQKDLLYPWLSVRDNVALGARL 99
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDALP-----LGANSFILPGLTGEENARMMASL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 100 RGekVDRARVAALLEQV-ELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLAGR 178
Cdd:PRK15177 77 YG--LDGDEFSHFCYQLtQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQQK 154
|
170
....*....|
gi 488994816 179 TVVLITHDPQ 188
Cdd:PRK15177 155 GLIVLTHNPR 164
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-186 |
1.81e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 11 LSLHVGDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsdgqPIQGRLAWMGQKDllyPWLSV- 89
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF----PGNWQLAWVNQET---PALPQp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 90 ---------RDNVALGARLR--GEKVD-------------------RARVAALLEQVELSSCADARP-ATLSGGMRQRAA 138
Cdd:PRK10636 80 aleyvidgdREYRQLEAQLHdaNERNDghaiatihgkldaidawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488994816 139 LARTLYEDRPIVLMDEPFSALDtltrtriqtLAATLLAGR-------TVVLITHD 186
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLD---------LDAVIWLEKwlksyqgTLILISHD 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-208 |
3.47e-07 |
|
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: 48.52 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 36 LLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQGRLAWMGQKDLLYPwlsvrdnvalgarlrgekvdrarvaalleq 115
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 116 velsscadaRPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLL-------AGRTVVLITHDPQ 188
Cdd:smart00382 57 ---------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLTVILTTNDEK 127
|
170 180
....*....|....*....|
gi 488994816 189 EacrlSHRLLVLSAADGDID 208
Cdd:smart00382 128 D----LGPALLRRRFDRRIV 143
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
11-187 |
3.81e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 11 LSLHVGDRRLFDnLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQ--PIQG-RLAWMGQKDLLYPWL 87
Cdd:PRK13541 7 LQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNinNIAKpYCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 88 SVRDNVALGARLRGEKvdrARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI 167
Cdd:PRK13541 86 TVFENLKFWSEIYNSA---ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|.
gi 488994816 168 QTLAATLL-AGRTVVLITHDP 187
Cdd:PRK13541 163 NNLIVMKAnSGGIVLLSSHLE 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
102-186 |
4.16e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 102 EKVD-RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTR----IQTLAAtllA 176
Cdd:COG1245 185 EKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNvarlIRELAE---E 261
|
90
....*....|
gi 488994816 177 GRTVVLITHD 186
Cdd:COG1245 262 GKYVLVVEHD 271
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-183 |
4.62e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 12 SLHV--GDRRLFDNL-----SFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIqgRLAWMGQK---- 80
Cdd:PRK10938 3 SLQIsqGTFRLSDTKtlqlpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHIT--RLSFEQLQklvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 --------DLLYPwlsVRDNVALGAR--LRGEKVDRARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIV 150
Cdd:PRK10938 81 dewqrnntDMLSP---GEDDTGRTTAeiIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190
....*....|....*....|....*....|....
gi 488994816 151 LMDEPFSALDTLTRTRIQTLAATLLA-GRTVVLI 183
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQsGITLVLV 191
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
31-207 |
5.13e-07 |
|
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: 49.14 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDG--------QPIQGRLAWMGQKDLLYPWlSVRDNvalgarLRGE 102
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGidisklplHTLRSRLSIILQDPILFSG-SIRFN------LDPE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 103 -KVDRARVAALLEQVELSSCADARPATL-----------SGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTL 170
Cdd:cd03288 119 cKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 171 AATLLAGRTVVLITHdpqeacRLSHRL---LVLSAADGDI 207
Cdd:cd03288 199 VMTAFADRTVVTIAH------RVSTILdadLVLVLSRGIL 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-201 |
5.72e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 6 IEVRGLSLHVGDRR---LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDGQPIQG-RLAW----- 76
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDiNLKWwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 --MGQKDLL----------YPWLSVRD------------------------------------------NVALGARLRGE 102
Cdd:PTZ00265 463 gvVSQDPLLfsnsiknnikYSLYSLKDlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 103 KVDRARVAALLEQVELSSCADARP-----------ATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLA 171
Cdd:PTZ00265 543 TIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|..
gi 488994816 172 ATLLA--GRTVVLITHDpQEACRLSHRLLVLS 201
Cdd:PTZ00265 623 NNLKGneNRITIIIAHR-LSTIRYANTIFVLS 653
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-202 |
7.99e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 24 LSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATcGEVVAsDGQPIQG--------RLAWMGQKDLLYPWLSVRDNVAL 95
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQF-AGQPLEAwsaaelarHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 96 GarlRGEKVDRARVAALLEQV-ELSSCAD--ARPA-TLSGGMRQRAALA-------RTLYEDRPIVLMDEPFSALDTLTR 164
Cdd:PRK03695 93 H---QPDKTRTEAVASALNEVaEALGLDDklGRSVnQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQ 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 488994816 165 TRIQTLAATLLA-GRTVVLITHDPQEACRLSHRLLVLSA 202
Cdd:PRK03695 170 AALDRLLSELCQqGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-185 |
8.37e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVvasdgqPIQGRLAWMGQKDLLYPWLSVRDNVALGARLRG 101
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV------DIKGSAALIAISSGLNGQLTGIENIELKGLMMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 102 EKVDRAR--VAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALD-TLTRTRIQTLAATLLAGR 178
Cdd:PRK13545 115 LTKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDKMNEFKEQGK 194
|
....*..
gi 488994816 179 TVVLITH 185
Cdd:PRK13545 195 TIFFISH 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-186 |
3.01e-06 |
|
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: 46.98 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAG-LAPATCG--------EVV-ASDGQPIQGRLAWMGQKDL----------LYPwLSVR 90
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNLGKfddppdwdEILdEFRGSELQNYFTKLLEGDVkvivkpqyvdLIP-KAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNValGARLrgEKVD-RARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQT 169
Cdd:cd03236 105 GKV--GELL--KKKDeRGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170
....*....|....*...
gi 488994816 170 LAATLLA-GRTVVLITHD 186
Cdd:cd03236 181 LIRELAEdDNYVLVVEHD 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-200 |
4.11e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLA--------WMGQKDL-LYPWLSVRDN 92
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-QGKEIDFKSSkealengiSMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 93 VALGAR-LRGEKVDRARV----AALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRI 167
Cdd:PRK10982 94 MWLGRYpTKGMFVDQDKMyrdtKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
170 180 190
....*....|....*....|....*....|....
gi 488994816 168 QTLAATLLA-GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK10982 174 FTIIRKLKErGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-201 |
4.35e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.77 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASD---GQPIQGRLAWMG-------------------- 78
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKKNNHELITNpyskkiknfkelrrrvsmvf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 79 ------------QKDLLY-PwlsvrdnVALGARlrgeKVDRARVAAL-LEQVEL-SSCADARPATLSGGMRQRAALARTL 143
Cdd:PRK13631 123 qfpeyqlfkdtiEKDIMFgP-------VALGVK----KSEAKKLAKFyLNKMGLdDSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488994816 144 YEDRPIVLMDEPFSALDTL-TRTRIQTLAATLLAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
126-186 |
5.52e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.64 E-value: 5.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994816 126 PATLSGGMRQRAALARTLYeDRPIVLM-DEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHD 186
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALL-CRPKLLIaDEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHD 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
36-186 |
7.18e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.77 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 36 LLGASGAGKTSLLRVMAGLAPATCGEVVASdGQPI----QGRLAWMGQKDLLYP-------WLSVRDNVALGARLRG--- 101
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQ-GKPLdyskRGLLALRQQVATVFQdpeqqifYTDIDSDIAFSLRNLGvpe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 102 EKVDRaRVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTV 180
Cdd:PRK13638 111 AEITR-RVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHV 189
|
....*.
gi 488994816 181 VLITHD 186
Cdd:PRK13638 190 IISSHD 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
77-185 |
9.64e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 77 MGQKDLLYPwLSVRDNVALGAR-LRGEKVDRA-RVAALLEQVE-LSSCADARPA----TLSGGMRQRAALARTLYEDRPI 149
Cdd:PTZ00265 1301 VSQEPMLFN-MSIYENIKFGKEdATREDVKRAcKFAAIDEFIEsLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKI 1379
|
90 100 110
....*....|....*....|....*....|....*...
gi 488994816 150 VLMDEPFSALDTLTRTRIQTLAATL--LAGRTVVLITH 185
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAH 1417
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-200 |
1.70e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 1 MTAPGIEVRGLSL---HVG-DRRLFDNLSFTVPGGQWVSLLGASGAGKT----SLLRVMAglAPATC---------GE-V 62
Cdd:PRK15134 1 MTQPLLAIENLSVafrQQQtVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPVVypsgdirfhGEsL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 63 VASDGQPIQG----RLAWMGQKDL--LYPWLSVRDNVALGARL-RGEKVDRARVAAL--LEQVELSSCA---DARPATLS 130
Cdd:PRK15134 79 LHASEQTLRGvrgnKIAMIFQEPMvsLNPLHTLEKQLYEVLSLhRGMRREAARGEILncLDRVGIRQAAkrlTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 131 GGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA--GRTVVLITHDPQEACRLSHRLLVL 200
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-159 |
2.06e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 22 DNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATC--GEVVAsDGQPIQGR----------------LAwmgqkdlL 83
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILF-DGEVCRFKdirdsealgiviihqeLA-------L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 YPWLSVRDNVALG-ARLRGEKVDR----ARVAALLEQVELSSCADARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSA 158
Cdd:NF040905 90 IPYLSIAENIFLGnERAKRGVIDWnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
.
gi 488994816 159 L 159
Cdd:NF040905 170 L 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-201 |
2.21e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 7 EVRGLSLHvgDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVAsDGQPIQGRLAWMGQKDLL--- 83
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL-NGKDISPRSPLDAVKKGMayi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 84 ---------YPWLSVRDNVALG-----ARLRG-----EKVDRARVAAllEQVELSS--CA--DARPATLSGGMRQRAALA 140
Cdd:PRK09700 344 tesrrdngfFPNFSIAQNMAISrslkdGGYKGamglfHEVDEQRTAE--NQRELLAlkCHsvNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994816 141 RTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLL-AGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVCDRIAVFC 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-186 |
2.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 20 LFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgqpiQGRLAWMGQKDLLYPWLSVRDNVALGARL 99
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA----KVRMAVFSQHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 100 RGekVDRARVAALLEQVELSSCADARPA-TLSGGMRQRAALARTLYEDRPIVLMDEPFSALD-TLTRTRIQTLAatLLAG 177
Cdd:PLN03073 600 PG--VPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLV--LFQG 675
|
....*....
gi 488994816 178 rTVVLITHD 186
Cdd:PLN03073 676 -GVLMVSHD 683
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-205 |
3.64e-05 |
|
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: 42.94 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLApatcgevvasdgQPIQGRLAWmgqkdllypwlsvrdnvalgarlrgekvDRARVA 110
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQL------------IPNGDNDEW----------------------------DGITPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 111 ALLEQVELSscadarpatlsGGMRQRAALARTLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLL--AGRTVVLITHDPQ 188
Cdd:cd03222 65 YKPQYIDLS-----------GGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLA 133
|
170
....*....|....*..
gi 488994816 189 EACRLSHRLLVLSAADG 205
Cdd:cd03222 134 VLDYLSDRIHVFEGEPG 150
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-207 |
5.02e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 3 APGIEVRGLSLHVGDRRLFDNLSFTV-PGGQWvSLLGASGAGKTSLLRVMAGLAP-ATCGEVVASDGQPIQGRLAWMGQK 80
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVnPGEHW-QIVGPNGAGKSTLLSLITGDHPqGYSNDLTLFGRRRGSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 81 DLLYPW----------LSVRdNVALGARLRGEKV-----DRARVAAL--LEQVELSSC-ADARPATLSGGmRQRAAL-AR 141
Cdd:PRK10938 337 HIGYVSsslhldyrvsTSVR-NVILSGFFDSIGIyqavsDRQQKLAQqwLDILGIDKRtADAPFHSLSWG-QQRLALiVR 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 142 TLYEDRPIVLMDEPFSALDTLTRTRIQTLAATLLA-GRTVVL-ITHDPQEA--CrLSHRLLVLsaADGDI 207
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLLfVSHHAEDApaC-ITHRLEFV--PDGDI 481
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-199 |
1.58e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 98 RLRGEKVD---RARVAALLEQVELSSCADA-RP-ATLSGGMRQRA------ALARTLYEDRPIVL----MDEPFSALDTL 162
Cdd:TIGR00618 915 RFHGRYADshvNARKYQGLALLVADAYTGSvRPsATLSGGETFLAslslalALADLLSTSGGTVLdslfIDEGFGSLDED 994
|
90 100 110
....*....|....*....|....*....|....*...
gi 488994816 163 TRTR-IQTLAATLLAGRTVVLITHDPQEACRLSHRLLV 199
Cdd:TIGR00618 995 SLDRaIGILDAIREGSKMIGIISHVPEFRERIPHRILV 1032
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
38-205 |
4.38e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.33 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 38 GASGAGKTSLLRVMAGlapATCGEVVASDGQPIQGRLAWMGQKDLlypwlsvrdNVALGARLRGE--KVDRAR------- 108
Cdd:cd03279 35 GPTGAGKSTILDAITY---ALYGKTPRYGRQENLRSVFAPGEDTA---------EVSFTFQLGGKkyRVERSRgldydqf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 109 -VAALLEQVELSSCAdARPA-TLSGGMRQRA------ALARTLYEDRPIVL----MDEPFSALDTLTRTRIQTLAATL-L 175
Cdd:cd03279 103 tRIVLLPQGEFDRFL-ARPVsTLSGGETFLAslslalALSEVLQNRGGARLealfIDEGFGTLDPEALEAVATALELIrT 181
|
170 180 190
....*....|....*....|....*....|
gi 488994816 176 AGRTVVLITHDPQEACRLSHRLLVLSAADG 205
Cdd:cd03279 182 ENRMVGVISHVEELKERIPQRLEVIKTPGG 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-202 |
4.52e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 31 GQWVSLLGASGAGKTSLLRVMAGLAPATCGEV---VASDGQP-------IQGRLAWMGQKDLLYPWLSVRDNVALGARL- 99
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHIGVegvITYDGITpeeikkhYRGDVVYNAETDVHFPHLTVGETLDFAARCk 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 100 ----RGEKVDRARVAALLEQVE-----LSSCADARPAT-----LSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLT-- 163
Cdd:TIGR00956 167 tpqnRPDGVSREEYAKHIADVYmatygLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATal 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488994816 164 ------RTRIQTLAATLLagrtvVLITHDPQEACRLSHRLLVLSA 202
Cdd:TIGR00956 247 efiralKTSANILDTTPL-----VAIYQCSQDAYELFDKVIVLYE 286
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-186 |
4.55e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 16 GDRRLFDNLSFTVPGGQWVSLLGASGAGKTSLLRVMAG-LAPATcGEVVASDGQpiqgRLAWMGQKDLLYpwlsvrdnva 94
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVS-GEIGLAKGI----KLGYFAQHQLEF---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 95 lgarLRGEKVDRARVAALLEQVELSSCAD-------------ARPATLSGGMRQRAALARTLYEDRPIVLMDEPFSALDT 161
Cdd:PRK10636 388 ----LRADESPLQHLARLAPQELEQKLRDylggfgfqgdkvtEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180
....*....|....*....|....*.
gi 488994816 162 LTRtriQTLAATLLAGR-TVVLITHD 186
Cdd:PRK10636 464 DMR---QALTEALIDFEgALVVVSHD 486
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-199 |
6.28e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 21 FDNLSFTVPGGQW-----VSLLGASGAGKTSLLRVMAGLAPATCGEV-----VASDGQPIQGRlawmgqkdllYPwLSVR 90
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkISYKPQYISPD----------YD-GTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 91 DNV--ALGARLRG-----EKVDRARVAALLEQvELSscadarpaTLSGGMRQRAALARTLYEDRPIVLMDEPFSALDTLT 163
Cdd:COG1245 420 EFLrsANTDDFGSsyyktEIIKPLGLEKLLDK-NVK--------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488994816 164 RTR----IQTLAATllAGRTVVLITHDPQEACRLSHRLLV 199
Cdd:COG1245 491 RLAvakaIRRFAEN--RGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-201 |
6.63e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 21 FDNLSFTVPGGQW-----VSLLGASGAGKTSLLRVMAGLAPATCGEVVASDgqpiqgRLAWMGQ----------KDLLYp 85
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL------KISYKPQyikpdydgtvEDLLR- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 86 wlSVRDNVAlGARLRGEKVDRARVAALLEQvELSscadarpaTLSGGMRQRAALARTLYEDRPIVLMDEPFSALD----- 160
Cdd:PRK13409 423 --SITDDLG-SSYYKSEIIKPLQLERLLDK-NVK--------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrl 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488994816 161 TLTRTrIQTLAATllAGRTVVLITHDPQEACRLSHRLLVLS 201
Cdd:PRK13409 491 AVAKA-IRRIAEE--REATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-185 |
2.59e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 24 LSFTVPGGQWVSLLGASGAGKTSLLRVMAGLApATCGEVVASDGQPIQG-------RLAWMGQKDllyPWL---SVRDNV 93
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV-EVCGGEIRVNGREIGAyglrelrRQFSMIPQD---PVLfdgTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994816 94 ALGARLRGEKVDRA--------RVAALLEQVElsSCADARPATLSGGMRQRAALARTLYE-DRPIVLMDEPFSALDTLTR 164
Cdd:PTZ00243 1405 DPFLEASSAEVWAAlelvglreRVASESEGID--SRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALD 1482
|
170 180
....*....|....*....|.
gi 488994816 165 TRIQTLAATLLAGRTVVLITH 185
Cdd:PTZ00243 1483 RQIQATVMSAFSAYTVITIAH 1503
|
|
| |
