|
Name |
Accession |
Description |
Interval |
E-value |
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-208 |
1.20e-109 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 312.88 E-value: 1.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPHLRHIGV 82
Cdd:COG4136 1 MLSLENLTITLGGRPLLApLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDALLFSHLTVAGNIAFAMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTiGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 639318220 162 FSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDAdAANGKLITL 208
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-198 |
3.42e-67 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 209.95 E-value: 3.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLR 78
Cdd:COG3842 2 AMPALELENVSKrYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDS----GRILLDGRDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 HIGVLYQDALLFSHLTVAGNIAFA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAI 156
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGlrMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 639318220 157 LLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEA 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-198 |
3.41e-62 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 193.05 E-value: 3.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQlYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPHLRHIGVLY 84
Cdd:COG3840 2 LRLDDLT-YRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP---DSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 85 QDALLFSHLTVAGNIAFAMPKG---NKKQRlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGlklTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 639318220 162 FSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDA 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-198 |
4.53e-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: 192.35 E-value: 4.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLRHIGV 82
Cdd:cd03259 1 LELKGlSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDS----GEILIDGRDVTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDALLFSHLTVAGNIAFA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 639318220 161 PFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEA 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-198 |
1.06e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 185.35 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNID-NTPPHLRHI 80
Cdd:COG1118 2 SIEVRNISKrFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDS----GRIVLNGRDLFtNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 81 GVLYQDALLFSHLTVAGNIAFAMP--KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRvrPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 159 DEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEA 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-194 |
6.32e-54 |
|
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: 171.89 E-value: 6.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIdnTPPHlRHIGVLYQDALLFSHLTVAGNIA 100
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPTS----GEVLVDGEPV--TGPG-PDRGYVFQQDALLPWLTVLDNVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVF 178
Cdd:cd03293 96 LGleLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELL 175
|
170
....*....|....*.
gi 639318220 179 SQIRDHKLPAIMVTHD 194
Cdd:cd03293 176 DIWRETGKTVLLVTHD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
25-194 |
6.53e-54 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.97 E-value: 6.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHlrhIGVLYQDALLFSHLTVAGNIAFAM 103
Cdd:COG1116 33 TVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTS----GEVLVDGKPVTGPGPD---RGVVFQEPALLPWLTVLDNVALGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 P--KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQI 181
Cdd:COG1116 106 ElrGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLW 185
|
170
....*....|...
gi 639318220 182 RDHKLPAIMVTHD 194
Cdd:COG1116 186 QETGKTVLFVTHD 198
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-198 |
4.65e-51 |
|
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: 164.72 E-value: 4.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLNeqVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGN 98
Cdd:cd03300 19 VSLD--IKEGEFFTLLGPSGCGKTTLLRLIAGfETPTS----GEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTR-E 175
Cdd:cd03300 93 IAFGlrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlE 172
|
170 180
....*....|....*....|...
gi 639318220 176 LVFSQiRDHKLPAIMVTHDHSDA 198
Cdd:cd03300 173 LKRLQ-KELGITFVFVTHDQEEA 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
29-198 |
1.19e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 162.16 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGtL--PSSfkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGNIAFA--MP 104
Cdd:COG3839 29 GEFLVLLGPSGCGKSTLLRMIAG-LedPTS----GEILIGGRDVTDLPPKDRNIAMVFQSYALYPHMTVYENIAFPlkLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 105 KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDH 184
Cdd:COG3839 104 KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRL 183
|
170
....*....|....
gi 639318220 185 KLPAIMVTHDHSDA 198
Cdd:COG3839 184 GTTTIYVTHDQVEA 197
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
14-194 |
8.94e-48 |
|
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: 159.88 E-value: 8.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLP---SSFKANGEVWLNGQNIDNTPPHLRHIGVLYQDALLF 90
Cdd:COG4148 10 RRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERpdsGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIAFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLR 170
Cdd:COG4148 90 PHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180
....*....|....*....|....*..
gi 639318220 171 vdtREL--VFSQIRDH-KLPAIMVTHD 194
Cdd:COG4148 170 ---AEIlpYLERLRDElDIPILYVSHS 193
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-206 |
1.43e-47 |
|
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: 155.96 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLRHIGVL 83
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDS----GKILLNGKDITNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 84 YQDALLFSHLTVAGNIAFAMPK--GNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKrkVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 639318220 162 FSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDADA--------ANGKLI 206
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAladkvaimLNGKLI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
25-201 |
4.22e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 154.18 E-value: 4.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH------LRHIGVLYQDALLFSHLTVAG 97
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILGGLDrPTS----GEVRVDGTDISKLSEKelaafrRRHIGFVFQSFNLLPDLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFAM--PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRE 175
Cdd:cd03255 102 NVELPLllAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVME 181
|
170 180
....*....|....*....|....*.
gi 639318220 176 LVFSQIRDHKLPAIMVTHDHSDADAA 201
Cdd:cd03255 182 LLRELNKEAGTTIVVVTHDPELAEYA 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
25-202 |
4.30e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.43 E-value: 4.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNwLTGTL--PSSfkanGEVWLNGQNIDNTPPH------LRHIGVLYQDALLFSHLTVA 96
Cdd:COG1136 30 SIEAGEFVAIVGPSGSGKSTLLN-ILGGLdrPTS----GEVLIDGQDISSLSERelarlrRRHIGFVFQFFNLLPELTAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 97 GNIAFAM-PKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTR 174
Cdd:COG1136 105 ENVALPLlLAGvSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVL 184
|
170 180
....*....|....*....|....*...
gi 639318220 175 ELVFSQIRDHKLPAIMVTHDHSDADAAN 202
Cdd:COG1136 185 ELLRELNRELGTTIVMVTHDPELAARAD 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-198 |
4.66e-47 |
|
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: 153.99 E-value: 4.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLP---SSFKANGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGNIAFAMPK 105
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKpdgGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 106 GNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHK 185
Cdd:cd03297 103 KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLN 182
|
170
....*....|...
gi 639318220 186 LPAIMVTHDHSDA 198
Cdd:cd03297 183 IPVIFVTHDLSEA 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
13-198 |
1.97e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 153.20 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSH 92
Cdd:PRK10771 9 WLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTP---ASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNIAFAMPKGNK-----KQRLEKIAhalEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDT 167
Cdd:PRK10771 86 LTVAQNIGLGLNPGLKlnaaqREKLHAIA---RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 168 QLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDA 193
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-198 |
1.97e-45 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 154.04 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLR 78
Cdd:TIGR03265 1 SSPYLSIDNiRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGlERQTA----GTIYQGGRDITRLPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 HIGVLYQDALLFSHLTVAGNIAFAMP--KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAI 156
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 639318220 157 LLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEA 198
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-209 |
1.41e-44 |
|
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: 147.70 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLpssFKANGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSH 92
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFI---EPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNIAFAMPKGNKKQRL--EKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLR 170
Cdd:TIGR01277 85 LTVRQNIGLGLHPGLKLNAEqqEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 639318220 171 VDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLITLS 209
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-208 |
2.67e-44 |
|
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: 146.87 E-value: 2.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFS 91
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQS----GRVLINGVDVTAAPPADRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGNIAFAMPKG---NKKQRlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:cd03298 84 HLTVEQNVGLGLSPGlklTAEDR-QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 169 LRVDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-198 |
9.11e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.10 E-value: 9.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFS 91
Cdd:PRK09452 24 FDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPDS----GRIMLDGQDITHVPAENRHVNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGNIAFA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:PRK09452 100 HMTVFENVAFGlrMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190
....*....|....*....|....*....|
gi 639318220 170 RVDTR-ELVFSQiRDHKLPAIMVTHDHSDA 198
Cdd:PRK09452 180 RKQMQnELKALQ-RKLGITFVFVTHDQEEA 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-208 |
3.75e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.80 E-value: 3.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH-LRHIgV 82
Cdd:COG4619 1 LELEGlSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPLSAMPPPeWRRQ-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LY--QDALLFSHlTVAGNIAFAMPKGNKKQRLEKIAHALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLD 159
Cdd:COG4619 77 AYvpQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 639318220 160 EPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-206 |
5.23e-43 |
|
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: 144.35 E-value: 5.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH-----LRHIGVLYQDALLFSHLTVAGNI 99
Cdd:COG1127 28 VPRGEILAIIGGSGSGKSVLLKLIIGLLrPDS----GEILVDGQDITGLSEKelyelRRRIGMLFQGGALFDSLTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAM---PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD--TQLRVDtr 174
Cdd:COG1127 104 AFPLrehTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpiTSAVID-- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 175 ELVFSQIRDHKLPAIMVTHDHSDADA--------ANGKLI 206
Cdd:COG1127 182 ELIRELRDELGLTSVVVTHDLDSAFAiadrvavlADGKII 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-210 |
3.00e-42 |
|
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: 140.40 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNID----NTPPHLRH 79
Cdd:cd03229 1 LELKNvSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD---SGSILIDGEDLTdledELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 IGVLYQDALLFSHLTVAGNIAFAmpkgnkkqrlekiahaleqvglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLD 159
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 639318220 160 EPFSKLDTQLRVDTRELVfSQIRD-HKLPAIMVTHDHSDADAANGKLITLSS 210
Cdd:cd03229 126 EPTSALDPITRREVRALL-KSLQAqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-208 |
3.55e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTP----PHLR-HIGVLYQ 85
Cdd:COG2884 11 YPGGREALSdVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErPTS----GQVLVNGQDLSRLKrreiPYLRrRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 86 DALLFSHLTVAGNIAFAM-----PKGNKKQRlekIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:COG2884 87 DFRLLPDRTVYENVALPLrvtgkSRKEIRRR---VREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 639318220 161 PFSKLDTQLRVDTRELvFSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:COG2884 164 PTGNLDPETSWEIMEL-LEEINRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
22-206 |
5.04e-42 |
|
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: 141.87 E-value: 5.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH-----LRHIGVLYQDALLFSHLTV 95
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDS----GEVLIDGEDISGLSEAelyrlRRRMGMLFQSGALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGNIAFAM---PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD--TQLR 170
Cdd:cd03261 95 FENVAFPLrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiASGV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 639318220 171 VDtrELVFSQIRDHKLPAIMVTHDHSDADA--------ANGKLI 206
Cdd:cd03261 175 ID--DLIRSLKKELGLTSIMVTHDLDTAFAiadriavlYDGKIV 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-209 |
1.62e-41 |
|
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: 143.02 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 34 IMGPSGSGKSSLLNWLTGTLPSSFkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGNIAFA--MPKGNKKQR 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS---GSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGlkMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 112 LEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTR-ELVFSQiRDHKLPAIM 190
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlELKTIQ-EQLGITFVF 156
|
170
....*....|....*....
gi 639318220 191 VTHDHSDADAANGKLITLS 209
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMR 175
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-194 |
5.72e-41 |
|
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: 138.43 E-value: 5.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQ-LYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTGtlPSSfkanGEVWLNGQNIDNTPPHL--- 77
Cdd:cd03262 1 IEIKNLHkSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrciNLLEE--PDS----GTIIIDGLKLTDDKKNInel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 -RHIGVLYQDALLFSHLTVAGNIAFAMPKGNKKQRLEKIAHA---LEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEP 153
Cdd:cd03262 75 rQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERAlelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 154 KAILLDEPFSKLDTQLrvdTREL--VFSQIRDHKLPAIMVTHD 194
Cdd:cd03262 155 KVMLFDEPTSALDPEL---VGEVldVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-200 |
8.90e-41 |
|
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: 137.98 E-value: 8.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH--LRHIGVLYQDA-LLFSHLTVAGNIAF 101
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDLTKLSLKelRRKVGLVFQNPdDQFFGPTVEEEVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 AMP--KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVfS 179
Cdd:cd03225 100 GLEnlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELL-K 178
|
170 180
....*....|....*....|.
gi 639318220 180 QIRDHKLPAIMVTHDHSDADA 200
Cdd:cd03225 179 KLKAEGKTIIIVTHDLDLLLE 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-198 |
5.75e-40 |
|
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: 136.70 E-value: 5.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGtLPSSfkANGEVWLNGQNIDNTPPHLRHIGV 82
Cdd:cd03296 2 SIEVRNvSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERP--DSGTILFGGEDATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDALLFSHLTVAGNIAFAMPKGNKKQRL------EKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAI 156
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPpeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 157 LLDEPFSKLDTQLRVDTRELVfSQIRDH-KLPAIMVTHDHSDA 198
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWL-RRLHDElHVTTVFVTHDQEEA 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-198 |
2.24e-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: 134.30 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRHIGVL 83
Cdd:cd03301 1 VELENvTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT---SGRIYIGGRDVTDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 84 YQDALLFSHLTVAGNIAFA-----MPKGNKKQRLEKIAHALeqvGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGlklrkVPKDEIDERVREVAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639318220 159 DEPFSKLDTQLRVDTR-ELVFSQiRDHKLPAIMVTHDHSDA 198
Cdd:cd03301 155 DEPLSNLDAKLRVQMRaELKRLQ-QRLGTTTIYVTHDQVEA 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-194 |
4.90e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.97 E-value: 4.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTgtLPSSfkanGEVWLNGQNIDNTPPHL--- 77
Cdd:COG1126 2 IEIENlHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLrciNLLE--EPDS----GTITVDGEDLTDSKKDInkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 -RHIGVLYQDALLFSHLTVAGNIAFAmP---KGNKKQRLEKIAHA-LEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSE 152
Cdd:COG1126 76 rRKVGMVFQQFNLFPHLTVLENVTLA-PikvKKMSKAEAEERAMElLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 639318220 153 PKAILLDEPFSKLDTQLrvdTRElVFSQIRDhkLPA-----IMVTHD 194
Cdd:COG1126 155 PKVMLFDEPTSALDPEL---VGE-VLDVMRD--LAKegmtmVVVTHE 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-201 |
6.85e-39 |
|
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: 132.99 E-value: 6.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR-HIGV 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSgLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS---AGEVLWNGEPIRDAREDYRrRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDALLFSHLTVAGNIAFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 639318220 163 SKLDTQlrvdTRELVFSQIRDHKLP---AIMVTHDHSDADAA 201
Cdd:COG4133 160 TALDAA----GVALLAELIAAHLARggaVLLTTHQPLELAAA 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-206 |
1.55e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.88 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLneQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLR-HIGVLYQDALLFSHLTVAG 97
Cdd:COG1131 19 VSL--TVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTS----GEVRVLGEDVARDPAEVRrRIGYVPQEPALYPDLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFA-----MPKGNKKQRlekIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVD 172
Cdd:COG1131 93 NLRFFarlygLPRKEARER---IDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 639318220 173 TRELVfSQIRDHKLPAIMVTHDHSDADA--------ANGKLI 206
Cdd:COG1131 170 LWELL-RELAAEGKTVLLSTHYLEEAERlcdrvaiiDKGRIV 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-198 |
2.90e-38 |
|
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: 133.15 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPP----HLR--HIGVLYQDALLFSHLTVAGN 98
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIePTS----GKVLIDGQDIAAMSRkelrELRrkKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFAMP-KG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTREL 176
Cdd:cd03294 123 VAFGLEvQGvPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180
....*....|....*....|..
gi 639318220 177 VFSQIRDHKLPAIMVTHDHSDA 198
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEA 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-208 |
5.99e-38 |
|
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: 130.61 E-value: 5.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTP----PHLR-HIGVLYQDALLFSH 92
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTS----GTIRVNGQDVSDLRgraiPYLRrKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNIAFAMPKGNKKQRL--EKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlr 170
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREirKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 171 vDTRELV--FSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:cd03292 171 -TTWEIMnlLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-194 |
1.23e-37 |
|
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: 136.57 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL---YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPHL 77
Cdd:COG1123 1 MTPLLEVRDLSVrypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 R--HIGVLYQDALL-FSHLTVAGNIAFAMPKGN--KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSE 152
Cdd:COG1123 81 RgrRIGMVFQDPMTqLNPVTVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 639318220 153 PKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHD 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-205 |
2.09e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.42 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGNIAFA-- 102
Cdd:PRK11607 42 IYKGEIFALLGASGCGKSTLLRMLAGfEQPTA----GQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGlk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 103 ---MPKGNKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFS 179
Cdd:PRK11607 118 qdkLPKAEIASRVNEM---LGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVD 194
|
170 180
....*....|....*....|....*.
gi 639318220 180 QIRDHKLPAIMVTHDHSDADAANGKL 205
Cdd:PRK11607 195 ILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-163 |
1.15e-36 |
|
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: 125.45 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFSHLTVAGNI 99
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDN----LSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:pfam00005 81 RLGllLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-198 |
1.40e-36 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 130.97 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLNeqVNGGEILTIMGPSGSGKSSLLNWLTGtLPSsfKANGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGNI 99
Cdd:PRK10851 21 ISLD--IPSGQMVALLGPSGSGKTTLLRIIAG-LEH--QTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAMPKGNKKQRL------EKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDT 173
Cdd:PRK10851 96 AFGLTVLPRRERPnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180
....*....|....*....|....*
gi 639318220 174 RELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:PRK10851 176 RRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-194 |
1.97e-36 |
|
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: 127.55 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLR-HIGVL--YQDALLFSHLTVAGNIA 100
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTS----GSVLFDGEDITGLPPHEIaRLGIGrtFQIPRLFPELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 ------------FAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:cd03219 98 vaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180
....*....|....*....|....*.
gi 639318220 169 LRVDTRELVfSQIRDHKLPAIMVTHD 194
Cdd:cd03219 178 ETEELAELI-RELRERGITVLLVEHD 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
14-194 |
9.50e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 128.69 E-value: 9.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSS--FKANGEVWLNGQNIDNTPPHLRHIGVLYQDALLF 90
Cdd:TIGR02142 8 RLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGlTRPDEgeIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIAFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLR 170
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180
....*....|....*....|....*..
gi 639318220 171 vdtRELV--FSQIRDH-KLPAIMVTHD 194
Cdd:TIGR02142 168 ---YEILpyLERLHAEfGIPILYVSHS 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-194 |
1.27e-35 |
|
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: 130.79 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTP-----PHLRHIGVLYQD--ALLFSHLTVAGNIA 100
Cdd:COG1123 291 GETLGLVGESGSGKSTLARLLLGLLrPTS----GSILFDGKDLTKLSrrslrELRRRVQMVFQDpySSLNPRMTVGDIIA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FAM---PKGNKKQRLEKIAHALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTREL 176
Cdd:COG1123 367 EPLrlhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQ 442
|
170 180
....*....|....*....|..
gi 639318220 177 VFSQIRD----HKLPAIMVTHD 194
Cdd:COG1123 443 ILNLLRDlqreLGLTYLFISHD 464
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
25-198 |
1.38e-35 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 125.14 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH--LRHIGVLYQ--DALLFShLTVAGNI 99
Cdd:COG1122 23 SIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTS----GEVLVDGKDITKKNLRelRRKVGLVFQnpDDQLFA-PTVEEDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAmPKgN----KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvdTRE 175
Cdd:COG1122 98 AFG-PE-NlglpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR----GRR 171
|
170 180
....*....|....*....|....*...
gi 639318220 176 LVFSQIRdhKLPA-----IMVTHDHSDA 198
Cdd:COG1122 172 ELLELLK--RLNKegktvIIVTHDLDLV 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-198 |
2.06e-35 |
|
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: 125.11 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 21 SLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPP-HLR-HIGVLYQDALLFSHLTVAG 97
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTS----GEIFIDGEDIREQDPvELRrKIGYVIQQIGLFPHMTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAfAMPKGNK---KQRLEKIAHALEQVGL--KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVD 172
Cdd:cd03295 95 NIA-LVPKLLKwpkEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQ 173
|
170 180
....*....|....*....|....*.
gi 639318220 173 TRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:cd03295 174 LQEEFKRLQQELGKTIVFVTHDIDEA 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-198 |
3.34e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.45 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 3 SSLQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG--TLPSsfkanGEVWLNGQNIDNTPPHLRH 79
Cdd:PRK11000 2 ASVTLRNvTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDITS-----GDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 IGVLYQDALLFSHLTVAGNIAFAM--PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAIL 157
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLklAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639318220 158 LDEPFSKLDTQLRVDTRelvfSQI-RDHK-LPAIM--VTHDHSDA 198
Cdd:PRK11000 157 LDEPLSNLDAALRVQMR----IEIsRLHKrLGRTMiyVTHDQVEA 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-194 |
4.53e-35 |
|
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: 123.44 E-value: 4.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG--TLPSSFKANGEVWLNGQNI---DNTPPHLR-HIGVLYQD 86
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDIydlDVDVLELRrRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 87 ALLFsHLTVAGNIAFAMP---KGNKKQRLEKIAHALEQVGLKDMGNR--HPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:cd03260 90 PNPF-PGSIYDNVAYGLRlhgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190
....*....|....*....|....*....|....*
gi 639318220 162 FSKLDtqlRVDTR--ELVFSQIRDhKLPAIMVTHD 194
Cdd:cd03260 169 TSALD---PISTAkiEELIAELKK-EYTIVIVTHN 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-194 |
1.68e-34 |
|
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: 122.84 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPP-HL-RHIGVLYQDALLF 90
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRrELaRRIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIAFA-MP-----KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSK 164
Cdd:COG1120 88 FGLTVRELVALGrYPhlglfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190
....*....|....*....|....*....|
gi 639318220 165 LDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:COG1120 168 LDLAHQLEVLELLRRLARERGRTVVMVLHD 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-208 |
3.33e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.45 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 2 QSSLQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRH 79
Cdd:PRK11432 4 KNFVVLKNiTKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTE----GQIFIDGEDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 IGVLYQDALLFSHLTVAGNIAFA--MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAIL 157
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 158 LDEPFSKLDTQLRVDTRElvfsQIRDHK----LPAIMVTHDHSDADAANGKLITL 208
Cdd:PRK11432 160 FDEPLSNLDANLRRSMRE----KIRELQqqfnITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-194 |
5.06e-34 |
|
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: 121.45 E-value: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFkanGEVWLNGQNIDNTPP--HLRHIGVLYQDALLFSH--LTVAGNIA 100
Cdd:COG1124 27 EVAPGESFGLVGESGSGKSTLLRALAGLERPWS---GEVTFDGRPVTRRRRkaFRRRVQMVFQDPYASLHprHTVDRILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FAMPKGNKKQRLEKIAHALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFS 179
Cdd:COG1124 104 EPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKD 183
|
170
....*....|....*
gi 639318220 180 QIRDHKLPAIMVTHD 194
Cdd:COG1124 184 LREERGLTYLFVSHD 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-194 |
3.02e-33 |
|
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: 118.40 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPphlRHIGVLYQ--DALLF 90
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK---PTSGSIRVFGKPLEKER---KRIGYVPQrrSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVA-----GNIAFA-MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSK 164
Cdd:cd03235 83 FPISVRdvvlmGLYGHKgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190
....*....|....*....|....*....|
gi 639318220 165 LDTQLRVDTRELVfSQIRDHKLPAIMVTHD 194
Cdd:cd03235 163 VDPKTQEDIYELL-RELRREGMTILVVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-194 |
3.67e-33 |
|
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: 119.21 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL-----RHIGVLYQDALLFSHL 93
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAF----------AMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:cd03256 94 SVLENVLSgrlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 164 KLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:cd03256 174 SLDPASSRQVMDLLKRINREEGITVIVSLHQ 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-194 |
4.45e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 119.37 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLR-HIGVL--YQDALLFSHLTVAGNIA 100
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGFYrPTS----GRILFDGRDITGLPPHRIaRLGIArtFQNPRLFPELTVLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FAM-----------------PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:COG0411 102 VAAharlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAA 181
|
170 180 190
....*....|....*....|....*....|..
gi 639318220 164 KLDTQLRVDTRELVFsQIRD-HKLPAIMVTHD 194
Cdd:COG0411 182 GLNPEETEELAELIR-RLRDeRGITILLIEHD 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-168 |
4.69e-33 |
|
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: 118.45 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPP-HLR----HIGVLYQDALLFSHLTVAGNI 99
Cdd:cd03258 28 VPKGEIFGIIGRSGAGKSTLIRCINGlERPTS----GSVLVDGTDLTLLSGkELRkarrRIGMIFQHFNLLSSRTVFENV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639318220 100 AFAMPKGN--KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:cd03258 104 ALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-194 |
1.57e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 118.04 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 3 SSLQIKNCQL----YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDnTPPH 76
Cdd:COG4525 2 SMLTVRHVSVrypgGGQPQPALQdVSLTIESGEFVVALGASGCGKTTLLNLIAGFLaPSS----GEITLDGVPVT-GPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 LRhiGVLYQDALLFSHLTVAGNIAFAMP-KG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPK 154
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRlRGvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 155 AILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-194 |
3.18e-32 |
|
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: 114.84 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH--LRHIGVLYQdallf 90
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKelARKIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 shltvagniafampkgnkkqrlekiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD--TQ 168
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiaHQ 133
|
170 180
....*....|....*....|....*.
gi 639318220 169 LRVDtrELVFSQIRDHKLPAIMVTHD 194
Cdd:cd03214 134 IELL--ELLRRLARERGKTVVMVLHD 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-201 |
4.19e-32 |
|
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: 121.80 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLneQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDN-TPPHLR-HIGVLYQDALLFSHlTVAG 97
Cdd:COG4987 354 LSL--TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDLRDlDEDDLRrRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:COG4987 428 NLRLARPDATD----EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
170 180 190
....*....|....*....|....*....|....*
gi 639318220 167 TQLRVDTRELVFSQIRDHKLpaIMVTHDHSDADAA 201
Cdd:COG4987 504 AATEQALLADLLEALAGRTV--LLITHRLAGLERM 536
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-206 |
4.82e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 121.40 E-value: 4.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 2 QSSLQIKNCQL-YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH--L 77
Cdd:COG4988 334 PPSIELEDVSFsYPGGRPALDgLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILINGVDLSDLDPAswR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 RHIGVLYQDALLFsHLTVAGNIAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALL 146
Cdd:COG4988 411 RQIAWVPQNPYLF-AGTIRENLRLGRPDASD----EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 147 RMLLSEPKAILLDEPFSKLDtqlrVDTRELVFSQIRD---HKLpAIMVTHDHSDADAA-------NGKLI 206
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLD----AETEAEILQALRRlakGRT-VILITHRLALLAQAdrilvldDGRIV 550
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-198 |
5.52e-32 |
|
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: 115.64 E-value: 5.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRhigVLYQDALLFSHLTVAG 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTS----GGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFA----MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDT 173
Cdd:TIGR01184 74 NIALAvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|....*
gi 639318220 174 RELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
25-194 |
9.42e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 115.54 E-value: 9.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPP-----HLRHIGVLYQDALLFSHLTVAGNI 99
Cdd:COG3638 25 EIERGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGEILVDGQDVTALRGralrrLRRRIGMIFQQFNLVPRLSVLTNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 ----------AFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:COG3638 102 lagrlgrtstWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKT 181
|
170 180
....*....|....*....|....*
gi 639318220 170 RVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:COG3638 182 ARQVMDLLRRIAREDGITVVVNLHQ 206
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
14-202 |
1.43e-31 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 114.35 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNwLTGTLPSSFKANGEVW---LNGQNIDNTPPHLRHIGVLYQDALLF 90
Cdd:TIGR02982 16 LRKQVLFDINLEINPGEIVILTGPSGSGKTTLLT-LIGGLRSVQEGSLKVLgqeLHGASKKQLVQLRRRIGYIFQAHNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIAFAM---PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDT 167
Cdd:TIGR02982 95 GFLTARQNVQMALelqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDS 174
|
170 180 190
....*....|....*....|....*....|....*
gi 639318220 168 QLRVDTRELVFSQIRDHKLPAIMVTHDHSDADAAN 202
Cdd:TIGR02982 175 KSGRDVVELMQKLAKEQGCTILMVTHDNRILDVAD 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-206 |
2.02e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTgTLPSsfkanGEVWLNGQNIDNTPPHLRHI----GVLYQ 85
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLE-EITS-----GDLIVDGLKVNDPKVDERLIrqeaGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 86 DALLFSHLTVAGNIAFAmP---KGNKKQRLEKIAHAL-EQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK09493 85 QFYLFPHLTALENVMFG-PlrvRGASKEEAEKQARELlAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639318220 162 FSKLDTQLRVDTRElVFSQIRDHKLPAIMVTHDHSDADAANGKLI 206
Cdd:PRK09493 164 TSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-199 |
4.33e-31 |
|
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: 119.55 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPP-HLR-HIGVLYQDALLFSHlTVAGNIAFA 102
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLGLYePTS----GRILIDGIDLRQIDPaSLRrQIGVVLQDVFLFSG-TIRENITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 103 MPKGNkkqrLEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrv 171
Cdd:COG2274 573 DPDAT----DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAE--- 645
|
170 180 190
....*....|....*....|....*....|...
gi 639318220 172 dTRELVFSQIRDHKLPA--IMVTHDHS---DAD 199
Cdd:COG2274 646 -TEAIILENLRRLLKGRtvIIIAHRLStirLAD 677
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-194 |
6.34e-31 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 115.71 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTG--TLPSsfkanGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSHLTVAGNIAFA---- 102
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAGleRITS-----GEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVRENMAYGlkir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 103 -MPKGNKKQRLEKIAHALEqvgLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRelvfSQI 181
Cdd:PRK11650 105 gMPKAEIEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR----LEI 177
|
170
....*....|....*..
gi 639318220 182 RD-H---KLPAIMVTHD 194
Cdd:PRK11650 178 QRlHrrlKTTSLYVTHD 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-212 |
2.68e-30 |
|
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: 111.06 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELL----LSLNeqVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLR 78
Cdd:cd03263 1 LQIRNlTKTYKKGTKPavddLSLN--VYKGEIFGLLGHNGAGKTTTLKMLTGELrPTS----GTAYINGYSIRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 -HIGVLYQDALLFSHLTVAGNIAF-AMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKA 155
Cdd:cd03263 75 qSLGYCPQFDALFDELTVREHLRFyARLKGlPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 156 ILLDEPFSKLDTQlrvdTRELVFSQIRD--HKLPAIMVTHDHSDADA--------ANGKLITLSSAL 212
Cdd:cd03263 155 LLLDEPTSGLDPA----SRRAIWDLILEvrKGRSIILTTHSMDEAEAlcdriaimSDGKLRCIGSPQ 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
25-168 |
3.47e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 113.63 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGtL--PSSfkanGEVWLNGQNIDNTPPH-LR----HIGVLYQDALLFSHLTVAG 97
Cdd:COG1135 27 TIEKGEIFGIIGYSGAGKSTLIRCINL-LerPTS----GSVLVDGVDLTALSEReLRaarrKIGMIFQHFNLLSSRTVAE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 98 NIAFAM--PKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:COG1135 102 NVALPLeiAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-206 |
3.66e-30 |
|
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: 111.49 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR-HIGVLYQDALLFS 91
Cdd:COG4555 11 YGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGEDVRKEPREARrQIGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGNIA-FAMPKGNKKQRLE-KIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtql 169
Cdd:COG4555 88 RLTVRENIRyFAELYGLFDEELKkRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD--- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 639318220 170 rVDTRELVFSQIRDHKLPAIMV---THDHSDADA--------ANGKLI 206
Cdd:COG4555 165 -VMARRLLREILRALKKEGKTVlfsSHIMQEVEAlcdrvvilHKGKVV 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
25-194 |
4.03e-30 |
|
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: 110.67 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPHLR-----HIGVLYQDAL--LFSHLTVAG 97
Cdd:cd03257 27 SIKKGETLGLVGESGSGKSTLARAILGLLK---PTSGSIIFDGKDLLKLSRRLRkirrkEIQMVFQDPMssLNPRMTIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFAM----PKGNKKQRLEKIAHALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVD 172
Cdd:cd03257 104 QIAEPLrihgKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170 180
....*....|....*....|...
gi 639318220 173 TRELvFSQIRD-HKLPAIMVTHD 194
Cdd:cd03257 184 ILDL-LKKLQEeLGLTLLFITHD 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-194 |
6.88e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 6.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNtppHLRH 79
Cdd:COG1121 3 MMPAIELENLTVsYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP---PTSGTVRLFGKPPRR---ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 IGVLYQDALLFSH--LTVA--------GNIAFaMPKGNKKQRlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRML 149
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRdvvlmgryGRRGL-FRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 639318220 150 LSEPKAILLDEPFSKLDTQlrvdTRELVFS---QIRDHKLPAIMVTHD 194
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAA----TEEALYEllrELRREGKTILVVTHD 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
25-199 |
1.02e-29 |
|
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: 109.83 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNtpphL----------RHIGVLYQDALLFSHL 93
Cdd:COG4181 34 EVEAGESVAIVGASGSGKSTLLGLLAGlDRPTS----GTVRLAGQDLFA----LdedararlraRHVGFVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDT 173
Cdd:COG4181 106 TALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI 185
|
170 180
....*....|....*....|....*.
gi 639318220 174 RELVFSQIRDHKLPAIMVTHDHSDAD 199
Cdd:COG4181 186 IDLLFELNRERGTTLVLVTHDPALAA 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-202 |
2.07e-29 |
|
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: 107.47 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFS 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLRDLDLESlrKNIAYVPQDPFLFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 hLTVAGNIafampkgnkkqrlekiahaleqvglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrv 171
Cdd:cd03228 90 -GTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE--- 130
|
170 180 190
....*....|....*....|....*....|...
gi 639318220 172 dTRELVFSQIRDHKLP--AIMVTHDHSDADAAN 202
Cdd:cd03228 131 -TEALILEALRALAKGktVIVIAHRLSTIRDAD 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-209 |
2.54e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNtPPHLRhiGVLYQDALLFSHLTVAGN 98
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEG-PGAER--GVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFAMPKG--NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTREL 176
Cdd:PRK11248 91 VAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170 180 190
....*....|....*....|....*....|...
gi 639318220 177 VFSQIRDHKLPAIMVTHDHSDADAANGKLITLS 209
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDIEEAVFMATELVLLS 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-198 |
4.38e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLY------RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR 78
Cdd:COG1101 2 LELKNLSKTfnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD---SGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 --HIGVLYQDALL--FSHLTVAGNIAFAMPKGNK--------KQRLEKIAHALEQVGLkDMGNRHPD---NLSGGQ-QAr 142
Cdd:COG1101 79 akYIGRVFQDPMMgtAPSMTIEENLALAYRRGKRrglrrgltKKRRELFRELLATLGL-GLENRLDTkvgLLSGGQrQA- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 143 VALLRMLLSEPKAILLDEPFSKLD-------TQLrvdTRELVfsqiRDHKLPAIMVTHDHSDA 198
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDpktaalvLEL---TEKIV----EENNLTTLMVTHNMEQA 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-193 |
5.84e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 110.73 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNG-------QNIdNTPPHLRHIGVLYQ 85
Cdd:PRK11144 9 QLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGlTRPQK----GRIVLNGrvlfdaeKGI-CLPPEKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 86 DALLFSHLTVAGNIAFAMPKGNKKQrLEKIAHALeqvGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:PRK11144 84 DARLFPHYKVRGNLRYGMAKSMVAQ-FDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 166 DTQLRvdtRELV-FSQ--IRDHKLPAIMVTH 193
Cdd:PRK11144 160 DLPRK---RELLpYLErlAREINIPILYVSH 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-166 |
1.04e-28 |
|
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: 106.97 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 2 QSSLQIKNCQLYRQNE-----LLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDntpPH 76
Cdd:cd03234 1 QRVLPWWDVGLKAKNWnkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRK---PD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 L--RHIGVLYQDALLFSHLTVAGNIAFA--------MPKGNKKQRLEKIahALEQVGLKDMGNRHPDNLSGGQQARVALL 146
Cdd:cd03234 78 QfqKCVAYVRQDDILLPGLTVRETLTYTailrlprkSSDAIRKKRVEDV--LLRDLALTRIGGNLVKGISGGERRRVSIA 155
|
170 180
....*....|....*....|
gi 639318220 147 RMLLSEPKAILLDEPFSKLD 166
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-166 |
4.86e-28 |
|
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: 105.70 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLRH---IGVLYQDALLFSHLTVAGNI- 99
Cdd:cd03218 22 SVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPDS----GKILLDGQDITKLPMHKRArlgIGYLPQEASIFRKLTVEENIl 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639318220 100 -AFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:cd03218 98 aVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-199 |
7.19e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 103.25 E-value: 7.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLR-HIGVLYQDALLF 90
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDS----GEIKVLGKDIKKEPEEVKrRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIafampkgnkkqrlekiahaleqvglkdmgnrhpdNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLR 170
Cdd:cd03230 86 ENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180
....*....|....*....|....*....
gi 639318220 171 VDTRELVfSQIRDHKLPAIMVTHDHSDAD 199
Cdd:cd03230 132 REFWELL-RELKKEGKTILLSSHILEEAE 159
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-162 |
9.53e-28 |
|
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: 104.44 E-value: 9.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR-HIGV 82
Cdd:cd03224 1 LEVENlNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR---SGSIRFDGRDITGLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LY--QDALLFSHLTVAGNI---AFAMPKGNKKQRLEKIAHALEQvgLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAIL 157
Cdd:cd03224 78 GYvpEGRRIFPELTVEENLllgAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
....*
gi 639318220 158 LDEPF 162
Cdd:cd03224 156 LDEPS 160
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-161 |
1.08e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.53 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR-HIGV 82
Cdd:TIGR03410 1 LEVSNlNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK---SGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LY--QDALLFSHLTVAGNI--AFAMPKGNKKQRLEKIaHALEQVgLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:TIGR03410 78 AYvpQGREIFPRLTVEENLltGLAALPRRSRKIPDEI-YELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
...
gi 639318220 159 DEP 161
Cdd:TIGR03410 156 DEP 158
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-208 |
1.37e-27 |
|
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: 102.32 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 6 QIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL--RHIGV 82
Cdd:cd00267 1 EIENLSFrYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPLEElrRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQdallfshltvagniafampkgnkkqrlekiahaleqvglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:cd00267 78 VPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 639318220 163 SKLDTQLRVDTRELVfSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:cd00267 109 SGLDPASRERLLELL-RELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-194 |
1.46e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL--RHI 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDdVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPLADWSPAElaRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 81 GVLYQDALL-FShLTVAGNIAF-AMPKGNKKQRLEKI-AHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLL------S 151
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMgRAPHGLSRAEDDALvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 152 EPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-198 |
4.05e-27 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 104.07 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPP----HLRH-IGVLYQ--DALLFShLTVAGNIA 100
Cdd:TIGR04521 31 GEFVAIIGHTGSGKSTLIQHLNGLLkPTS----GTVTIDGRDITAKKKkklkDLRKkVGLVFQfpEHQLFE-ETVYKDIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FAmPK--GNKKQRLEKIAH-ALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvdTREL 176
Cdd:TIGR04521 106 FG-PKnlGLSEEEAEERVKeALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK----GRKE 180
|
170 180
....*....|....*....|....*.
gi 639318220 177 VFSQIRD----HKLPAIMVTHDHSDA 198
Cdd:TIGR04521 181 ILDLFKRlhkeKGLTVILVTHSMEDV 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-194 |
9.07e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTgtLPSSfkanGEVWLNGQNID-NTPPH-- 76
Cdd:COG4161 2 SIQLKNiNCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLE--TPDS----GQLNIAGHQFDfSQKPSek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 ----LRH-IGVLYQDALLFSHLTVAGNIAFA---MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRM 148
Cdd:COG4161 76 airlLRQkVGMVFQQYNLWPHLTVMENLIEApckVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 639318220 149 LLSEPKAILLDEPFSKLDTQLrvdTRELVfSQIRDHKLPAI---MVTHD 194
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEI---TAQVV-EIIRELSQTGItqvIVTHE 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-168 |
9.59e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH-LR-HIGVLYQDAL 88
Cdd:COG1132 349 YPGDRPVLKdISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTS----GRILIDGVDIRDLTLEsLRrQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 89 LFsHLTVAGNIAFampkGNKKQRLEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAIL 157
Cdd:COG1132 425 LF-SGTIRENIRY----GRPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILI 499
|
170
....*....|.
gi 639318220 158 LDEPFSKLDTQ 168
Cdd:COG1132 500 LDEATSALDTE 510
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-202 |
3.93e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.98 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 3 SSLQIKN-CQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTgtLPSSfkanGEVWLNGQNIDNTPP--- 75
Cdd:PRK11264 2 SAIEVKNlVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLE--QPEA----GTIRVGDITIDTARSlsq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 76 ------HLR-HIGVLYQDALLFSHLTVAGNI--AFAMPKGNKKQRLEKIAHAL-EQVGLKDMGNRHPDNLSGGQQARVAL 145
Cdd:PRK11264 76 qkglirQLRqHVGFVFQNFNLFPHRTVLENIieGPVIVKGEPKEEATARARELlAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639318220 146 LRMLLSEPKAILLDEPFSKLDTQLRVDtrelVFSQIR---DHKLPAIMVTHDHSDA-DAAN 202
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGE----VLNTIRqlaQEKRTMVIVTHEMSFArDVAD 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-194 |
6.36e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.42 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLtGTL--PSSfkanGEVWLNGQNI----DNTPPHLR--HIGVLYQD 86
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLdkPTS----GTYRVAGQDVatldADALAQLRreHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 87 ALLFSHLTVAGNIAF-AMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSK 164
Cdd:PRK10535 95 YHLLSHLTAAQNVEVpAVYAGlERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190
....*....|....*....|....*....|
gi 639318220 165 LDTQLRVDTRElVFSQIRDHKLPAIMVTHD 194
Cdd:PRK10535 175 LDSHSGEEVMA-ILHQLRDRGHTVIIVTHD 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-200 |
1.05e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.14 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVwLNGqnidNTPPH--LRHIGVLYQDALL 89
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSA----GEL-LAG----TAPLAeaREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHLTVAGNIAFAMpKGNKKQRLEKiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:PRK11247 93 LPWKKVIDNVGLGL-KGQWRDAALQ---ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 170 RVDTRELVFSQIRDHKLPAIMVTHDHSDADA 200
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHDVSEAVA 199
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-196 |
2.02e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNE---QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHL--RHiGVL--YQDALLF 90
Cdd:PRK11300 18 LLAVNNvnlEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG----GTILLRGQHIEGLPGHQiaRM-GVVrtFQHVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIA---------------FAMPKGNKKQR--LEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEP 153
Cdd:PRK11300 93 REMTVIENLLvaqhqqlktglfsglLKTPAFRRAESeaLDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 154 KAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHS 196
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMK 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-209 |
2.51e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 97.57 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIdntpphlRHIGVLYQDALLF--------SHL 93
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP---DAGEVLWQGEPI-------RRQRDEYHQDLLYlghqpgikTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAMPKGNKkQRLEKIAHALEQVGLK---DMGNRHpdnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlR 170
Cdd:PRK13538 90 TALENLRFYQRLHGP-GDDEALWEALAQVGLAgfeDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-G 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 639318220 171 VDTRELVFSQIRDHKLPAIMVThdHSDADAANGKLITLS 209
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTT--HQDLPVASDKVRKLR 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-208 |
7.24e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.48 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPHLR--HIGvlYQDALL 89
Cdd:PRK13539 11 VRGGRVLFSgLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP---PAAGTIKLDGGDIDDPDVAEAchYLG--HRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 fSHLTVAGNIAF-AMPKGnkkQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtq 168
Cdd:PRK13539 86 -PALTVAENLEFwAAFLG---GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639318220 169 lrVDTRELVFSQIRDH-KLPAIMVTHDHSDADAANGKLITL 208
Cdd:PRK13539 160 --AAAVALFAELIRAHlAQGGIVIAATHIPLGLPGARELDL 198
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
23-166 |
7.58e-25 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 97.37 E-value: 7.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 23 NEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH-----LRHIGVLYQDALLFSHLTVA 96
Cdd:TIGR02315 22 NLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSS----GSILLEGTDITKLRGKklrklRRRIGMIFQHYNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 97 GN--------------IAFAMPKGNKKQRLEkiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:TIGR02315 98 ENvlhgrlgykptwrsLLGRFSEEDKERALS----ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
....
gi 639318220 163 SKLD 166
Cdd:TIGR02315 174 ASLD 177
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-193 |
2.40e-24 |
|
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: 95.73 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFS 91
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTS----GSVLLDGTDIRQLDPADlrRNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HlTVAGNIAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:cd03245 92 G-TLRDNITLGAPLADD----ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190
....*....|....*....|....*....|....*
gi 639318220 161 PFSKLDTQlrvdTRELVFSQIRDHKLP--AIMVTH 193
Cdd:cd03245 167 PTSAMDMN----SEERLKERLRQLLGDktLIIITH 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-211 |
2.99e-24 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 95.51 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRH-IGVLYQDALLFS 91
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT---SGRATVAGHDVVREPREVRRrIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGNIA-FAMPKGNKKQRL-EKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:cd03265 87 ELTGWENLYiHARLYGVPGAERrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 639318220 170 RVDTRELVFSQIRDHKLPAIMVTHDHSDADA--------ANGKLITLSSA 211
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlcdrvaiiDHGRIIAEGTP 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-194 |
3.55e-24 |
|
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: 99.37 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkanGEVWLNGQNIDNTP-----PHLRHIGVLYQDAllFSHL----TVAGNI 99
Cdd:COG4172 312 GETLGLVGESGSGKSTLGLALLRLIPSE----GEIRFDGQDLDGLSrralrPLRRRMQVVFQDP--FGSLsprmTVGQII 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAM----PKGNKKQRLEKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD--TQLRVD 172
Cdd:COG4172 386 AEGLrvhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsVQAQIL 465
|
170 180
....*....|....*....|....
gi 639318220 173 T--RELvfsQiRDHKLPAIMVTHD 194
Cdd:COG4172 466 DllRDL---Q-REHGLAYLFISHD 485
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-166 |
3.79e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRH---IGVLYQDALLFSHLTVAGNI-A 100
Cdd:COG1137 25 EVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGRIFLDGEDITHLPMHKRArlgIGYLPQEASIFRKLTVEDNIlA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 101 FA-MPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:COG1137 102 VLeLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-161 |
4.05e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.43 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR-HIGVLY--QDALLFSHLTVAGNIAF 101
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPR---SGSIRFDGEDITGLPPHRIaRLGIGYvpEGRRIFPSLTVEENLLL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 102 AMPKGNKKqrlEKIAHALEQVG-----LKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:COG0410 102 GAYARRDR---AEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-169 |
4.36e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 95.64 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELL--LSLneQVNGGEILTIMGPSGSGKSSLL---NWLTgtLPSSfkanGEVWLNGQNIDNTPP------------ 75
Cdd:COG4598 18 FGDLEVLkgVSL--TARKGDVISIIGSSGSGKSTFLrciNLLE--TPDS----GEIRVGGEEIRLKPDrdgelvpadrrq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 76 --HLR-HIGVLYQDALLFSHLTVAGNIAFAmP----KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRM 148
Cdd:COG4598 90 lqRIRtRLGMVFQSFNLWSHMTVLENVIEA-PvhvlGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180
....*....|....*....|.
gi 639318220 149 LLSEPKAILLDEPFSKLDTQL 169
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPEL 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-201 |
4.73e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.68 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTgTLPSSFKANGEVWLNGQNI---DNT 73
Cdd:PRK14267 1 MKFAIETVNLRVyYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLL-ELNEEARVEGEVRLFGRNIyspDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 74 PPHLR-HIGVLYQDALLFSHLTVAGNIAFAMPKGN----KKQRLEKIAHALEQVGL----KDMGNRHPDNLSGGQQARVA 144
Cdd:PRK14267 80 PIEVRrEVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvksKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 145 LLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLpaIMVThdHSDADAA 201
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVT--HSPAQAA 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-166 |
5.72e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTGTLPSsFKANGEVWLNGQNI---DNT 73
Cdd:COG1117 8 LEPKIEVRNLNVyYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPG-ARVEGEILLDGEDIydpDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 74 PPHLR-HIGVLYQDALLFSHlTVAGNIAFAmPK--GNK-KQRLEKIA-HALEQVGL----KDMGNRHPDNLSGGQQARVA 144
Cdd:COG1117 87 VVELRrRVGMVFQKPNPFPK-SIYDNVAYG-LRlhGIKsKSELDEIVeESLRKAALwdevKDRLKKSALGLSGGQQQRLC 164
|
170 180
....*....|....*....|..
gi 639318220 145 LLRMLLSEPKAILLDEPFSKLD 166
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALD 186
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
25-168 |
6.17e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.79 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLL---NWLTGtlPSSfkanGEVWLNGQNIDN-TPPHL----RHIGVLYQDALLFSHLTVA 96
Cdd:PRK11153 27 HIPAGEIFGVIGASGAGKSTLIrciNLLER--PTS----GRVLVDGQDLTAlSEKELrkarRQIGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 97 GNIAFAM-----PKGNKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:PRK11153 101 DNVALPLelagtPKAEIKARVTEL---LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-194 |
8.44e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 96.28 E-value: 8.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLNEqvngGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPH------LRHIGVLYQDAllFSHL 93
Cdd:COG0444 26 FDVRR----GETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKelrkirGREIQMIFQDP--MTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 ----TVaGNIaFAMP-----KGNKKQRLEKIAHALEQVGL---KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:COG0444 100 npvmTV-GDQ-IAEPlrihgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639318220 162 FSKLDtqlrVDTRelvfSQI--------RDHKLPAIMVTHD 194
Cdd:COG0444 178 TTALD----VTIQ----AQIlnllkdlqRELGLAILFITHD 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-194 |
1.82e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIK--NCqLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSL---LNWLTgtLPSSfkanGEVWLNGQNID-NTPPH- 76
Cdd:PRK11124 2 SIQLNgiNC-FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLE--MPRS----GTLNIAGNHFDfSKTPSd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 -----LRH-IGVLYQDALLFSHLTVAGNIAFA------MPKGNKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVA 144
Cdd:PRK11124 75 kaireLRRnVGMVFQQYNLWPHLTVQQNLIEApcrvlgLSKDQALARAEKL---LERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 639318220 145 LLRMLLSEPKAILLDEPFSKLDTQLrvdTRELVfSQIRDHKLPAI---MVTHD 194
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEI---TAQIV-SIIRELAETGItqvIVTHE 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-201 |
2.23e-23 |
|
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: 96.97 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 16 NELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPH--LRHIGVLYQDALLFSHl 93
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP---TEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAMPKGNKkqrlEKIAHALEQVGLKDMGN-----------RHPDNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:TIGR02857 411 TIAENIRLARPDASD----AEIREALERAGLDEFVAalpqgldtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|....*....
gi 639318220 163 SKLDTQLRVDTRELVFSQIRDHKLpaIMVTHDHSDADAA 201
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGRTV--LLVTHRLALAALA 523
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-206 |
2.30e-23 |
|
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: 92.64 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNC-QLYRQNELLLSLNEQVNGGeILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR-HIGV 82
Cdd:cd03264 1 LQLENLtKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQDVLKQPQKLRrRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDALLFSHLTVAGNIAF-AMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYiAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 639318220 161 PFSKLDTQLRVDTRELVFSQIRDHKLpaIMVTHDHSDADA--------ANGKLI 206
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESlcnqvavlNKGKLV 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-198 |
3.55e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.49 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDN-TPPHLRH-----IGVLYQDALLFSHLTVAGNI 99
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIAKiSDAELREvrrkkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAMPKGN--KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELV 177
Cdd:PRK10070 128 AFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180
....*....|....*....|.
gi 639318220 178 FSQIRDHKLPAIMVTHDHSDA 198
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEA 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-194 |
3.83e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 93.64 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL-YRQNELLLSLNE---QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQ--NIDNTP 74
Cdd:PRK13650 1 MSNIIEVKNLTFkYKEDQEKYTLNDvsfHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQIIIDGDllTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 75 PHLRHIGVLYQDA-LLFSHLTVAGNIAFAMP-KG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLS 151
Cdd:PRK13650 78 DIRHKIGMVFQNPdNQFVGATVEDDVAFGLEnKGiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 152 EPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-194 |
4.28e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 96.28 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFsH 92
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNIAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPDNL-----------SGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:TIGR02868 423 TTVRENLRLARPDATD----EELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....*
gi 639318220 162 FSKLDtqlrVDTRELVFSQIRD--HKLPAIMVTHD 194
Cdd:TIGR02868 499 TEHLD----AETADELLEDLLAalSGRTVVLITHH 529
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-162 |
4.98e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 93.29 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIdntpPHL------ 77
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDnISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD---HGEILFDGENI----PAMsrsrly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 ---RHIGVLYQDALLFSHLTVAGNIAFamPKGNKKQRLEKIAHA-----LEQVGLKDMGNRHPDNLSGGQQARVALLRML 149
Cdd:PRK11831 81 tvrKRMSMLFQSGALFTDMNVFDNVAY--PLREHTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170
....*....|...
gi 639318220 150 LSEPKAILLDEPF 162
Cdd:PRK11831 159 ALEPDLIMFDEPF 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-196 |
6.80e-23 |
|
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: 95.59 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDN-TPPHL-RHIGVLYQDALLFSHlTVAGNIA-F 101
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT---AGSVRLDGADLSQwDREELgRHIGYLPQDVELFDG-TIAENIArF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 AMPKGnkkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLR 170
Cdd:COG4618 430 GDADP------EKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE 503
|
170 180
....*....|....*....|....*.
gi 639318220 171 VDTRELVfSQIRDHKLPAIMVTHDHS 196
Cdd:COG4618 504 AALAAAI-RALKARGATVVVITHRPS 528
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-194 |
8.30e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 91.76 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR------HIGVLYQDALLFSHLTVAGNI 99
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGS---SGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AF-AMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELV 177
Cdd:PRK10584 110 ELpALLRGeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170
....*....|....*..
gi 639318220 178 FSQIRDHKLPAIMVTHD 194
Cdd:PRK10584 190 FSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-197 |
1.12e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLRHI----GVLYQ--DALLFSHlT 94
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTS----GKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFAmPKG---NKKQRLEKIAHALEQVGLK--DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQl 169
Cdd:PRK13637 101 IEKDIAFG-PINlglSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK- 178
|
170 180 190
....*....|....*....|....*....|..
gi 639318220 170 rvdTRELVFSQIRD----HKLPAIMVTHDHSD 197
Cdd:PRK13637 179 ---GRDEILNKIKElhkeYNMTIILVSHSMED 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-166 |
1.99e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNtpPHLRHI-GVLYQDALLFSHLTVAGNIAFA----M 103
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDA--KEMRAIsAYVQQDDLFIPTLTVREHLMFQahlrM 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639318220 104 PKG-NKKQRLEKIAHALEQVGLKD-------MGNRHpDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:TIGR00955 129 PRRvTKKEKRERVDEVLQALGLRKcantrigVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-212 |
2.24e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 16 NELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHLRHIGVLY--QDALLFSH 92
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTS----GTLLFEGEDISTLKPEIYRQQVSYcaQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 lTVAGNIAFAMPKGNKKQRLEKIAHALEQVGLKD-MGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRV 171
Cdd:PRK10247 96 -TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639318220 172 DTRELVFSQIRDHKLPAIMVTHDHSDADAANgKLITLSSAL 212
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDEINHAD-KVITLQPHA 214
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-193 |
2.38e-22 |
|
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: 93.95 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFSHlTVAGNIAfam 103
Cdd:TIGR01842 341 LQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENIA--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 pKGNKKQRLEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVD 172
Cdd:TIGR01842 414 -RFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQA 492
|
170 180
....*....|....*....|.
gi 639318220 173 TRELVfSQIRDHKLPAIMVTH 193
Cdd:TIGR01842 493 LANAI-KALKARGITVVVITH 512
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-194 |
2.94e-22 |
|
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: 89.62 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 6 QIKNC--QLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPpHLRHIGVL 83
Cdd:cd03226 1 RIENIsfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES---SGSILLNGKPIKAKE-RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 84 YQDA--LLFSHlTVAGNIAFAMPKGNKKQrlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:cd03226 77 MQDVdyQLFTD-SVREELLLGLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....*
gi 639318220 162 FSKLDtqlRVDTREL--VFSQIRDHKLPAIMVTHD 194
Cdd:cd03226 154 TSGLD---YKNMERVgeLIRELAAQGKAVIVITHD 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-184 |
3.54e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.34 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPHL-RHIGVLYQDALLFSHLTV 95
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGTPLAEQRDEPhENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGNIAFAMPKGNKKQRleKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTRE 175
Cdd:TIGR01189 91 LENLHFWAAIHGGAQR--TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD----KAGVA 164
|
....*....
gi 639318220 176 LVFSQIRDH 184
Cdd:TIGR01189 165 LLAGLLRAH 173
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-193 |
9.28e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 88.32 E-value: 9.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPHLrHIGVL 83
Cdd:cd03231 1 LEADELTCERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP---PLAGRVLLNGGPLDFQRDSI-ARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 84 Y---QDALLfSHLTVAGNIAFAMPKGNKKQRLEkiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:cd03231 77 YlghAPGIK-TTLSVLENLRFWHADHSDEQVEE----ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 639318220 161 PFSKLDTQlrvdTRELVFSQIRDHKLP---AIMVTH 193
Cdd:cd03231 152 PTTALDKA----GVARFAEAMAGHCARggmVVLTTH 183
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-202 |
1.06e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLpssFKANGEVWLNGQ--NIDNTPPHLRHIGVLYQDA-LLFSHLTVAGNIAF 101
Cdd:PRK13635 29 SVYEGEWVAIVGHNGSGKSTLAKLLNGLL---LPEAGTITVGGMvlSEETVWDVRRQVGMVFQNPdNQFVGATVQDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 A-----MPKgnkKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTREL 176
Cdd:PRK13635 106 GlenigVPR---EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180
....*....|....*....|....*..
gi 639318220 177 VfSQIRDHK-LPAIMVTHDHSDADAAN 202
Cdd:PRK13635 183 V-RQLKEQKgITVLSITHDLDEAAQAD 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
26-166 |
1.20e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.56 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHL-----RHIGVLYQD--ALLFSHLTVAG 97
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEePTS----GEILFDGQDITGLSGRElrplrRRMQMVFQDpyASLNPRMTVGD 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 98 NIAFAM---PKGNKKQRLEKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:COG4608 117 IIAEPLrihGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-194 |
1.31e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 89.41 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNI---DNTPPHLRHIGVLYQD-------Allf 90
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTS----GKVTVDGLDTldeENLWEIRKKVGMVFQNpdnqfvgA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 shlTVAGNIAFAM-----PKGNKKQRlekIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:TIGR04520 94 ---TVEDDVAFGLenlgvPREEMRKR---VDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180
....*....|....*....|....*....
gi 639318220 166 DTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHD 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-194 |
2.10e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPH---LRHIGVLYQDALL 89
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP---RDAGNIIIDDEDISLLPLHaraRRGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHLTVAGNIAFAMP---KGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PRK10895 90 FRRLSVYDNLMAVLQirdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180
....*....|....*....|....*...
gi 639318220 167 TQLRVDTRELVfSQIRDHKLPAIMVTHD 194
Cdd:PRK10895 170 PISVIDIKRII-EHLRDSGLGVLITDHN 196
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-166 |
2.16e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 87.22 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLpSSFKANGEVWLNGQNID-NTPPhlRHIGVLYQDALLFSHLTV 95
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGRPLDkRSFR--KIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639318220 96 AGNIAFAmpkgnkkqrlekiAHaleqvgLKdmgnrhpdNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:cd03213 100 RETLMFA-------------AK------LR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-209 |
2.54e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGT-LPSSfkanGEVWLNGQNID-----NTPPHLRHIGVLYQDALLFSHLTVAGNIAF- 101
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIeRPSA----GKIWFSGHDITrlknrEVPFLRRQIGMIFQDHHLLMDRTVYDNVAIp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 ---AMPKGNKKQRleKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELvF 178
Cdd:PRK10908 104 liiAGASGDDIRR--RVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRL-F 180
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 179 SQIRDHKLPAIMVTHDHSDADAANGKLITLS 209
Cdd:PRK10908 181 EEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-167 |
3.36e-21 |
|
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: 87.67 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNI-DNTPPHLR-HIGVLYQDALLFSHlTV 95
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDS----GRILIDGHDVrDYTLASLRrQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGNIAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDEPFSK 164
Cdd:cd03251 93 AENIAYGRPGATR----EEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
...
gi 639318220 165 LDT 167
Cdd:cd03251 169 LDT 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-209 |
3.53e-21 |
|
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: 87.67 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLtgtlpssFK----ANGEVWLNGQNIDN-TPPHLR-HIGVLYQDALLFsHLTVAGNI 99
Cdd:cd03253 24 IPAGKKVAIVGPSGSGKSTILRLL-------FRfydvSSGSILIDGQDIREvTLDSLRrAIGVVPQDTVLF-NDTIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAMPKGNKKQRLE--KIAHALEQV--------------GLKdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:cd03253 96 RYGRPDATDEEVIEaaKAAQIHDKImrfpdgydtivgerGLK---------LSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 639318220 164 KLDTQlrvdTRELVFSQIRD---HKlPAIMVTHDHS---DADaangKLITLS 209
Cdd:cd03253 167 ALDTH----TEREIQAALRDvskGR-TTIVIAHRLStivNAD----KIIVLK 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-193 |
3.99e-21 |
|
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: 85.73 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNT-PPHLR-HIGVLYQDALLFSH 92
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRVRLDGADISQWdPNELGdHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 lTVAGNIafampkgnkkqrlekiahaleqvglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVD 172
Cdd:cd03246 91 -SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD----VE 130
|
170 180
....*....|....*....|....
gi 639318220 173 TRELVFSQIRDHKLP---AIMVTH 193
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAH 154
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-190 |
4.14e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 87.16 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQL-YRQNE--LLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH-LR- 78
Cdd:cd03244 2 DIEFKNVSLrYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS---SGSILIDGVDISKIGLHdLRs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 HIGVLYQDALLFSHlTVAGNIAfamPKGNKKQrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLR 147
Cdd:cd03244 79 RISIIPQDPVLFSG-TIRSNLD---PFGEYSD--EELWQALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 639318220 148 MLLSEPKAILLDEPFSKLDTQlrvdTRELVFSQIRD-----------HKLPAIM 190
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPE----TDALIQKTIREafkdctvltiaHRLDTII 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-201 |
5.58e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVwlngqnidnTPPHLRHIGVLYQ-----D 86
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLrPTS----GTV---------RRAGGARVAYVPQrsevpD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 87 ALlfsHLTVAGniAFAM---PKGNKKQRLEK-----IAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:NF040873 69 SL---PLTVRD--LVAMgrwARRGLWRRLTRddraaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 159 DEPFSKLDTQLRVDTRELVfSQIRDHKLPAIMVTHDHSDADAA 201
Cdd:NF040873 144 DEPTTGLDAESRERIIALL-AEEHARGATVVVVTHDLELVRRA 185
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
1-168 |
6.19e-21 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 90.31 E-value: 6.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQLYRQNELLLSLNEQ---VNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPP-H 76
Cdd:TIGR03375 460 LQGEIEFRNVSFAYPGQETPALDNVsltIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT---EGSVLLDGVDIRQIDPaD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 LRH-IGVLYQDALLFsHLTVAGNIAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVA 144
Cdd:TIGR03375 537 LRRnIGYVPQDPRLF-YGTLRDNIALGAPYADD----EEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180
....*....|....*....|....
gi 639318220 145 LLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNR 635
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-194 |
8.00e-21 |
|
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: 89.86 E-value: 8.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVW--LNGQNIDNTPPHL-------RHIGVLYQDALLFSHLTV 95
Cdd:TIGR03269 306 EVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT---SGEVNvrVGDEWVDMTKPGPdgrgrakRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGN----IAFAMPKGNKKQrleKIAHALEQVGL-----KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:TIGR03269 383 LDNlteaIGLELPDELARM---KAVITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180
....*....|....*....|....*...
gi 639318220 167 TQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:TIGR03269 460 PITKVDVTHSILKAREEMEQTFIIVSHD 487
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-193 |
9.04e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 2 QSSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTGTLPSSfKANGEVWLNGQNIDNTPPHL 77
Cdd:PRK14247 1 MNKIEIRDLKVsFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEA-RVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 --RHIGVLYQDALLFSHLTVAGNIAFAmPKGN-----KKQRLEKIAHALEQVGL----KDMGNRHPDNLSGGQQARVALL 146
Cdd:PRK14247 80 lrRRVQMVFQIPNPIPNLSIFENVALG-LKLNrlvksKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 639318220 147 RMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDhkLPAIMVTH 193
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTH 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-193 |
1.09e-20 |
|
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: 85.80 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDntPPHLRHIGVLYQDALLFS 91
Cdd:cd03269 10 FGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDS----GEVLFDGKPLD--IAARNRIGYLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGN-IAFAMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTqL 169
Cdd:cd03269 84 KMKVIDQlVYLAQLKGlKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-V 162
|
170 180
....*....|....*....|....
gi 639318220 170 RVDTRELVFSQIRDHKLPAIMVTH 193
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTH 186
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-207 |
2.16e-20 |
|
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: 84.50 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYR-QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGtLPSSFKANGEVWLNGQNIDNTPPHLRH---I 80
Cdd:cd03217 1 LEIKDLHVSVgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEVTEGEILFKGEDITDLPPEERArlgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 81 GVLYQDALLFSHLtvagniafampkgnkkqrleKIAHALEQVGlkdmgnrhpDNLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:cd03217 80 FLAFQYPPEIPGV--------------------KNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 639318220 161 PFSKLDtqlrVDTRELV---FSQIRDHKLPAIMVTH-----DHSDADAA----NGKLIT 207
Cdd:cd03217 131 PDSGLD----IDALRLVaevINKLREEGKSVLIITHyqrllDYIKPDRVhvlyDGRIVK 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-194 |
3.09e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYR----QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHL- 77
Cdd:PRK11629 6 LQCDNlCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTS----GDVIFNGQPMSKLSSAAk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 -----RHIGVLYQDALLFSHLTVAGNIAFAMPKGNKK--QRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLL 150
Cdd:PRK11629 82 aelrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 639318220 151 SEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-202 |
3.30e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWL------NGQNIDNTPPHLRHIGVLYQ--DALL 89
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTS----GTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFA-MPKGNKKQRLEKIA-HALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PRK13634 99 FEE-TVEKDICFGpMNFGVSEEDAKQKArEMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 639318220 167 TQLRVDTRELVFSQIRDHKLPAIMVThdHSDADAAN 202
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVT--HSMEDAAR 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-206 |
3.50e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.81 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLL--SLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNID-NTPPHLR-HIGVLYQDA 87
Cdd:PRK13632 17 YPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQS----GEIKIDGITISkENLKEIRkKIGIIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 88 -LLFSHLTVAGNIAFAMPkgNKKQRLEK----IAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:PRK13632 93 dNQFIGATVEDDIAFGLE--NKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 639318220 163 SKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDADAA-------NGKLI 206
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILAdkvivfsEGKLI 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-167 |
4.55e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 87.63 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfKANGEVWLNGQNIdnTPPHLRHIGVLYQDALLFSHLTVAGNIAFA----MP 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGN-NFTGTILANNRKP--TKQILKRTGFVTQDDILYPHLTVRETLVFCsllrLP 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639318220 105 KGNKKQRLEKIAHA-LEQVGLKD-----MGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDT 167
Cdd:PLN03211 171 KSLTKQEKILVAESvISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-193 |
5.01e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.13 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQL-YRQNE--LLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRH-I 80
Cdd:cd03247 1 LSINNVSFsYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVPVSDLEKALSSlI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 81 GVLYQDALLFSHlTVAGNIafampkgnkkqrlekiahaleqvglkdmGNRhpdnLSGGQQARVALLRMLLSEPKAILLDE 160
Cdd:cd03247 78 SVLNQRPYLFDT-TLRNNL----------------------------GRR----FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190
....*....|....*....|....*....|...
gi 639318220 161 PFSKLDTQLRVDTRELVFSQIRDHKLpaIMVTH 193
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTL--IWITH 155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-194 |
5.96e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkanGEVWLNGQNIDNTP-----PHLRHIGVLYQD--A 87
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ----GEIWFDGQPLHNLNrrqllPVRHRIQVVFQDpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 88 LLFSHLTVAGNIAFAM----PKGNKKQRLEKIAHALEQVGLkDMGNRH--PDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLrvhqPTLSAAQREQQVIAVMEEVGL-DPETRHryPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190
....*....|....*....|....*....|...
gi 639318220 162 FSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-185 |
6.09e-20 |
|
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: 83.81 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRHIGVLYQDALLFSH 92
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQKNIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNI-AFAMPKGNKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRV 171
Cdd:cd03268 87 LTARENLrLLARLLGIRKKRIDEV---LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170
....*....|....
gi 639318220 172 DTRELvfsqIRDHK 185
Cdd:cd03268 164 ELREL----ILSLR 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-202 |
6.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PS--SFKANGEVWLNGQNIDNTPPHLRHIGVLYQ--DALLFSHl 93
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTegKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAmPK--GNKKQRLEKIA-HALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:PRK13643 101 TVLKDVAFG-PQnfGIPKEKAEKIAaEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190
....*....|....*....|....*....|....
gi 639318220 170 RVDTRELvFSQIRDHKLPAIMVTHDHSD-ADAAN 202
Cdd:PRK13643 180 RIEMMQL-FESIHQSGQTVVLVTHLMDDvADYAD 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-183 |
6.64e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQI-KNCQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPHLR- 78
Cdd:PRK09984 1 MQTIIRVeKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 ------HIGVLYQDALLFSHLTVAGNIAFAMPKGN----------KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQAR 142
Cdd:PRK09984 81 irksraNTGYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639318220 143 VALLRMLLSEPKAILLDEPFSKLDTQlrvdTRELVFSQIRD 183
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPE----SARIVMDTLRD 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-206 |
7.24e-20 |
|
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: 83.81 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH-LR-HIGVLYQDALL 89
Cdd:cd03254 12 YDEKKPVLKdINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRDISRKsLRsMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFampkGNKKQRLEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILL 158
Cdd:cd03254 89 FSG-TIMENIRL----GRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 159 DEPFSKLDTQlrvdTRELVFSQIRD--HKLPAIMVTHDHS---DADAA----NGKLI 206
Cdd:cd03254 164 DEATSNIDTE----TEKLIQEALEKlmKGRTSIIIAHRLStikNADKIlvldDGKII 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-194 |
9.03e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.74 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHL----RHIGVLYQ--DALL 89
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTS----GEVLIKGEPIKYDKKSLlevrKTVGIVFQnpDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFA-MPKGNKKQRLEK-IAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDT 167
Cdd:PRK13639 92 FAP-TVEEDVAFGpLNLGLSKEEVEKrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180
....*....|....*....|....*..
gi 639318220 168 QLRVDTRELVFsQIRDHKLPAIMVTHD 194
Cdd:PRK13639 171 MGASQIMKLLY-DLNKEGITIIISTHD 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-209 |
1.21e-19 |
|
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: 83.54 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 12 LYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGqNI--DNTPPHLRHIGVLY-QDA 87
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTS----GEVRVAG-LVpwKRRKKFLRRIGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 88 LLFSHLTVAGNIAF-----AMPKGNKKQRLEKIAHALEQVGLKDMGNRhpdNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:cd03267 105 QLWWDLPVIDSFYLlaaiyDLPPARFKKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 639318220 163 SKLD--TQLRVdtRELVFSQIRDHKLPAIMVTHDHSDADAANGKLITLS 209
Cdd:cd03267 182 IGLDvvAQENI--RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-193 |
1.45e-19 |
|
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: 82.52 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQL------YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGqnidntpphlr 78
Cdd:cd03250 1 ISVEDASFtwdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 hiGVLY--QDALLFShLTVAGNIAFAMPKgnKKQRLEKIAHA------LEQVGLKDM------GNrhpdNLSGGQQARVA 144
Cdd:cd03250 67 --SIAYvsQEPWIQN-GTIRENILFGKPF--DEERYEKVIKAcalepdLEILPDGDLteigekGI----NLSGGQKQRIS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 639318220 145 LLRMLLSEPKAILLDEPFSKLDTQLRVD-TRELVFSQIRDHKlPAIMVTH 193
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLNNK-TRILVTH 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-193 |
1.66e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.21 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLL-SLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFkaNGEVWLNGQNIDNTPPH-LR-HIG 81
Cdd:COG1119 4 LELRNVTVRRGGKTILdDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY--GNDVRLFGERRGGEDVWeLRkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 82 VLYQD-ALLFSHLTVAGNI----AFAM----PKGNKKQRlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSE 152
Cdd:COG1119 82 LVSPAlQLRFPRDETVLDVvlsgFFDSiglyREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 639318220 153 PKAILLDEPFSKLDTQLRVDTRELVfSQIRDHKLPA-IMVTH 193
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALL-DKLAAEGAPTlVLVTH 201
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-208 |
1.99e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTGtlPSSfkanGEVWLNGQNID---NTPPHLR-------- 78
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLrciNFLEK--PSE----GSIVVNGQTINlvrDKDGQLKvadknqlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 ----HIGVLYQDALLFSHLTVAGNIAFA------MPKGNKKQRLEKIahaLEQVGLKDMGN-RHPDNLSGGQQARVALLR 147
Cdd:PRK10619 89 llrtRLTMVFQHFNLWSHMTVLENVMEApiqvlgLSKQEARERAVKY---LAKVGIDERAQgKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639318220 148 MLLSEPKAILLDEPFSKLDTQLrVDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-208 |
2.79e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.11 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 21 SLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDN--TPPHLRHIGVLYQDALLFSHLTVAGN 98
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHyaSKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAfampKGN----------KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:PRK10253 102 VA----RGRyphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 169 LRVDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLITL 208
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-193 |
2.90e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLP--SSFKANGeVWLNgqNIDntPPHLR-HIGVLYQDALLFsHLTVAGN 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqGSLKING-IELR--ELD--PESWRkHLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPDNL-----------SGGQQARVALLRMLLSEPKAILLDEPFSKLDT 167
Cdd:PRK11174 443 VLLGNPDASD----EQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180
....*....|....*....|....*...
gi 639318220 168 QlrvdTRELVFSQIRD--HKLPAIMVTH 193
Cdd:PRK11174 519 H----SEQLVMQALNAasRRQTTLMVTH 542
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-193 |
4.31e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH--LRH-IGVLYQDALLFSHLTVAGNIA 100
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVYqPDS----GEILLDGEPVRFRSPRdaQAAgIAIIHQELNLVPNLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FA-MPKG----NKKQRLEKIAHALEQVGLkdmgNRHPD----NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlRV 171
Cdd:COG1129 102 LGrEPRRggliDWRAMRRRARELLARLGL----DIDPDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLT---ER 174
|
170 180
....*....|....*....|....*..
gi 639318220 172 DTRELvFSQIRDhkLPA-----IMVTH 193
Cdd:COG1129 175 EVERL-FRIIRR--LKAqgvaiIYISH 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-166 |
5.36e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.13 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLT--GTLPSSFKANGEVWLNGQNI----DNT 73
Cdd:PRK14239 2 TEPILQVSDLSVyYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHNIysprTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 74 PPHLRHIGVLYQDALLFShLTVAGNIAFAMP-KGNK-KQRL-EKIAHALEQVGLKD-MGNRHPDN---LSGGQQARVALL 146
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRlKGIKdKQVLdEAVEKSLKGASIWDeVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180
....*....|....*....|
gi 639318220 147 RMLLSEPKAILLDEPFSKLD 166
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALD 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-193 |
9.08e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 2 QSSLQIKNCQL-YRQNEL--LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLT-GTLPSSfkanGEVWLNGQNI-DNTPPH 76
Cdd:PRK11160 336 QVSLTLNNVSFtYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQ----GEILLNGQPIaDYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 LRH-IGVLYQDALLFSHlTVAGNIAFAMPKGNKkqrlEKIAHALEQVGLKDM-------------GNRHpdnLSGGQQAR 142
Cdd:PRK11160 412 LRQaISVVSQRVHLFSA-TLRDNLLLAAPNASD----EALIEVLQQVGLEKLleddkglnawlgeGGRQ---LSGGEQRR 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 639318220 143 VALLRMLLSEPKAILLDEPFSKLDTqlrvDTRELVFSQIRDH---KlPAIMVTH 193
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDA----ETERQILELLAEHaqnK-TVLMITH 532
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-168 |
9.92e-19 |
|
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: 81.05 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWL------TgtlpssfkaNGEVWLNGQNI-DNTPPHLR-HIGVLYQD 86
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydpT---------SGEILLDGVDIrDLNLRWLRsQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 87 ALLFShLTVAGNIAFampkGNKKQRLEKIAHALEQVGLKDMGNRHPDN-----------LSGGQQARVALLRMLLSEPKA 155
Cdd:cd03249 86 PVLFD-GTIAENIRY----GKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRIAIARALLRNPKI 160
|
170
....*....|...
gi 639318220 156 ILLDEPFSKLDTQ 168
Cdd:cd03249 161 LLLDEATSALDAE 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-194 |
1.18e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPHL----RHIGVLYQ--DALL 89
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSS----GRILFDGKPIDYSRKGLmklrESVGMVFQdpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FShLTVAGNIAFA-----MPKGNKKQRLEkiaHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSK 164
Cdd:PRK13636 96 FS-ASVYQDVSFGavnlkLPEDEVRKRVD---NALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190
....*....|....*....|....*....|
gi 639318220 165 LDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-206 |
1.69e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNI-DNTPPHLRH-IGVLYQDA-LLFSHLTVAGN 98
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLtAKTVWDIREkVGIVFQNPdNQFVGATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFAMP-KGNKKQRLEKIAH-ALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTREL 176
Cdd:PRK13640 106 VAFGLEnRAVPRPEMIKIVRdVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170 180 190
....*....|....*....|....*....|
gi 639318220 177 VFSQIRDHKLPAIMVTHDHSDADAANGKLI 206
Cdd:PRK13640 186 IRKLKKKNNLTVISITHDIDEANMADQVLV 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-198 |
1.72e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.95 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLSLNE---QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNID--NTPPHLRH 79
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDvsfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK---SGEIFYNNQAITddNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 IGVLYQDAL-LFSHLTVAGNIAF-----AMPKGNKKqrlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEP 153
Cdd:PRK13648 85 IGIVFQNPDnQFVGSIVKYDVAFglenhAVPYDEMH---RRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639318220 154 KAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-194 |
1.89e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 18 LLLSLNEQVNGGEILTIMGPSGSGKSSLL---NWLTGTLPSSFKANGEVWLNGQNIDNTPP-HLR-HIGVLYQDALLFSH 92
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRkEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNIAFAMPK-GNKKQR-LEKIAH-ALEQVGL----KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:PRK14246 105 LSIYDNIAYPLKShGIKEKReIKKIVEeCLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180
....*....|....*....|....*....
gi 639318220 166 DTQLRVDTRELVfSQIRDhKLPAIMVTHD 194
Cdd:PRK14246 185 DIVNSQAIEKLI-TELKN-EIAIVIVSHN 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-168 |
4.38e-18 |
|
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: 81.69 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNI-DNTPPHLR-HIGVLYQDALLF 90
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRfYEPDS----GQILLDGHDLaDYTLASLRrQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHlTVAGNIAFAMPKGNKKQRLEKiahALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLD 159
Cdd:TIGR02203 419 ND-TIANNIAYGRTEQADRAEIER---ALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILD 494
|
....*....
gi 639318220 160 EPFSKLDTQ 168
Cdd:TIGR02203 495 EATSALDNE 503
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-194 |
5.50e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.15 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLNeqVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDntPPHLRHIGV------LYQ-----DA 87
Cdd:COG4152 20 VSFT--VPKGEIFGLLGPNGAGKTTTIRIILGiLAPDS----GEVLWDGEPLD--PEDRRRIGYlpeergLYPkmkvgEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 88 LLFshltvagniaFAMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:COG4152 92 LVY----------LARLKGlSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 167 tqlrVDTRELVFSQIRDHKL---PAIMVTHD 194
Cdd:COG4152 162 ----PVNVELLKDVIRELAAkgtTVIFSSHQ 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-198 |
5.94e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.44 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLL---SLNEQVNggEILTIMGPSGSGKSSLL---NWLTGTLPSsFKANGEVWLNGQNI---DNTPP 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVknvWLDIPKN--QITAFIGPSGCGKSTILrcfNRLNDLIPG-FRVEGKVTFHGKNLyapDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 76 HLR-HIGVLYQDALLFSHlTVAGNIAF-AMPKGNKKQRLEKIAHALEQVGL----KDMGNRHPDNLSGGQQARVALLRML 149
Cdd:PRK14243 88 EVRrRIGMVFQKPNPFPK-SIYDNIAYgARINGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 639318220 150 LSEPKAILLDEPFSKLD--TQLRVDtrELVFSQIRDHKLpaIMVTHDHSDA 198
Cdd:PRK14243 167 AVQPEVILMDEPCSALDpiSTLRIE--ELMHELKEQYTI--IIVTHNMQQA 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-194 |
1.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSL---LNWL----TGTLPSSFKA--------NGEVWLNGQNIDNTPPH--------LRHIGV 82
Cdd:PRK13651 30 INQGEFIAIIGQTGSGKTTFiehLNALllpdTGTIEWIFKDeknkkktkEKEKVLEKLVIQKTRFKkikkikeiRRRVGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDA--LLFSHlTVAGNIAF-AMPKGNKKQRLEKIAHA-LEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAIL 157
Cdd:PRK13651 110 VFQFAeyQLFEQ-TIEKDIIFgPVSMGVSKEEAKKRAAKyIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLV 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 639318220 158 LDEPFSKLDTQLRVDTRELvFSQIRDHKLPAIMVTHD 194
Cdd:PRK13651 189 FDEPTAGLDPQGVKEILEI-FDNLNKQGKTIILVTHD 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-209 |
2.01e-17 |
|
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: 80.06 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 30 EILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRH-IGVLYQDALLFSHLTVAGNIAF-AMPKGN 107
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLVGGKDIETNLDAVRQsLGMCPQHNILFHHLTVAEHILFyAQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 108 KKQRLE-KIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKL 186
Cdd:TIGR01257 1034 SWEEAQlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
170 180
....*....|....*....|...
gi 639318220 187 paIMVTHDHSDADAANGKLITLS 209
Cdd:TIGR01257 1114 --IMSTHHMDEADLLGDRIAIIS 1134
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-194 |
2.63e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.59 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEV-WLNGQNIDNTPPHLRH----IGVLYQDAL--LFSHLTVAGNIAF 101
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKAT---DGEVaWLGKDLLGMKDDEWRAvrsdIQMIFQDPLasLNPRMTIGEIIAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 AM----PKGNKKQRLEKIAHALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTREL 176
Cdd:PRK15079 124 PLrtyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170
....*....|....*...
gi 639318220 177 VFSQIRDHKLPAIMVTHD 194
Cdd:PRK15079 204 LQQLQREMGLSLIFIAHD 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-166 |
2.69e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTlPSSFKANGEVWLNGQNIDNTPPHLR-HIGV 82
Cdd:CHL00131 8 LEIKNLHAsVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYKILEGDILFKGESILDLEPEERaHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LyqdaLLFSH-LTVAG--NIAFAMPKGNKKQR------------LEKIAHALEQVGLKD-MGNRH-PDNLSGGQQARVAL 145
Cdd:CHL00131 87 F----LAFQYpIEIPGvsNADFLRLAYNSKRKfqglpeldplefLEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEI 162
|
170 180
....*....|....*....|.
gi 639318220 146 LRMLLSEPKAILLDEPFSKLD 166
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLD 183
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-196 |
3.95e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 2 QSSLQIKNCQLYRQN-ELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLngqnidntpPHLRH 79
Cdd:COG4178 360 DGALALEDLTLRTPDgRPLLEdLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY---GSGRIAR---------PAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 IGVLYQ----------DALLFshltvagniafamPKGNKKQRLEKIAHALEQVGLKDMGNRH------PDNLSGGQQARV 143
Cdd:COG4178 428 VLFLPQrpylplgtlrEALLY-------------PATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 639318220 144 ALLRMLLSEPKAILLDEPFSKLDTqlrvDTRELVFSQIRDHkLPA---IMVTHDHS 196
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDE----ENEAALYQLLREE-LPGttvISVGHRST 545
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-168 |
5.36e-17 |
|
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: 76.37 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFSHlT 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE---NGRVLVDGHDLALADPAWlrRQVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFAMPKGNKKQRLE--KIAHALEQV-----GLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDT 167
Cdd:cd03252 92 IRDNIALADPGMSMERVIEaaKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
.
gi 639318220 168 Q 168
Cdd:cd03252 172 E 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-194 |
5.85e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLngqnidntPPHLRhIGVLYQDALLFSHLTVAGNI----- 99
Cdd:COG0488 20 SINPGDRIGLVGRNGAGKSTLLKILAGELEPD---SGEVSI--------PKGLR-IGYLPQEPPLDDDLTVLDTVldgda 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 ----------------AFAMPKGNKKQRLE-------------KIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRML 149
Cdd:COG0488 88 elraleaeleeleaklAEPDEDLERLAELQeefealggweaeaRAEEILSGLGFPeEDLDRPVSELSGGWRRRVALARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639318220 150 LSEPKAILLDEPFSKLDtqlrVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:COG0488 168 LSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-206 |
1.74e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQLYRQNElllSLNEQVNG-------GEILTIMGPSGSGKSS---LLNWLTGTLPSSFKANGEVwLNGQNI 70
Cdd:PRK13642 1 MNKILEVENLVFKYEKE---SDVNQLNGvsfsitkGEWVSIIGQNGSGKSTtarLIDGLFEEFEGKVKIDGEL-LTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 71 DNTPphlRHIGVLYQDA-LLFSHLTVAGNIAFAMPKGN--KKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLR 147
Cdd:PRK13642 77 WNLR---RKIGMVFQNPdNQFVGATVEDDVAFGMENQGipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 639318220 148 MLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLI 206
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILV 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-195 |
2.47e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLnGQNIdntpphlrHIGVLYQD-ALLF 90
Cdd:COG0488 325 YGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDS----GTVKL-GETV--------KIGYFDQHqEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 SHLTVAGNIAFAMPKGNKKQrlekIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtql 169
Cdd:COG0488 392 PDKTVLDELRDGAPGGTEQE----VRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD--- 464
|
170 180
....*....|....*....|....*.
gi 639318220 170 rVDTRELVFSQIRDHKLPAIMVTHDH 195
Cdd:COG0488 465 -IETLEALEEALDDFPGTVLLVSHDR 489
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-194 |
3.62e-16 |
|
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: 73.94 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 18 LLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSS-FKANGEVWLNGQNIDNTPPHLRHIGVLYQDAL-----LFS 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGlTQTSGEILLDGRPLLPLSIRGRHIATIMQNPRtafnpLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGNIAFAMPKGNKKQRlEKIAHALEQVGLKDMG---NRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQAR-ALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180
....*....|....*....|....*.
gi 639318220 169 LRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHD 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-189 |
3.84e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRHIGVLY---QDALLFSHL 93
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARLTPAKAHQLGIYlvpQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAMPKGNK-KQRLEKIAHALeQVGLKdmgnrhPDNLSG----GQQARVALLRMLLSEPKAILLDEPFSKLDTq 168
Cdd:PRK15439 102 SVKENILFGLPKRQAsMQKMKQLLAAL-GCQLD------LDSSAGslevADRQIVEILRGLMRDSRILILDEPTASLTP- 173
|
170 180 190
....*....|....*....|....*....|...
gi 639318220 169 lrVDTRELvFSQIR------------DHKLPAI 189
Cdd:PRK15439 174 --AETERL-FSRIRellaqgvgivfiSHKLPEI 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-206 |
3.85e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.33 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLY-RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG------TlpssfkaNGEVWLNGQNIDNTPPHL 77
Cdd:COG0396 1 LEIKNLHVSvEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyevT-------SGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 RH---IGVLYQDALLFSHLTVAGNIAFAMpkgNKKQR--------LEKIAHALEQVGL-KDMGNRH-PDNLSGGQQARVA 144
Cdd:COG0396 74 RAragIFLAFQYPVEIPGVSVSNFLRTAL---NARRGeelsarefLKLLKEKMKELGLdEDFLDRYvNEGFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639318220 145 LLRMLLSEPKAILLDEPFSKLDtqlrVDTRELV---FSQIRDHKLPAIMVTH-----DHSDADA----ANGKLI 206
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD----IDALRIVaegVNKLRSPDRGILIITHyqrilDYIKPDFvhvlVDGRIV 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-194 |
3.95e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPH----LR--HIGVLYQDAL--LFSHL 93
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPEKelnkLRaeQISMIFQDPMtsLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIA--FAMPKG-NKKQRLEKIAHALEQVGL----KDMgNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PRK09473 115 RVGEQLMevLMLHKGmSKAEAFEESVRMLDAVKMpearKRM-KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180
....*....|....*....|....*...
gi 639318220 167 TQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-190 |
4.74e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH--LRH-IGVLYQDALLFSHLTVAGNIA 100
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYqPDS----GEILIDGKPVRIRSPRdaIALgIGMVHQHFMLVPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 FAMPKG-----NKKQRLEKIAHALEQVGLK-DMgNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvDTR 174
Cdd:COG3845 103 LGLEPTkggrlDRKAARARIRELSERYGLDvDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ---EAD 178
|
170 180
....*....|....*....|....*...
gi 639318220 175 ELvFSQIRD------------HKLPAIM 190
Cdd:COG3845 179 EL-FEILRRlaaegksiifitHKLREVM 205
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-193 |
5.37e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.83 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTlPSSFKANGEVWLNGQNIDNTPPHLR-HIGVL--YQ-------- 85
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-PSYEVTSGTILFKGQDLLELEPDERaRAGLFlaFQypeeipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 86 DALLF------SHLTVAGNIAFAMPKGNKKqrLEKIAHALEQVGlkDMGNRH-PDNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:TIGR01978 93 SNLEFlrsalnARRSARGEEPLDLLDFEKL--LKEKLALLDMDE--EFLNRSvNEGFSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 639318220 159 DEPFSKLDtqlrVDTRELVFSQIRDHKLPA---IMVTH 193
Cdd:TIGR01978 169 DEIDSGLD----IDALKIVAEGINRLREPDrsfLIITH 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-194 |
6.81e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 32 LTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNI--DNTPPHLRHIGVLYQ--DALLFSHlTVAGNIAFAmpKG 106
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILkPTS----GSVLIRGEPItkENIREVRKFVGLVFQnpDDQIFSP-TVEQDIAFG--PI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 107 NKKQRLEKIAH----ALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIR 182
Cdd:PRK13652 106 NLGLDEETVAHrvssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170
....*....|..
gi 639318220 183 DHKLPAIMVTHD 194
Cdd:PRK13652 186 TYGMTVIFSTHQ 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-167 |
7.06e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 75.55 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTlpssFKA-NGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFShl 93
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF----FQArSGEILLNGFSLKDIDRHTlrQFINYLPQEPYIFS-- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 tvaGNIAFAMPKGNK-KQRLEKIAHALEQVGLKD------MG-----NRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:TIGR01193 562 ---GSILENLLLGAKeNVSQDEIWAACEIAEIKDdienmpLGyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*.
gi 639318220 162 FSKLDT 167
Cdd:TIGR01193 639 TSNLDT 644
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-206 |
8.27e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTP------PHLRHIGVLYQ--DALL 89
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQ----GSVRVDDTLITSTSknkdikQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFAmPK--GNKKQRLEKIA-HALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:PRK13649 99 FEE-TVLKDVAFG-PQnfGVSQEEAEALArEKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 639318220 166 DTQLRvdtREL--VFSQIRDHKLPAIMVTHDHSD-ADAAN-------GKLI 206
Cdd:PRK13649 177 DPKGR---KELmtLFKKLHQSGMTIVLVTHLMDDvANYADfvyvlekGKLV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
25-200 |
1.38e-15 |
|
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: 72.40 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH-LRHIGVLYQDALLFSHLTVAGNIAF- 101
Cdd:cd03266 27 TVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDA----GFATVDGFDVVKEPAEaRRRLGFVSDSTGLYDRLTARENLEYf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 ----AMPKGNKKQRLEKIAhalEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELV 177
Cdd:cd03266 103 aglyGLKGDELTARLEELA---DRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180
....*....|....*....|...
gi 639318220 178 fSQIRDHKLPAIMVTHDHSDADA 200
Cdd:cd03266 180 -RQLRALGKCILFSTHIMQEVER 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-168 |
2.01e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTgtlpsSFK--ANGEVWLNGQNI-DNTPPHLR-HIGVLYQDALLFSHlT 94
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLT-----RFYdiDEGEILLDGHDLrDYTLASLRnQVALVSQNVHLFND-T 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFAmpKGNKKQRLE-----KIAHALEQV-----GLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSK 164
Cdd:PRK11176 433 IANNIAYA--RTEQYSREQieeaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
....
gi 639318220 165 LDTQ 168
Cdd:PRK11176 511 LDTE 514
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-166 |
2.13e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkanGEVWLNGQNIDNTPphlrhigvLYQDALLFSHLTVAGN 98
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS----GSIQFAGQPLEAWS--------AAELARHRAYLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFAMP-------KGNKKQRLEKIAHAL----EQVGLKDMGNRHPDNLSGGQQARVALLRMLL-------SEPKAILLDE 160
Cdd:PRK03695 80 PPFAMPvfqyltlHQPDKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDE 159
|
....*.
gi 639318220 161 PFSKLD 166
Cdd:PRK03695 160 PMNSLD 165
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-194 |
2.52e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.53 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGtLPSSfkANGEVWLNGQNIDNTPPH-----LRHIGVLYQDAL--LFSHLTVAG 97
Cdd:TIGR02769 33 SIEEGETVGLLGRSGCGKSTLARLLLG-LEKP--AQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQDSPsaVNPRMTVRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFAM---PKGNKKQRLEKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDT 173
Cdd:TIGR02769 110 IIGEPLrhlTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVI 189
|
170 180
....*....|....*....|.
gi 639318220 174 RELVFSQIRDHKLPAIMVTHD 194
Cdd:TIGR02769 190 LELLRKLQQAFGTAYLFITHD 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-206 |
3.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNID------NTPPHLRHIGVLYQ--DALL 89
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSS----GTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFAmPKG---NKKQRLEKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:PRK13641 99 FEN-TVLKDVEFG-PKNfgfSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 639318220 166 DTQLRVDTRELvFSQIRDHKLPAIMVTHDHSD-ADAAN-------GKLI 206
Cdd:PRK13641 177 DPEGRKEMMQL-FKDYQKAGHTVILVTHNMDDvAEYADdvlvlehGKLI 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-198 |
4.86e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 31 ILTIMGPSGSGKSSLLNWLT--GTLPSSFKANGEVWLNGQNIDNTPPHL---RHIGVLYQDALLFShLTVAGNIaFAMPK 105
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNrmNDKVSGYRYSGDVLLGGRSIFNYRDVLefrRRVGMLFQRPNPFP-MSIMDNV-LAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 106 GNK---KQRLEKIAHA-LEQVGL----KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELV 177
Cdd:PRK14271 127 AHKlvpRKEFRGVAQArLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180
....*....|....*....|.
gi 639318220 178 FSqIRDhKLPAIMVTHDHSDA 198
Cdd:PRK14271 207 RS-LAD-RLTVIIVTHNLAQA 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-194 |
5.90e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.22 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLT--GTLPSSFKANGEVWLNGQNIDNTPPHL--- 77
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEgVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVRVEGRVEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 -RHIGVLYQDALLFShLTVAGNIAFAMPKGNKKQRLEK---IAHALEQVGL----KDMGNRHPDNLSGGQQARVALLRML 149
Cdd:PRK14258 87 rRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIddiVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639318220 150 LSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-194 |
7.13e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNID--NTPPHLRHIGVLYQDALLFSHLTVAGNIAF----- 101
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 --AMPKGNKKQRlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFS 179
Cdd:PRK10575 114 hgALGRFGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170
....*....|....*
gi 639318220 180 QIRDHKLPAIMVTHD 194
Cdd:PRK10575 193 LSQERGLTVIAVLHD 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-194 |
7.32e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTP-----PHLRHIGVLYQD--ALLFSHLTVAGNI-- 99
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQ---GGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpyASLDPRQTVGDSIme 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 ---AFAMPKGNKKQRleKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRE 175
Cdd:PRK10261 427 plrVHGLLPGKAAAA--RVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
170
....*....|....*....
gi 639318220 176 LVFSQIRDHKLPAIMVTHD 194
Cdd:PRK10261 505 LLLDLQRDFGIAYLFISHD 523
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-194 |
7.88e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKA-NGEVWLNGQNIdnTPPHLR- 78
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQtAGRVLLDGKPV--APCALRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 -HIGVLYQDAL-LFSHL-TVAGNIAFAMPKGNKKQRLEKIAHALEQVGLKDMG---NRHPDNLSGGQQARVALLRMLLSE 152
Cdd:PRK10418 79 rKIATIMQNPRsAFNPLhTMHTHARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 639318220 153 PKAILLDEPFSKLD--TQLRVdtRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK10418 159 APFIIADEPTTDLDvvAQARI--LDLLESIVQKRALGMLLVTHD 200
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-168 |
7.96e-15 |
|
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: 72.16 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLtgtlpssFKA----NGEVWLNGQNI-DNTPPHLR-HIGVLYQDALLFSHlTVAGNI 99
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLL-------FRFydvtSGRILIDGQDIrDVTQASLRaAIGIVPQDTVLFND-TIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 AFAMPKGNKkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:COG5265 453 AYGRPDASE----EEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-194 |
8.06e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFSHLTVAGNIAfaM 103
Cdd:PRK09536 26 VREGSLVGLVGPNGAGKTTLLRAINGTLTP---TAGTVLVAGDDVEALSARAasRRVASVPQDTSLSFEFDVRQVVE--M 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 PKGNKKQRLEK--------IAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRE 175
Cdd:PRK09536 101 GRTPHRSRFDTwtetdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLE 180
|
170
....*....|....*....
gi 639318220 176 LVFSQIRDHKlPAIMVTHD 194
Cdd:PRK09536 181 LVRRLVDDGK-TAVAAIHD 198
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-197 |
3.23e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.42 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPP--HLRHI----GVLYQ--D 86
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT---TGTVTVDDITITHKTKdkYIRPVrkriGMVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 87 ALLFSHlTVAGNIAFAmPKgNKKQRLEKI---AHAL-EQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK13646 96 SQLFED-TVEREIIFG-PK-NFKMNLDEVknyAHRLlMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 639318220 162 FSKLDTQLRVDTRELVFS-QIRDHKlPAIMVTHDHSD 197
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSlQTDENK-TIILVSHDMNE 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-193 |
3.98e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.49 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 30 EILTIMGPSGSGKSSLLNWLTGTLPSSFkanGEVWL----NGQNIDNTPPHLRH--------------IGVLYQ--DALL 89
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLIKSKY---GTIQVgdiyIGDKKNNHELITNPyskkiknfkelrrrVSMVFQfpEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFA-MPKGNKKQRL-EKIAHALEQVGLKD-MGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PRK13631 130 FKD-TIEKDIMFGpVALGVKKSEAkKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
170 180
....*....|....*....|....*..
gi 639318220 167 TQLRVDTRELVFSQIRDHKlPAIMVTH 193
Cdd:PRK13631 209 PKGEHEMMQLILDAKANNK-TVFVITH 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-196 |
5.12e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.22 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTgtL---PSSfkanGEVWLNGQNIDNTPPHLRH-----IGVLYQD--ALLFSHLTVaGN 98
Cdd:PRK11308 41 GKTLAVVGESGCGKSTLARLLT--MietPTG----GELYYQGQDLLKADPEAQKllrqkIQIVFQNpyGSLNPRKKV-GQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IaFAMP-----KGNKKQRLEKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVD 172
Cdd:PRK11308 114 I-LEEPllintSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQ 192
|
170 180
....*....|....*....|....
gi 639318220 173 TRELVFSQIRDHKLPAIMVTHDHS 196
Cdd:PRK11308 193 VLNLMMDLQQELGLSYVFISHDLS 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-190 |
5.79e-14 |
|
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: 69.97 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 10 CQLYRQN-ELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPH-LR-HIGVLYQ 85
Cdd:TIGR00957 1291 CLRYREDlDLVLRhINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES---AEGEIIIDGLNIAKIGLHdLRfKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 86 DALLFShltvaGNIAFAM-PKGNKKQrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEP 153
Cdd:TIGR00957 1368 DPVLFS-----GSLRMNLdPFSQYSD--EEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 639318220 154 KAILLDEPFSKLDtqlrVDTRELVFSQIRD-----------HKLPAIM 190
Cdd:TIGR00957 1441 KILVLDEATAAVD----LETDNLIQSTIRTqfedctvltiaHRLNTIM 1484
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-194 |
5.83e-14 |
|
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: 68.32 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNT---PPHLRHI-----GVLYQDAL--LFSHLTVAGN 98
Cdd:TIGR02323 29 GEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYqlsEAERRRLmrtewGFVHQNPRdgLRMRVSAGAN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IA-FAMPKGNKKQ-RLEKIAHA-LEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTR 174
Cdd:TIGR02323 109 IGeRLMAIGARHYgNIRATAQDwLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLL 188
|
170 180
....*....|....*....|
gi 639318220 175 ELVFSQIRDHKLPAIMVTHD 194
Cdd:TIGR02323 189 DLLRGLVRDLGLAVIIVTHD 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-195 |
7.14e-14 |
|
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: 65.93 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLnGQNIdntpphlrhigvl 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKdISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP---DEGIVTW-GSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 84 yqdallfshltvagniafampkgnkkqrleKIAHaLEQvglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:cd03221 64 ------------------------------KIGY-FEQ-------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|..
gi 639318220 164 KLDtqlrVDTRELVFSQIRDHKLPAIMVTHDH 195
Cdd:cd03221 100 HLD----LESIEALEEALKEYPGTVILVSHDR 127
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-193 |
8.67e-14 |
|
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: 66.30 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH--LRH-IGVLYQdallfshltvagnia 100
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILSGLYkPDS----GEILVDGKEVSFASPRdaRRAgIAMVYQ--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 101 fampkgnkkqrlekiahaleqvglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTRELVFSQ 180
Cdd:cd03216 83 ----------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT----PAEVERLFKV 124
|
170
....*....|....*.
gi 639318220 181 IRDHK---LPAIMVTH 193
Cdd:cd03216 125 IRRLRaqgVAVIFISH 140
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-206 |
1.11e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 14 RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANG-----EVWLNGQ---NIDntPPHL-RHIGVLY 84
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGarvtgDVTLNGEplaAID--APRLaRLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 85 QD---ALLFS--HLTVAGNIAFAMPKGNKKQRLEKIA-HALEQVGLKDMGNRHPDNLSGGQQARVALLRML--------- 149
Cdd:PRK13547 90 QAaqpAFAFSarEIVLLGRYPHARRAGALTHRDGEIAwQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 150 LSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD------HSDADA--ANGKLI 206
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDpnlaarHADRIAmlADGAIV 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
29-194 |
1.23e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSS-----FKANGEVWLNGQNIdnTPPHLRHI-----GVLYQDAL--LFSHLTVA 96
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDagevhYRMRDGQLRDLYAL--SEAERRRLlrtewGFVHQHPRdgLRMQVSAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 97 GNIA-FAMPKGNKK-QRL-EKIAHALEQVGLKdmGNR---HPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD--TQ 168
Cdd:PRK11701 110 GNIGeRLMAVGARHyGDIrATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQ 187
|
170 180
....*....|....*....|....*...
gi 639318220 169 LRV-D-TRELVfsqiRDHKLPAIMVTHD 194
Cdd:PRK11701 188 ARLlDlLRGLV----RELGLAVVIVTHD 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-194 |
1.34e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL--PSSFKANgEVWLNGQNIDNTPPHLRH------IGVLYQDAL--LFSHLT 94
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRVMAE-KLEFNGQDLQRISEKERRnlvgaeVAMIFQDPMtsLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFAMP---KGNKKQRLEKIAHALEQVGLKDMGNR---HPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:PRK11022 108 VGFQIMEAIKvhqGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT 187
|
170 180
....*....|....*....|....*.
gi 639318220 169 LRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK11022 188 IQAQIIELLLELQQKENMALVLITHD 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-197 |
1.40e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPS-SFKANGEVWLNgqNIDNTPPHLRHIGvlyqdallfshl 93
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtPVAGCVDVPDN--QFGREASLIDAIG------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 tvagniafamPKGNKKQRLEkiahALEQVGLKDMGN--RHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRV 171
Cdd:COG2401 108 ----------RKGDFKDAVE----LLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....*.
gi 639318220 172 DTRELVFSQIRDHKLPAIMVTHdHSD 197
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATH-HYD 198
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-171 |
1.44e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.83 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNI-DNTPPHLRH-IGVLYQDALLFSHlTVAGNIAFAMPK 105
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFdPQS----GRILIDGTDIrTVTRASLRRnIAVVFQDAGLFNR-SIEDNIRVGRPD 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 106 GNKKQRLE--KIAHALEQV-----GLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD--TQLRV 171
Cdd:PRK13657 436 ATDEEMRAaaERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDveTEAKV 510
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-189 |
1.48e-13 |
|
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: 66.73 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNI---DNTPPHlRHIGVLYQDALLFSHlTVAGNIAFAMPK 105
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLENFYQPQ---GGQVLLDGKPIsqyEHKYLH-SKVSLVGQEPVLFAR-SLQDNIAYGLQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 106 GNKKQRLE--KIAHA------LEQVGLKDMGNRHpDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELV 177
Cdd:cd03248 115 CSFECVKEaaQKAHAhsfiseLASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
170
....*....|..
gi 639318220 178 FSQIRDHKLPAI 189
Cdd:cd03248 194 YDWPERRTVLVI 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-196 |
1.76e-13 |
|
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: 65.64 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 18 LLLSLNEQVNGGEILTIMGPSGSGKSSLlnwltgtlpssFKANGEVWLNGQNIDNTPPHlrhigvlyqdallfshltvaG 97
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSL-----------FRALAGLWPWGSGRIGMPEG--------------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFA-----MPKGNKKqrlEKIAHALEQVglkdmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVD 172
Cdd:cd03223 65 DLLFLpqrpyLPLGTLR---EQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EE 125
|
170 180
....*....|....*....|....
gi 639318220 173 TRELVFSQIRDHKLPAIMVTHDHS 196
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPS 149
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-194 |
2.26e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 30 EILTIMGPSGSGKSSLLNWLTGTLPS----SFKANGEVWLNGQNIDNTPPHLRHIGVLYQ--DALLFSHlTVAGNIAFAm 103
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGLIISetgqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 P---KGNKKQRLEKIAHALEQVGL-KDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFS 179
Cdd:PRK13645 116 PvnlGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFER 195
|
170
....*....|....*
gi 639318220 180 QIRDHKLPAIMVTHD 194
Cdd:PRK13645 196 LNKEYKKRIIMVTHN 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-194 |
3.56e-13 |
|
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: 67.65 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 34 IMGPSGSGKSSLLNWLTGtLPSSFkaNGEVWLnGQNIDntpphlrhIGVLYQDALLFSHLTVAGNIAFAM-PKGNKKQRL 112
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAG-VDKDF--NGEARP-QPGIK--------VGYLPQEPQLDPTKTVRENVEEGVaEIKDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 113 EKIAHA---------------------LEQVGLKDMGN---------RHPD------NLSGGQQARVALLRMLLSEPKAI 156
Cdd:TIGR03719 104 NEISAKyaepdadfdklaaeqaelqeiIDAADAWDLDSqleiamdalRCPPwdadvtKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 639318220 157 LLDEPFSKLDTQlRVDTRElvfSQIRDHKLPAIMVTHD 194
Cdd:TIGR03719 184 LLDEPTNHLDAE-SVAWLE---RHLQEYPGTVVAVTHD 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-166 |
6.34e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQLYRQ--NELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGT-LPSsfkaNGEVWLNGQNID-NTPPH 76
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQ----RGRVKVMGREVNaENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 77 LR-HIGVLYQDA--LLFShLTVAGNIAFAmPKG---NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLL 150
Cdd:PRK13647 77 VRsKVGLVFQDPddQVFS-STVWDDVAFG-PVNmglDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170
....*....|....*.
gi 639318220 151 SEPKAILLDEPFSKLD 166
Cdd:PRK13647 155 MDPDVIVLDEPMAYLD 170
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-161 |
7.08e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDN--TPPHLRH-IGVLYQDALL 89
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT---SGRIVFDGKDITDwqTAKIMREaVAIVPEGRRV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 90 FSHLTVAGNIAFAMPKGNKKQRLEKIAHALEQVG-LKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK11614 92 FSRMTVEENLAMGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-183 |
8.56e-13 |
|
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: 63.99 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPH--LRHiGVLY-----QDALLFSHLTVAG 97
Cdd:cd03215 22 EVRAGEIVGIAGLVGNGQTELAEALFGLRP---PASGEITLDGKPVTRRSPRdaIRA-GIAYvpedrKREGLVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFampkgnkkqrlekiahaleqvglkdmgnrhPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTRELV 177
Cdd:cd03215 98 NIAL------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAKAEI 143
|
....*.
gi 639318220 178 FSQIRD 183
Cdd:cd03215 144 YRLIRE 149
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-166 |
8.80e-13 |
|
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: 64.21 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNID-NTPPHLRHIGVLYQDALLFSHLTVAGNIAFAmp 104
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKeFAEKYPGEIIYVSEEDVHFPTLTVRETLDFA-- 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639318220 105 kgnkkqrlekiahaleqvgLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:cd03233 108 -------------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-193 |
1.08e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 16 NELLLSLNEQVNGGEILTIMGPSGSGKSS----LLNWLTGTlpssfkaNGEVWLNGQNIDNTPPHL--RHIGVLYQDALL 89
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTvaalLQNLYQPT-------GGQVLLDGVPLVQYDHHYlhRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHlTVAGNIAFampkGNKKQRLEKIAHALEQVGLKDMGNRHPDN-----------LSGGQQARVALLRMLLSEPKAILL 158
Cdd:TIGR00958 567 FSG-SVRENIAY----GLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190
....*....|....*....|....*....|....*.
gi 639318220 159 DEPFSKLDTQLrvdtrELVFSQIRDHK-LPAIMVTH 193
Cdd:TIGR00958 642 DEATSALDAEC-----EQLLQESRSRAsRTVLLIAH 672
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-194 |
1.37e-12 |
|
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: 65.86 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKS----SLLnwltGTLPSSF-KANGEVWLNGQNIDNTPPH-LRH-----IGVLYQDAL--LFS 91
Cdd:COG4172 32 DIAAGETLALVGESGSGKSvtalSIL----RLLPDPAaHPSGSILFDGQDLLGLSEReLRRirgnrIAMIFQEPMtsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 92 HLTVAGNIA------FAMpkgNKKQRLEKIAHALEQVGLKDMGNR---HPDNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:COG4172 108 LHTIGKQIAevlrlhRGL---SGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
170 180 190
....*....|....*....|....*....|..
gi 639318220 163 SKLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:COG4172 185 TALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-193 |
1.85e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNG---QNIDNTPPHLRHIGVLYQ--DALLFSHLtV 95
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSE----GKVYVDGldtSDEENLWDIRNKAGMVFQnpDNQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGNIAFAmPKG---NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRvd 172
Cdd:PRK13633 104 EEDVAFG-PENlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR-- 180
|
170 180
....*....|....*....|....*
gi 639318220 173 tRElVFSQIRD----HKLPAIMVTH 193
Cdd:PRK13633 181 -RE-VVNTIKElnkkYGITIILITH 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-178 |
3.27e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 9 NCQLYRQNELLLSLNEqvngGEILTIMGPSGSGKSSLLNWLTGTLPSSFKanGEVWLNGQNIDNTPPH--LRH-IGVLYQ 85
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRR----GEILGVAGLVGAGRTELVQALFGAYPGKFE--GNVFINGKPVDIRNPAqaIRAgIAMVPE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 86 DAL---LFSHLTVAGNIAFAMPKG-------NKKQRLEKIAHALEQVGLKdmgNRHPD----NLSGGQQARVALLRMLLS 151
Cdd:TIGR02633 344 DRKrhgIVPILGVGKNITLSVLKSfcfkmriDAAAELQIIGSAIQRLKVK---TASPFlpigRLSGGNQQKAVLAKMLLT 420
|
170 180
....*....|....*....|....*..
gi 639318220 152 EPKAILLDEPFSKLDTQLRVDTRELVF 178
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLIN 447
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-202 |
3.90e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTP--PHLRHI-GVLYQDA-LLFSHLT 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ---KGKVLVSGIDTGDFSklQGIRKLvGIVFQNPeTQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFA-----MPKGNKKQRLEKiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTql 169
Cdd:PRK13644 95 VEEDLAFGpenlcLPPIEIRKRVDR---ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP-- 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 639318220 170 rvDTRELVFSQIRD-HKLPAIMV--THDHSDADAAN 202
Cdd:PRK13644 170 --DSGIAVLERIKKlHEKGKTIVyiTHNLEELHDAD 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-194 |
5.74e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 3 SSLQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNI-DNTPPHL-R 78
Cdd:PRK11231 1 MTLRTENLTVgYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQS----GTVFLGDKPIsMLSSRQLaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 HIGVLYQDALLFSHLTVAGNIAFAM-PKGNKKQRL-----EKIAHALEQVGLKDMGNRHPDNLSGGQQARvALLRMLLSE 152
Cdd:PRK11231 77 RLALLPQHHLTPEGITVRELVAYGRsPWLSLWGRLsaednARVNQAMEQTRINHLADRRLTDLSGGQRQR-AFLAMVLAQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 639318220 153 PKAI-LLDEPFSKLDTQLRVDTRELVfSQIRDHKLPAIMVTHD 194
Cdd:PRK11231 156 DTPVvLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHD 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-161 |
6.59e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPH--LRHiGVLY------QDALLFShLTVAG 97
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLYGALP---RTSGYVTLDGHEVVTRSPQdgLAN-GIVYisedrkRDGLVLG-MSVKE 349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 98 NIAF-AMPKGNKKqrLEKIAHALEQVGLKD---MGN-RHPD------NLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK10762 350 NMSLtALRYFSRA--GGSLKHADEQQAVSDfirLFNiKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-166 |
7.34e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNiDNTPPHLRHIGVLYQDALLFSHLTVAGNIAF 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE---SGQIQIDGKT-ATRGDRSRFMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639318220 102 AMP-KGNKKQRLEkiAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PRK13543 106 LCGlHGRRAKQMP--GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-194 |
7.59e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNG--------QNIDNTPPHLRHIG----VLYQDALLFSH 92
Cdd:PRK15056 29 TVPGGSIAALVGVNGSGKSTLFKALMGFVRL---ASGKISILGqptrqalqKNLVAYVPQSEEVDwsfpVLVEDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LtvaGNIAFA-MPKGNKKQRLEKiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRV 171
Cdd:PRK15056 106 Y---GHMGWLrRAKKRDRQIVTA---ALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|...
gi 639318220 172 DTRELVfSQIRDHKLPAIMVTHD 194
Cdd:PRK15056 180 RIISLL-RELRDEGKTMLVSTHN 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-166 |
1.14e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 34 IMGPSGSGKSSLLNWLTGtLPSSFkaNGEVWLNgqnidntpPHLRhIGVLYQDALLFSHLTVAGNIAFAM-PKGNKKQRL 112
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAG-VDKEF--EGEARPA--------PGIK-VGYLPQEPQLDPEKTVRENVEEGVaEVKAALDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 113 EKIAHA---------------------LEQVGLKDMGN---------RHPD------NLSGGQQARVALLRMLLSEPKAI 156
Cdd:PRK11819 106 NEIYAAyaepdadfdalaaeqgelqeiIDAADAWDLDSqleiamdalRCPPwdakvtKLSGGERRRVALCRLLLEKPDML 185
|
170
....*....|
gi 639318220 157 LLDEPFSKLD 166
Cdd:PRK11819 186 LLDEPTNHLD 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-170 |
1.27e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIDNTPPHLR-HIGVLYQDALLFSHLTVAGNI 99
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDA----GSISLCGEPVPSRARHARqRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639318220 100 A-----FAMPKGNKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLR 170
Cdd:PRK13537 102 LvfgryFGLSAAAARALVPPL---LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
29-192 |
2.14e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLR--HIGVLYQDAL--LFSHLTVAGNIAFAM- 103
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPT---SGELLIDDHPLHFGDYSYRsqRIRMIFQDPStsLNPRQRISQILDFPLr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 --PKGNKKQRLEKIAHALEQVGLK-DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQ 180
Cdd:PRK15112 116 lnTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
170
....*....|..
gi 639318220 181 IRDHKLPAIMVT 192
Cdd:PRK15112 196 QEKQGISYIYVT 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-200 |
2.29e-11 |
|
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: 60.91 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 1 MQSSLQIKNCQ----LYRQNELLLS----LNEQVNGGEILTIMGPSGSGKSSLLNWLTGT-LPSSfkanGEVWLN--GQN 69
Cdd:COG4778 1 MTTLLEVENLSktftLHLQGGKRLPvldgVSFSVAAGECVALTGPSGAGKSTLLKCIYGNyLPDS----GSILVRhdGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 70 ID--NTPPH----LR--HIGVLYQdallF-------SHLTVAGNIAFAMpkGNKKQR-LEKIAHALEQVGLkdmgnrhPD 133
Cdd:COG4778 77 VDlaQASPReilaLRrrTIGYVSQ----FlrviprvSALDVVAEPLLER--GVDREEaRARARELLARLNL-------PE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 134 NL--------SGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvdTRELVFSQIRDHKlpA-----IMVTHDHSDADA 200
Cdd:COG4778 144 RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAA----NRAVVVELIEEAK--ArgtaiIGIFHDEEVREA 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
38-185 |
2.71e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 38 SGSGKSSLLnwltgtlpssFKANGEVWLNGQNI-DNTPPHLRHI-GVLYQDALLFShLTVAGNIAFAMPKGNKK--QRLE 113
Cdd:PTZ00265 1264 GGSGEDSTV----------FKNSGKILLDGVDIcDYNLKDLRNLfSIVSQEPMLFN-MSIYENIKFGKEDATREdvKRAC 1332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639318220 114 KIAhALEQVgLKDMGNRHPDN-------LSGGQQARVALLRMLLSEPKAILLDEPFSKLDTqlrvDTRELVFSQIRDHK 185
Cdd:PTZ00265 1333 KFA-AIDEF-IESLPNKYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDS----NSEKLIEKTIVDIK 1405
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-193 |
3.36e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHLRH---IGVLYQDALLFSHLTV 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNINYNKLDHKLAAqlgIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGNI---------AFAMPKGNKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLd 166
Cdd:PRK09700 98 LENLyigrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL- 176
|
170 180
....*....|....*....|....*..
gi 639318220 167 TQLRVDTRELVFSQIRDHKLPAIMVTH 193
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-187 |
4.26e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLnwltGTLPSSFK-ANGEVWLNgqnidntpphlRHIGVLYQDALLFShLTV 95
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLL----QSLLSQFEiSEGRVWAE-----------RSIAYVPQQAWIMN-ATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 96 AGNIAFAMPKgnKKQRLEK-------------IAHALE-QVGLKDMgnrhpdNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PTZ00243 738 RGNILFFDEE--DAARLADavrvsqleadlaqLGGGLEtEIGEKGV------NLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190
....*....|....*....|....*....|....*....
gi 639318220 162 FSKLDTQ-------------LRVDTRELVFSQIrdHKLP 187
Cdd:PTZ00243 810 LSALDAHvgervveecflgaLAGKTRVLATHQV--HVVP 846
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-193 |
5.32e-11 |
|
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: 59.65 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPHLRHIGVLY------QDALLFSh 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVHWSNKNESEPSFEATRSRNRYsvayaaQKPWLLN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 LTVAGNIAFAMPkgNKKQRLEKIAHA---------LEQVGLKDMGNRHPdNLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:cd03290 93 ATVEENITFGSP--FNKQRYKAVTDAcslqpdidlLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 164 KLDTQLRVD-TRELVFSQIRDHKLPAIMVTH 193
Cdd:cd03290 170 ALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-161 |
1.13e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSsfKANGEVWLNGQNID-NTPPH-LRH-IGVLYQDAL---LFSHLTVAGNIAFA 102
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPG--RWEGEIFIDGKPVKiRNPQQaIAQgIAMVPEDRKrdgIVPVMGVGKNITLA 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639318220 103 MPKgnKKQRLEKIAHALEQVGLKDMGNR------HPD----NLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK13549 366 ALD--RFTGGSRIDDAAELKTILESIQRlkvktaSPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-161 |
1.13e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPH--LRHiGVLY------QDALlFSHLTVA 96
Cdd:COG1129 274 SVRAGEILGIAGLVGAGRTELARALFGADP---ADSGEIRLDGKPVRIRSPRdaIRA-GIAYvpedrkGEGL-VLDLSIR 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 97 GNIAFAMPKG-------NKKQRLEKIAHALEQVGLKDMGNRHP-DNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:COG1129 349 ENITLASLDRlsrggllDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-194 |
1.86e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfKANGEVWLNGQnidntpphlrhigVLY--QDALLFShLTVA 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVVIRGT-------------VAYvpQVSWIFN-ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 97 GNIAFAMP----KGNKKQRLEKIAHALEQV---GLKDMGNRHPdNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ- 168
Cdd:PLN03130 697 DNILFGSPfdpeRYERAIDVTALQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHv 775
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639318220 169 ------------LRVDTRELVFSQIrdHKLPA---IMVTHD 194
Cdd:PLN03130 776 grqvfdkcikdeLRGKTRVLVTNQL--HFLSQvdrIILVHE 814
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-194 |
2.58e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGtLPSSfkANGEVWLNGQNID--NTPPH---LRHIGVLYQDAL--LFSHLTVAG 97
Cdd:PRK10419 34 SLKSGETVALLGRSGCGKSTLARLLVG-LESP--SQGNVSWRGEPLAklNRAQRkafRRDIQMVFQDSIsaVNPRKTVRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFAM---PKGNKKQRLEKIAHALEQVGLKD-MGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDT 173
Cdd:PRK10419 111 IIREPLrhlLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
170 180
....*....|....*....|.
gi 639318220 174 RELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK10419 191 IRLLKKLQQQFGTACLFITHD 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-193 |
3.56e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGT---LPSSfkanGEV-----------WLNGQNIDNTPPHL----- 77
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTS----GRIiyhvalcekcgYVERPSKVGEPCPVcggtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 -------------------RHIGVLYQDAL-LFSHLTVAGNIAFAMPKGNKKQRlEKIAHALEQVGLKDMGNR--H-PDN 134
Cdd:TIGR03269 90 epeevdfwnlsdklrrrirKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGK-EAVGRAVDLIEMVQLSHRitHiARD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 135 LSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvdTRELVFSQIR----DHKLPAIMVTH 193
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ----TAKLVHNALEeavkASGISMVLTSH 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-167 |
4.61e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLS-LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIdNTPPH--LR-HIGVLYQDAL 88
Cdd:PRK10790 350 YRDDNLVLQnINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRPL-SSLSHsvLRqGVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 89 LFSHlTVAGNIAFAMPKGNkkqrlEKIAHALEQVGLKDMGNRHPD-----------NLSGGQQARVALLRMLLSEPKAIL 157
Cdd:PRK10790 426 VLAD-TFLANVTLGRDISE-----EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILI 499
|
170
....*....|
gi 639318220 158 LDEPFSKLDT 167
Cdd:PRK10790 500 LDEATANIDS 509
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-195 |
5.09e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 56.65 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQL-YRQN--ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPH-LRH 79
Cdd:cd03369 6 EIEVENLSVrYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE---EGKIEIDGIDISTIPLEdLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 -IGVLYQDALLFSHlTVAGNIAfamPKGnkKQRLEKIAHALEqvgLKDMGNrhpdNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:cd03369 83 sLTIIPQDPTLFSG-TIRSNLD---PFD--EYSDEEIYGALR---VSEGGL----NLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 639318220 159 DEPFSKLDtqlrVDTRELVFSQIRDHKLPAIMVTHDH 195
Cdd:cd03369 150 DEATASID----YATDALIQKTIREEFTNSTILTIAH 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-183 |
5.18e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGT-LPSSfkanGEVWLNGQ--NIDNTPPHLRH-IGVLYQDALLFSHLTVAGNIAF 101
Cdd:PRK11288 27 CRAGQVHALMGENGAGKSTLLKILSGNyQPDA----GSILIDGQemRFASTTAALAAgVAIIYQELHLVPEMTVAENLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 -AMP-KGNKKQRLEKIAHALEQvgLKDMGNR-HPD----NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvDTR 174
Cdd:PRK11288 103 gQLPhKGGIVNRRLLNYEAREQ--LEHLGVDiDPDtplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR---EIE 177
|
....*....
gi 639318220 175 ELvFSQIRD 183
Cdd:PRK11288 178 QL-FRVIRE 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-194 |
5.20e-10 |
|
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: 57.38 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLpssfKANGEVWLNGQNIDNTPPHLRhiGVLYQDalLFSHL--------------- 93
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKL----KPNLGKFDDPPDWDEILDEFR--GSELQN--YFTKLlegdvkvivkpqyvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 ----TVAGNIAFAMPKGNKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:cd03236 98 lipkAVKGKVGELLKKKDERGKLDEL---VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*
gi 639318220 170 RVDTRELVFSQIRDHKlPAIMVTHD 194
Cdd:cd03236 175 RLNAARLIRELAEDDN-YVLVVEHD 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-194 |
5.66e-10 |
|
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: 57.03 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPphlRHIGVLYQ---DALLFSHLTVAGNIAFA 102
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPD---EGDIEIELDTVSYKP---QYIKADYEgtvRDLLSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 103 MPKGNKKQRLEKIahaleqvglkdMGNRHPDnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIR 182
Cdd:cd03237 96 KTEIAKPLQIEQI-----------LDREVPE-LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170
....*....|..
gi 639318220 183 DHKLPAIMVTHD 194
Cdd:cd03237 164 NNEKTAFVVEHD 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-193 |
6.49e-10 |
|
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: 57.91 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfKANGEVWLNGQNIDNTppHLRH-----IGVLYQDALLFSHLTVAGNI 99
Cdd:TIGR02633 23 EVRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPLKAS--NIRDteragIVIIHQELTLVPELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 100 ----AFAMPKG--NKKQRLEKIAHALEQVGLKDMGNRHP-DNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlrvd 172
Cdd:TIGR02633 100 flgnEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK---- 175
|
170 180
....*....|....*....|....
gi 639318220 173 TRELVFSQIRD---HKLPAIMVTH 193
Cdd:TIGR02633 176 ETEILLDIIRDlkaHGVACVYISH 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-166 |
6.66e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPH------LRHIGVLYQDALLFSHLTVAGN 98
Cdd:PRK09700 285 SVCRGEILGFAGLVGSGRTELMNCLFGVDK---RAGGEIRLNGKDISPRSPLdavkkgMAYITESRRDNGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFA--MPKGNKKQRLEKIAHALEQ---------VGLKDMG-NRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PRK09700 362 MAISrsLKDGGYKGAMGLFHEVDEQrtaenqrelLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-168 |
7.05e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIdntpPHLR------HIGVLYQDAL 88
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS---EGDIRFHDIPL----TKLQldswrsRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 89 LFSHlTVAGNIAFAMPKGNKKQrLEKIAHA---------LEQVGLKDMGNRHPdNLSGGQQARVALLRMLLSEPKAILLD 159
Cdd:PRK10789 400 LFSD-TVANNIALGRPDATQQE-IEHVARLasvhddilrLPQGYDTEVGERGV-MLSGGQKQRISIARALLLNAEILILD 476
|
....*....
gi 639318220 160 EPFSKLDTQ 168
Cdd:PRK10789 477 DALSAVDGR 485
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-166 |
1.49e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDntpPH----LRHIGVLYQDALLFSHLTVAGNIA---- 100
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVD---AGdiatRRRVGYMSQAFSLYGELTVRQNLElhar 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 101 -FAMPKGNKKQRlekIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:NF033858 366 lFHLPAAEIAAR---VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-185 |
1.73e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPphlrhigVLYQDALLF- 90
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEK----GEILFERQSIKKDL-------CTYQKQLCFv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 -------SHLTVAGNIAFAMPKGNKKQ------RLEKIAHALE-QVGLkdmgnrhpdnLSGGQQARVALLRMLLSEPKAI 156
Cdd:PRK13540 80 ghrsginPYLTLRENCLYDIHFSPGAVgitelcRLFSLEHLIDyPCGL----------LSSGQKRQVALLRLWMSKAKLW 149
|
170 180
....*....|....*....|....*....
gi 639318220 157 LLDEPFSKLDTQlrvdTRELVFSQIRDHK 185
Cdd:PRK13540 150 LLDEPLVALDEL----SLLTIITKIQEHR 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-209 |
4.19e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNIDNTPPH--LRHIGVLYQDALLFSHLtvagniafaMPK 105
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYqPQS----GEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQL---------LGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 106 GNKKQRLEKIAHALEQVGLKD----MGNRHPD-NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQ 180
Cdd:PRK10522 416 EGKPANPALVEKWLERLKMAHklelEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 639318220 181 IRDHKLPAIMVTHD-----HSDA--DAANGKLITLS 209
Cdd:PRK10522 496 LQEMGKTIFAISHDdhyfiHADRllEMRNGQLSELT 531
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-168 |
4.25e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPhlRHIGVLYQDALLFSHLTVAGNIAFA------ 102
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQ--RSIGYVQQQDLHLPTSTVRESLRFSaylrqp 866
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639318220 103 --MPKGNKKQRLEKIAHALEQ-------VGLKDMGnrhpdnLSGGQQARVALLRMLLSEPKAIL-LDEPFSKLDTQ 168
Cdd:TIGR00956 867 ksVSKSEKMEYVEEVIKLLEMesyadavVGVPGEG------LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-193 |
5.97e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQL-YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFkANGEVWLNGQNIDNTPPHLRH---I 80
Cdd:PRK09580 2 LSIKDLHVsVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-TGGTVEFKGKDLLELSPEDRAgegI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 81 GVLYQDAL--------LFshLTVAGNiafAMPKGNKKQRLEKIAHA---LEQVGLKDMgnrhPDNL---------SGGQQ 140
Cdd:PRK09580 81 FMAFQYPVeipgvsnqFF--LQTALN---AVRSYRGQEPLDRFDFQdlmEEKIALLKM----PEDLltrsvnvgfSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 639318220 141 ARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTRELV---FSQIRDHKLPAIMVTH 193
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLD----IDALKIVadgVNSLRDGKRSFIIVTH 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-179 |
8.06e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPHLR-HIGVLY-----QDALLF----- 90
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRP---ARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 91 ----SHLTVaGNIAFAMPKGNKKQRLEKIAHALeqvGLKDMGNRHP-DNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:PRK15439 359 awnvCALTH-NRRGFWIKPARENAVLERYRRAL---NIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170
....*....|....
gi 639318220 166 DTQLRVDTRELVFS 179
Cdd:PRK15439 435 DVSARNDIYQLIRS 448
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-194 |
8.18e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSFKANgevwlngqnidnTPPHLRhIGV----LYQDALL 89
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIK------------RNGKLR-IGYvpqkLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 fsHLTVAgniAFAMPKGNKKQrlEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQL 169
Cdd:PRK09544 83 --PLTVN---RFLRLRPGTKK--EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*.
gi 639318220 170 RVDTRELVfSQIRDHKLPAI-MVTHD 194
Cdd:PRK09544 156 QVALYDLI-DQLRRELDCAVlMVSHD 180
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-160 |
9.03e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.42 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGtL--PSSfkanGEVWLNGQNID--NTPPHLRHIGVLYQDALLFSHLTVAGNIAFAmp 104
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTG-LyrPES----GEILLDGQPVTadNREAYRQLFSAVFSDFHLFDRLLGLDGEADP-- 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639318220 105 kgnkkqrlEKIAHALEQVGLKD----MGNRHPD-NLSGGQQARVALLRMLLsEPKAIL-LDE 160
Cdd:COG4615 431 --------ARARELLERLELDHkvsvEDGRFSTtDLSQGQRKRLALLVALL-EDRPILvFDE 483
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-182 |
9.44e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.07 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGQNIdntPPHLR----HIGVLYQDA 87
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGmTSPDA----GKITVLGVPV---PARARlaraRIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 88 LLFSHLTVAGN-IAFAMPKGNKKQRLEK-IAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:PRK13536 124 NLDLEFTVRENlLVFGRYFGMSTREIEAvIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170
....*....|....*..
gi 639318220 166 DTQlrvdTRELVFSQIR 182
Cdd:PRK13536 204 DPH----ARHLIWERLR 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-166 |
1.04e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 16 NELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLpssfKANGEVWLNGQNIDNTPPH--LRHIGVLYQDALLFSHl 93
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL----NTEGDIQIDGVSWNSVPLQkwRKAFGVIPQKVFIFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAfamPKGNKKQrlEKIAHALEQVGLKDMGNRHPDN-----------LSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:cd03289 92 TFRKNLD---PYGKWSD--EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
....
gi 639318220 163 SKLD 166
Cdd:cd03289 167 AHLD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-166 |
1.04e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 16 NELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkaNGEVWLNGQNIDNTPPHL--RHIGVLYQDALLFSHl 93
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST----EGEIQIDGVSWNSVTLQTwrKAFGVIPQKVFIFSG- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIafampKGNKKQRLEKIAHALEQVGLKDMGNRHPDN-----------LSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:TIGR01271 1307 TFRKNL-----DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 639318220 163 SKLD 166
Cdd:TIGR01271 1382 AHLD 1385
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-193 |
1.53e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTLPS-SFKanGEVWLNGQ-----NIDNTppHLRHIGVLYQDALLFSHLTVAGN 98
Cdd:PRK13549 27 KVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgTYE--GEIIFEGEelqasNIRDT--ERAGIAIIHQELALVKELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFA---MPKG-----NKKQRLEKIahaLEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQlr 170
Cdd:PRK13549 103 IFLGneiTPGGimdydAMYLRAQKL---LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTES-- 177
|
170 180
....*....|....*....|....*
gi 639318220 171 vDTREL--VFSQIRDHKLPAIMVTH 193
Cdd:PRK13549 178 -ETAVLldIIRDLKAHGIACIYISH 201
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
5-181 |
1.87e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTP-PHLRHIGvl 83
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS---SGNIYYKNCNINNIAkPYCTYIG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 84 yQDALLFSHLTVAGNIAFAMPKGNKkqrLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEpfs 163
Cdd:PRK13541 77 -HNLGLKLEMTVFENLKFWSEIYNS---AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE--- 149
|
170
....*....|....*...
gi 639318220 164 kLDTQLRVDTRELVFSQI 181
Cdd:PRK13541 150 -VETNLSKENRDLLNNLI 166
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-166 |
2.56e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLneQVNGGEILTIMGPSGSGKS----SLLNWLTgTLPSSFKAnGEVWLNGQNIDNTP-PHLRHI-GvlYQDALLFSHL 93
Cdd:PRK15134 28 VSL--QIEAGETLALVGESGSGKSvtalSILRLLP-SPPVVYPS-GDIRFHGESLLHASeQTLRGVrG--NKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAMPK----------GNKKQ--RLEkIAHALEQVGLKDMGNR---HPDNLSGGQQARVALLRMLLSEPKAILL 158
Cdd:PRK15134 102 MVSLNPLHTLEKqlyevlslhrGMRREaaRGE-ILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
....*...
gi 639318220 159 DEPFSKLD 166
Cdd:PRK15134 181 DEPTTALD 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-183 |
3.44e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLneQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSsfkANGEVWLNGQNIDNTPPH-LRHIGVLY--QDAL---LFSHL 93
Cdd:COG3845 277 VSL--EVRAGEILGIAGVAGNGQSELAEALAGLRPP---ASGSIRLDGEDITGLSPReRRRLGVAYipEDRLgrgLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIAFAMPKGNKKQR-----LEKI-AHALEQVglKDMGNRHPD------NLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:COG3845 352 SVAENLILGRYRRPPFSRggfldRKAIrAFAEELI--EEFDVRTPGpdtparSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180
....*....|....*....|..
gi 639318220 162 FSKLDtqlrVDTRELVFSQIRD 183
Cdd:COG3845 430 TRGLD----VGAIEFIHQRLLE 447
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-176 |
3.45e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 3 SSLQIKNCQLYRQNELLLSLNE-QVNGGEILTIMGPSGSGKSSLLNWLTGTLP-------SSF------------KANGE 62
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLQLPSlTLNAGDSWAFVGANGSGKSALARALAGELPllsgerqSQFshitrlsfeqlqKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 63 VWLNgQNIDNTPPHLRHIGVLYQDALLFSHltvagniafampkgNKKQRLEKIAhalEQVGLKDMGNRHPDNLSGGQQAR 142
Cdd:PRK10938 82 EWQR-NNTDMLSPGEDDTGRTTAEIIQDEV--------------KDPARCEQLA---QQFGITALLDRRFKYLSTGETRK 143
|
170 180 190
....*....|....*....|....*....|....
gi 639318220 143 VALLRMLLSEPKAILLDEPFSKLDTQLRVDTREL 176
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-194 |
5.05e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKS----SLLNWL--TGTLPSSfkanGEVWL---NGQNID---NTPPHLRH-----IGVLYQDAL--L 89
Cdd:PRK10261 42 GETLAIVGESGSGKSvtalALMRLLeqAGGLVQC----DKMLLrrrSRQVIElseQSAAQMRHvrgadMAMIFQEPMtsL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHLTVAGNIAFAMPKGNKKQRLEKIAHA---LEQVGLKD---MGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:PRK10261 118 NPVFTVGEQIAESIRLHQGASREEAMVEAkrmLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTT 197
|
170 180 190
....*....|....*....|....*....|.
gi 639318220 164 KLDTQLRVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK10261 198 ALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
111-196 |
5.55e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 111 RLE-KIAHALEQVGLkdmgnrHPD----NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTRELVFSQIRDHK 185
Cdd:PRK11147 134 QLEnRINEVLAQLGL------DPDaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQ 203
|
90
....*....|.
gi 639318220 186 LPAIMVTHDHS 196
Cdd:PRK11147 204 GSIIFISHDRS 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-169 |
6.34e-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: 52.26 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 19 LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQnidntpphlrhIGVLYQDALLfSHLTVAGN 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD---KVEGHVHMKGS-----------VAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 IAFAMPKGNKKQRLEKIAHALeqvgLKDM-----GNRHPD-----NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACAL----LPDLeilpsGDRTEIgekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
.
gi 639318220 169 L 169
Cdd:TIGR00957 795 V 795
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-197 |
6.48e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNGQNI-DNTPPHLRHIGVLY-QDALL 89
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvPTS----GEVRVLGYVPfKRRKEFARRIGVVFgQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHLTVA------GNIaFAMPKGNKKQRLEKIAHALEqvgLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFS 163
Cdd:COG4586 108 WWDLPAIdsfrllKAI-YRIPDAEYKKRLDELVELLD---LGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 639318220 164 KLD--TQLRVdtRELVFSQIRDHKLPAIMVTHDHSD 197
Cdd:COG4586 184 GLDvvSKEAI--REFLKEYNRERGTTILLTSHDMDD 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-167 |
7.97e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 18 LLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKA-NGEVWLNGQNIDNTPPHLRHiGVLY--QDALLFSHLT 94
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGvEGVITYDGITPEEIKKHYRG-DVVYnaETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFAM--------PKG-NKKQRLEKIAH-ALEQVGL---KD--MGNRHPDNLSGGQQARVALLRMLLSEPKAILLD 159
Cdd:TIGR00956 155 VGETLDFAArcktpqnrPDGvSREEYAKHIADvYMATYGLshtRNtkVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWD 234
|
....*...
gi 639318220 160 EPFSKLDT 167
Cdd:TIGR00956 235 NATRGLDS 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-185 |
9.78e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 21 SLNeqVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNID-NTPPHLRH--IGVLYQDALLFSHLTVAG 97
Cdd:PRK10762 24 ALN--VYPGRVMALVGENGAGKSTMMKVLTGIYT---RDAGSILYLGKEVTfNGPKSSQEagIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAFAMPKGNK------KQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL-DTQlr 170
Cdd:PRK10762 99 NIFLGREFVNRfgridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE-- 176
|
170
....*....|....*
gi 639318220 171 vdTRELvFSQIRDHK 185
Cdd:PRK10762 177 --TESL-FRVIRELK 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-194 |
1.05e-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: 51.32 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL-PssfkangevwlNGQNIDNTPPH---LRHigvlYQDALLFSHLT--VAGNIAFA 102
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELkP-----------NLGDYDEEPSWdevLKR----FRGTELQDYFKklANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 103 M--------P---KGNKKQRLEKI------AHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKL 165
Cdd:COG1245 164 HkpqyvdliPkvfKGTVRELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*....
gi 639318220 166 DTQLRVDTRELVFSQIRDHKlPAIMVTHD 194
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGK-YVLVVEHD 271
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-166 |
1.68e-07 |
|
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: 50.24 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 16 NELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSS--FKANGEVWLNGQNIDNTPPHLRH---IGVLYQDall 89
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELePSEgkIKHSGRISFSSQFSWIMPGTIKEniiFGVSYDE--- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 90 FSHLTVAgniafampkgnKKQRLEKIAHALEQVGLKDMGNRHPdNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:cd03291 127 YRYKSVV-----------KACQLEEDITKFPEKDNTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-196 |
2.64e-07 |
|
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: 50.13 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 18 LLLSLNEQVNGGEILTIMGPSGSGKSSLlnwltgtlpssFKANGEVW-LNGqnidntpphlrhiGVLYQDAL-------- 88
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSL-----------FRILGELWpVYG-------------GRLTKPAKgklfyvpq 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 89 --LFSHLTVAGNIAFAMP------KGNKKQRLEKIahaLEQVGLKDMGNRH---------PDNLSGGQQARVALLRMLLS 151
Cdd:TIGR00954 523 rpYMTLGTLRDQIIYPDSsedmkrRGLSDKDLEQI---LDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639318220 152 EPKAILLDEPFSKLDtqlrVDTRELVFSQIRDHKLPAIMVTHDHS 196
Cdd:TIGR00954 600 KPQFAILDECTSAVS----VDVEGYMYRLCREFGITLFSVSHRKS 640
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-200 |
2.66e-07 |
|
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: 50.40 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGtlpSSFKANGEVWLNGQNI-DNTPPHLRHIGVLYQ----DALLF--SHLTVagn 98
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSIlTNISDVHQNMGYCPQfdaiDDLLTgrEHLYL--- 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 99 iaFAMPKGNKKQRLEKIAH-ALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELV 177
Cdd:TIGR01257 2036 --YARLRGVPAEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|...
gi 639318220 178 FSQIRDHKlPAIMVTHDHSDADA 200
Cdd:TIGR01257 2114 VSIIREGR-AVVLTSHSMEECEA 2135
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-183 |
6.66e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQL-YRQN--ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLtgtlpssFK----ANGEVWLNGQNIDNTP-P 75
Cdd:PLN03130 1237 SIKFEDVVLrYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNAL-------FRivelERGRILIDGCDISKFGlM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 76 HLRHI-GVLYQDALLFShltvaGNIAFAMPKGNKKQRLEkIAHALEQVGLKDMGNRHP-----------DNLSGGQQARV 143
Cdd:PLN03130 1310 DLRKVlGIIPQAPVLFS-----GTVRFNLDPFNEHNDAD-LWESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLL 1383
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 144 ALLRMLLSEPKAILLDEPFSKLDtqlrVDTRELVFSQIRD 183
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD----VRTDALIQKTIRE 1419
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-189 |
7.07e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 15 QNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANgeVWLNGQnidntpphlrhIGVLYQDALLFShLT 94
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSS--VVIRGS-----------VAYVPQVSWIFN-AT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 95 VAGNIAFAmpkgnKKQRLEKIAHALEQVGLK------------DMGNRHPdNLSGGQQARVALLRMLLSEPKAILLDEPF 162
Cdd:PLN03232 695 VRENILFG-----SDFESERYWRAIDVTALQhdldllpgrdltEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639318220 163 SKLDT-------------QLRVDTRELVFSQIrdHKLPAI 189
Cdd:PLN03232 769 SALDAhvahqvfdscmkdELKGKTRVLVTNQL--HFLPLM 806
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-171 |
7.20e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLNEqvngGEILTIMGPSGSGKSSLLNWLTGTLPSSFKANGE-VWLNGQNIDNTPPHLRH------IGVLYQDALlfSH 92
Cdd:COG4170 28 LTLNE----GEIRGLVGESGSGKSLIAKAICGITKDNWHVTADrFRWNGIDLLKLSPRERRkiigreIAMIFQEPS--SC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 93 L----TVAGNIAFAMP----KGN----KKQRLEKIAHALEQVGLKD---MGNRHPDNLSGGQQARVALLRMLLSEPKAIL 157
Cdd:COG4170 102 LdpsaKIGDQLIEAIPswtfKGKwwqrFKWRKKRAIELLHRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170
....*....|....*.
gi 639318220 158 LDEPFSKLD--TQLRV 171
Cdd:COG4170 182 ADEPTNAMEstTQAQI 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-198 |
8.28e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSF----------KANGE-VWlngqNIDntpphlRHIG 81
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYsndltlfgrrRGSGEtIW----DIK------KHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 82 vlYQDALLfsHL-----TVAGNI---AFAMPKGNKKQ---RLEKIAHA-LEQVGL-KDMGNRHPDNLSGGQQARVALLRM 148
Cdd:PRK10938 340 --YVSSSL--HLdyrvsTSVRNVilsGFFDSIGIYQAvsdRQQKLAQQwLDILGIdKRTADAPFHSLSWGQQRLALIVRA 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 639318220 149 LLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDA 198
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-166 |
8.35e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 18 LLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSS---FKANGEVWLNGQNIDNTPPHLRH---IGVLYQDallFS 91
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkIKHSGRISFSPQTSWIMPGTIKDniiFGLSYDE---YR 517
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 92 HLTVAgniafampkgNKKQRLEKIAHALEQ--VGLKDMGNrhpdNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:TIGR01271 518 YTSVI----------KACQLEEDIALFPEKdkTVLGEGGI----TLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-168 |
1.34e-06 |
|
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: 46.85 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 17 ELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfKANGEVWLNGQNIDNTPPhlRHIGVLYQDALLFSHLTVA 96
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAG-VITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639318220 97 GNIAFampkgnkkqrlekiaHALeqvgLKDmgnrhpdnLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:cd03232 98 EALRF---------------SAL----LRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-194 |
1.49e-06 |
|
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: 47.86 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSFKANGEVwlngqNIDNTPPHLRHIGVLYQDALLFSHLT--VAGNIAF 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDL-----KISYKPQYISPDYDGTVEEFLRSANTddFGSSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 ampkgnkkqrlEKIAHALeqvGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQI 181
Cdd:COG1245 437 -----------TEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
170
....*....|...
gi 639318220 182 RDHKLPAIMVTHD 194
Cdd:COG1245 503 ENRGKTAMVVDHD 515
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-197 |
1.89e-06 |
|
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: 46.76 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTG-TLPSSfkanGEVWLNGqnidntpphlrhigvlyQDALLF-------SHLTVAG 97
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGiYPPDS----GTVTVRG-----------------RVSSLLglgggfnPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 98 NIAF-AMPKG-NKKQRLEKIAHALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRE 175
Cdd:cd03220 104 NIYLnGRLLGlSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180
....*....|....*....|..
gi 639318220 176 LVFSQIRDHKLpAIMVTHDHSD 197
Cdd:cd03220 184 RLRELLKQGKT-VILVSHDPSS 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-194 |
2.96e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSFKANGEVwlngqNIDNTPPHLRHigvlyqDallfSHLTVAGNIAFAM 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPEL-----KISYKPQYIKP------D----YDGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 PKGNKKQRLEKIAHALeqvGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRD 183
Cdd:PRK13409 426 DDLGSSYYKSEIIKPL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEE 502
|
170
....*....|.
gi 639318220 184 HKLPAIMVTHD 194
Cdd:PRK13409 503 REATALVVDHD 513
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-170 |
3.13e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.54 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 13 YRQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDNTPPHL----RHIGVLYQDA- 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ---KGAVLWQGKPLDYSKRGLlalrQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 88 -LLFsHLTVAGNIAFAM-----PKGNKKQRLEKiahALEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK13638 88 qQIF-YTDIDSDIAFSLrnlgvPEAEITRRVDE---ALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
....*....
gi 639318220 162 FSKLDTQLR 170
Cdd:PRK13638 164 TAGLDPAGR 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-161 |
3.23e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 26 VNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNID-NTPPHLRHIGVLY------QDALLFSHlTVAGN 98
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRT---AGQVYLDGKPIDiRSPRDAIRAGIMLcpedrkAEGIIPVH-SVADN 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639318220 99 IAFA-----MPKG---NKKQRLEKIAHALEQVGLKDMGNRHP-DNLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:PRK11288 352 INISarrhhLRAGcliNNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-210 |
7.76e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQLYRQNEL---LLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLNGQNIDN--TPPHLR 78
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLppvLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE---KGRIMIDDCDVAKfgLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 HIGVLYQDALLFShltvaGNIAFAMPKGNKKQRLEkIAHALEQVGLKDMGNRHP-----------DNLSGGQQARVALLR 147
Cdd:PLN03232 1311 VLSIIPQSPVLFS-----GTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639318220 148 MLLSEPKAILLDEPFSKLDtqLRVDTreLVFSQIRDHKLPAIMVTHDHS-----DADaangKLITLSS 210
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVD--VRTDS--LIQRTIREEFKSCTMLVIAHRlntiiDCD----KILVLSS 1444
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-194 |
1.22e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 32 LTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNgqnidntpPHLRhIGVLYQDALlfSHLTVAGNIAFAMPK---GN 107
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELqPSS----GTVFRS--------AKVR-MAVFSQHHV--DGLDLSSNPLLYMMRcfpGV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 108 KKQRLEkiAHaLEQVGLKDMGNRHPD-NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDTRELVFSQIRDHKL 186
Cdd:PLN03073 603 PEQKLR--AH-LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQGLVLFQG 675
|
....*...
gi 639318220 187 PAIMVTHD 194
Cdd:PLN03073 676 GVLMVSHD 683
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
110-166 |
3.43e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 3.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639318220 110 QRLEKIAHALEQV--------------GLK---DMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLD 166
Cdd:PLN03073 303 QRLEEIYKRLELIdaytaearaasilaGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-202 |
4.00e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 34 IMGPSGSGKSSLLNW----LTGTLPSSFKANgevwlngqnidntpPHLRHI----GVLYQDALLFSHLTvagniafampk 105
Cdd:cd03240 27 IVGQNGAGKTTIIEAlkyaLTGELPPNSKGG--------------AHDPKLiregEVRAQVKLAFENAN----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 106 GNKKQRLEKIAhALEQV------GLKDMGNRHPDNLSGGQQA------RVALLRMLLSEPKAILLDEPFSKLDT-QLRVD 172
Cdd:cd03240 82 GKKYTITRSLA-ILENVifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEES 160
|
170 180 190
....*....|....*....|....*....|
gi 639318220 173 TRELVFSQIRDHKLPAIMVTHDHSDADAAN 202
Cdd:cd03240 161 LAEIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-166 |
6.68e-05 |
|
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: 42.59 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKN-CQLYRQN--ELLLSLNEQVNGGEILTIMGPSGSGKSSL-LNWLtgTLPSSFkaNGEVWLNGQNIDNTPPH-LR- 78
Cdd:cd03288 20 IKIHDlCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFF--RMVDIF--DGKIVIDGIDISKLPLHtLRs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 79 HIGVLYQDALLFShltvaGNIAFAMPKgNKKQRLEKIAHALEQVGLKDMGNRHP-----------DNLSGGQQARVALLR 147
Cdd:cd03288 96 RLSIILQDPILFS-----GSIRFNLDP-ECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLAR 169
|
170
....*....|....*....
gi 639318220 148 MLLSEPKAILLDEPFSKLD 166
Cdd:cd03288 170 AFVRKSSILIMDEATASID 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-161 |
7.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 23 NEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPS-SFkaNGEVWLNGQnidntPPHLRHI------GV--LYQDALLFSHL 93
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgSY--EGEILFDGE-----VCRFKDIrdsealGIviIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 94 TVAGNIaFAmpkGNKKQRL------EKIAHA---LEQVGLKDmgnrHPDNLSG----GQQARVALLRMLLSEPKAILLDE 160
Cdd:NF040905 94 SIAENI-FL---GNERAKRgvidwnETNRRArelLAKVGLDE----SPDTLVTdigvGKQQLVEIAKALSKDVKLLILDE 165
|
.
gi 639318220 161 P 161
Cdd:NF040905 166 P 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-194 |
7.88e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVwlngqnidntpphlrHIG----VLYQD---ALLFSHLTVA 96
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLqADS----GRI---------------HCGtkleVAYFDqhrAELDPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 97 GNIAfampkgNKKQRLE---KIAHALEQvgLKD-----MGNRHP-DNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDt 167
Cdd:PRK11147 402 DNLA------EGKQEVMvngRPRHVLGY--LQDflfhpKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD- 472
|
170 180
....*....|....*....|....*..
gi 639318220 168 qlrVDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:PRK11147 473 ---VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-194 |
8.39e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL-PSSFKANGEVwlngqNIDNTpphLRHigvlYQDALLFSHLT--VAGNIAFAM-- 103
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELiPNLGDYEEEP-----SWDEV---LKR----FRGTELQNYFKklYNGEIKVVHkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 104 ------P---KGNKKQRLEKIAHA------LEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:PRK13409 167 qyvdliPkvfKGKVRELLKKVDERgkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180
....*....|....*....|....*.
gi 639318220 169 LRVDTRELVFSQIRDHKLpaIMVTHD 194
Cdd:PRK13409 247 QRLNVARLIRELAEGKYV--LVVEHD 270
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-194 |
1.36e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 4 SLQIKNCQLYRqNELLLSLNEQVNGgeiltIMGPSGSGKSSLLN---W-LTGTLPSSFKANGEVwlngQNIDNTPP---- 75
Cdd:COG0419 4 RLRLENFRSYR-DTETIDFDDGLNL-----IVGPNGAGKSTILEairYaLYGKARSRSKLRSDL----INVGSEEAsvel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 76 HLRHIGVLYQ------DALLFSHLT-------------------VAGNIAFAMPKGNKKQRLEKIAHALEQVGLKDM-GN 129
Cdd:COG0419 74 EFEHGGKRYRierrqgEFAEFLEAKpserkealkrllgleiyeeLKERLKELEEALESALEELAELQKLKQEILAQLsGL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 130 RHPDNLSGGQQARVALLRMLlsepkAILLDepFSKLDTqlrvDTRELVFSQIRDHKLpaimVTHD 194
Cdd:COG0419 154 DPIETLSGGERLRLALADLL-----SLILD--FGSLDE----ERLERLLDALEELAI----ITHV 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-67 |
1.50e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 41.22 E-value: 1.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 639318220 25 QVNGGEILTIMGPSGSGKSSLLNWLTGTL-PSSfkanGEVWLNG 67
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLIAGILePTS----GRVEVNG 87
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-167 |
2.38e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 34 IMGPSGSGKSSLLNWLTGTLPSSFKANGEVWLNGQNIDNTPPHLR---------HIGVL-YQDAL--------------L 89
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTsayisqndvHVGVMtVKETLdfsarcqgvgtrydL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 90 FSHLTVAGNIAFAMPKGNKKQRLEKIA-----------HALEQVGL---KD--MGNRHPDNLSGGQQARVALLRMLLSEP 153
Cdd:PLN03140 276 LSELARREKDAGIFPEAEVDLFMKATAmegvksslitdYTLKILGLdicKDtiVGDEMIRGISGGQKKRVTTGEMIVGPT 355
|
170
....*....|....
gi 639318220 154 KAILLDEPFSKLDT 167
Cdd:PLN03140 356 KTLFMDEISTGLDS 369
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-183 |
3.48e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 3.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 119 LEQVGLKDMGNRHPDNLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRD 183
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-168 |
4.80e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLY----RQNELLLSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPSSfkaNGEVWLN-GQNID--NTPPHL 77
Cdd:PTZ00265 383 IQFKNVRFHydtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT---EGDIIINdSHNLKdiNLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 78 RHIGVLYQDALLFSHlTVAGNIAFAM-------------------PKGNKKQR----------LEKIAHALEQVGLKDMG 128
Cdd:PTZ00265 460 SKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndSQENKNKRnscrakcagdLNDMSNTTDSNELIEMR 538
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 129 NRH------------------------PDN-----------LSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQ 168
Cdd:PTZ00265 539 KNYqtikdsevvdvskkvlihdfvsalPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
134-206 |
5.04e-04 |
|
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: 39.48 E-value: 5.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639318220 134 NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHKLPAIMVTHDHSDADAANGKLI 206
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-194 |
5.10e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.23 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 22 LNEQVNGGEILTIMGPSGSGKSSLLNwltgtlpSSFKANGEVWLNGqnidnTPPHLRHIGVLYQDALlfshltvagniaf 101
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVN-------EGLYASGKARLIS-----FLPKFSRNKLIFIDQL------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 102 ampkgnkkQRLekIAHALEQVGLkdmgNRHPDNLSGGQQARVALLRMLLSEPKAIL--LDEPFSKLDTQlrvDTREL--V 177
Cdd:cd03238 69 --------QFL--IDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQ---DINQLleV 131
|
170
....*....|....*..
gi 639318220 178 FSQIRDHKLPAIMVTHD 194
Cdd:cd03238 132 IKGLIDLGNTVILIEHN 148
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-53 |
8.06e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 8.06e-04
10 20
....*....|....*....|....*
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGTL 53
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPEL 109
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-166 |
1.45e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 5 LQIKNCQLYRQNELLlSLNEQVNGGEILTIMGPSGSGKSSLLNWLTGTLPssfKANGEVWLNGQNIDNTPPH--LRHIGV 82
Cdd:PRK10982 251 LEVRNLTSLRQPSIR-DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE---KSAGTITLHGKKINNHNANeaINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 83 LYQDAL----LFSHLTVAGNIAFAMPKGNKKQ-------RLEK-IAHALEQVGLKDMGNR-HPDNLSGGQQARVALLRML 149
Cdd:PRK10982 327 LVTEERrstgIYAYLDIGFNSLISNIRNYKNKvglldnsRMKSdTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWL 406
|
170
....*....|....*..
gi 639318220 150 LSEPKAILLDEPFSKLD 166
Cdd:PRK10982 407 LTQPEILMLDEPTRGID 423
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-194 |
1.67e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 129 NRHPDNLSGGQQARVALLRMLLSEPKAI--LLDEPFSKLDTQlrvDTREL--VFSQIRDHKLPAIMVTHD 194
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQ---DTHKLinVIKKLRDQGNTVLLVEHD 537
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-194 |
2.28e-03 |
|
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: 38.38 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGT-LPSSfkanGEVWLnGQNIDntpphlrhigVLYQDAllfSHLTVAGNiafampkgn 107
Cdd:TIGR03719 348 GGIVGVIGPNGAGKSTLFRMITGQeQPDS----GTIEI-GETVK----------LAYVDQ---SRDALDPN--------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 108 kKQRLEKIAHALE--QVGLKDMGNRH---------PD------NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlr 170
Cdd:TIGR03719 401 -KTVWEEISGGLDiiKLGKREIPSRAyvgrfnfkgSDqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD---- 475
|
170 180
....*....|....*....|....
gi 639318220 171 VDTRELVFSQIRDHKLPAIMVTHD 194
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHD 499
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-166 |
2.66e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.29 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 20 LSLNEQVNG----GEILTIMGPSGSGKSSLLNWLTGTLPSSFkANGEVWLNG----------------QNIDNTPPhlrh 79
Cdd:PLN03140 893 LQLLREVTGafrpGVLTALMGVSGAGKTTLMDVLAGRKTGGY-IEGDIRISGfpkkqetfarisgyceQNDIHSPQ---- 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639318220 80 igVLYQDALLFShltvagniAF-AMPKGNKKQR----LEKIAHALEQVGLKD--MGNRHPDNLSGGQQARVALLRMLLSE 152
Cdd:PLN03140 968 --VTVRESLIYS--------AFlRLPKEVSKEEkmmfVDEVMELVELDNLKDaiVGLPGVTGLSTEQRKRLTIAVELVAN 1037
|
170
....*....|....
gi 639318220 153 PKAILLDEPFSKLD 166
Cdd:PLN03140 1038 PSIIFMDEPTSGLD 1051
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
14-74 |
3.01e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.10 E-value: 3.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639318220 14 RQNEL--LLSLNEQVNGG--EILTIMGPSGSGKSSLLNwltgTLPSSFKANGEVWLNGQNIDNTP 74
Cdd:pfam13191 5 REEELeqLLDALDRVRSGrpPSVLLTGEAGTGKTTLLR----ELLRALERDGGYFLRGKCDENLP 65
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
134-173 |
4.11e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.41 E-value: 4.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 639318220 134 NLSGGQQARVALLRMLLSEPKAILLDEPFSKLDtqlrVDT 173
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD----VET 480
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
133-201 |
5.40e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.19 E-value: 5.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639318220 133 DNLSGGQQA------RVALLRMLLSEPKAILLDEPFSKLDTQLRVDTRELVFSQIRDHK-LP-AIMVTHdHSDADAA 201
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdIPqVIMISH-HRELLSV 875
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
29-71 |
5.94e-03 |
|
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.
Pssm-ID: 410898 [Multi-domain] Cd Length: 226 Bit Score: 36.56 E-value: 5.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 639318220 29 GEILTIMGPSGSGKSSLLNWLTGT--LPSSFkanGEVWLNGQNID 71
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARciLPSSW---GGVPLGGLEAA 42
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
134-161 |
7.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 36.69 E-value: 7.29e-03
10 20
....*....|....*....|....*...
gi 639318220 134 NLSGGQQARVALLRMLLSEPKAILLDEP 161
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
29-53 |
8.09e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 35.98 E-value: 8.09e-03
|
| |
