|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-264 |
1.62e-120 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 345.54 E-value: 1.62e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 8 TVTQPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD 87
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RIMVFQEfDQLPPWKTVLENTLFPLVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKV 167
Cdd:COG1116 82 RGVVFQE-PALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 168 LLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPHPGRVRAEINC---HQFALSDQGSE 244
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVdlpRPRDRELRTSP 239
|
250 260
....*....|....*....|
gi 2316062753 245 AFQTTAQRIHHLLFPTDVAA 264
Cdd:COG1116 240 EFAALRAEILDLLREEAERA 259
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-231 |
1.19e-109 |
|
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: 316.34 E-value: 1.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQ 93
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 94 EfDQLPPWKTVLENTLFPLVASRQAtRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:cd03293 81 Q-DALLPWLTVLDNVALGLELQGVP-KAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 174 FAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPHPGRVRAEI 231
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEV 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-237 |
1.18e-89 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 267.11 E-value: 1.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMV 91
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 FQEfDQLPPWKTVLENTLFPLVASRQAtRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:COG4525 82 FQK-DALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPHPGRVRAEIN---CHQFA 237
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLEldfSRRFL 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-221 |
2.34e-73 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.83 E-value: 2.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTrrslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR--PGPD 87
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RI-MVFQEFDqLPPWKTVLENTLFPLVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:COG3842 78 NVgMVFQDYA-LFPHLTVAENVAFGLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 167 VLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMN 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
30-227 |
9.28e-69 |
|
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: 212.38 E-value: 9.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQEFdQLPPWKTVLE 106
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQDY-ALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:cd03259 92 NIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:cd03259 171 EELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRI 209
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
32-220 |
1.25e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 217.66 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---------MVFQEFdQLPPWK 102
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrrkkmsMVFQHF-ALLPHR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFPL-VasRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:COG4175 121 TVLENVAFGLeI--QGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLI 198
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316062753 182 RRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:COG4175 199 RREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-227 |
1.28e-68 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 213.41 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVF 92
Cdd:PRK11248 1 MLQISHLYADYGGKPAL----EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 93 QEfDQLPPWKTVLENTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:PRK11248 77 QN-EGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 173 PFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPHPGRV 227
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-231 |
3.68e-68 |
|
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: 211.56 E-value: 3.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPpWKTVLENTLFPL-V 113
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLP-WLTVRENIALAVdR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 114 ASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALW 193
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIW 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316062753 194 EEVRFTLLFVTHSIEEALIVGSRVLLLSPHPGRVRAEI 231
Cdd:TIGR01184 162 EEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-220 |
2.69e-65 |
|
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: 205.18 E-value: 2.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 22 EYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---------MVF 92
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrrkkisMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 93 QEFdQLPPWKTVLENTLFPL-VASRqaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:cd03294 109 QSF-ALLPHRTVLENVAFGLeVQGV--PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM 234
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
14-232 |
4.38e-64 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 201.51 E-value: 4.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQ 93
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 94 EFdQLPPWKTVLENTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:NF040729 82 NY-ALFPWMTVKENIEYPM-KQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 174 FAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPHPGRVRAEIN 232
Cdd:NF040729 160 LGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLK 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-227 |
1.10e-63 |
|
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: 208.22 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRS-LVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR 88
Cdd:COG1123 257 AEPLLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 I--------MVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIA 158
Cdd:COG1123 337 LrelrrrvqMVFQDpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 159 RALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM--YDGRI 483
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-221 |
5.06e-62 |
|
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: 195.02 E-value: 5.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -----MVFQEFdQLPPWKTVLENTLFPLVASRQAtRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQ 164
Cdd:cd03255 81 rrhigFVFQSF-NLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 165 PKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIvGSRVLLLS 221
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-220 |
3.59e-61 |
|
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: 193.49 E-value: 3.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -----MVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARY-FLNKVGLAK-FADAYPHTLSGGMKQRVAIARAL 161
Cdd:cd03257 81 rkeiqMVFQDpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLlLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 162 TMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-231 |
6.51e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.57 E-value: 6.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI- 89
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 --------MVFQEFdQLPPWKTVLENTLFPLVASRQaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARAL 161
Cdd:COG1136 82 rlrrrhigFVFQFF-NLLPELTALENVALPLLLAGV-SRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 162 TMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSiEEALIVGSRVLLLspHPGRVRAEI 231
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRIVSDE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
34-230 |
3.68e-60 |
|
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: 191.35 E-value: 3.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD-------RI-MVFQE---FDQLppwk 102
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelrrRIgMLFQGgalFDSL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTR 182
Cdd:COG1127 98 TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316062753 183 RKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:COG1127 178 AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL--ADGKIIAE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
34-220 |
8.05e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 190.21 E-value: 8.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD------RI-MVFQEFdQLPPWKTVLE 106
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklrrKVgMVFQQF-NLFPHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD-------- 178
Cdd:COG1126 97 NVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 179 ----ALTRRKMqeellalweevrfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:COG1126 177 dvmrDLAKEGM-------------TMVVVTHEMGFAREVADRVVFM 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
31-221 |
6.98e-59 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 191.51 E-value: 6.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT--RPGPDRIM--VFQEFDqLPPWKTVLE 106
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnLPPRERRVgfVFQHYA-LFPHMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:COG1118 95 NIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELR 173
|
170 180 190
....*....|....*....|....*....|....*
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:COG1118 174 RWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-221 |
1.02e-58 |
|
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: 187.44 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---MVFQEFdQLPPWKTVLEN 107
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpvnTVFQNY-ALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 108 TLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQE 187
Cdd:cd03300 93 IAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 188 ELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:cd03300 172 ELKRLQKELGITFVFVTHDQEEALTMSDRIAVMN 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
34-220 |
3.63e-58 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 185.04 E-value: 3.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD------RI-MVFQEFDqLPPWKTVLE 106
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelrqKVgMVFQQFN-LFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:cd03262 96 NITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 187 EELLALWEEvRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03262 176 DVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFM 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-230 |
3.40e-57 |
|
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: 183.30 E-value: 3.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRslvRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQE-FDQL--PpwkTVLENTLFPLVASRQaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQP 165
Cdd:COG1122 78 gLVFQNpDDQLfaP---TVEEDVAFGPENLGL-PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 166 KVLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVL--DDGRIVAD 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
30-227 |
3.53e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 187.20 E-value: 3.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DR-I-MVFQEFDqLPPWKTVLE 106
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPkDRnIaMVFQSYA-LYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:COG3839 95 NIAFPLKL-RKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:COG3839 174 AEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM--NDGRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-220 |
4.39e-55 |
|
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: 178.26 E-value: 4.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03295 1 IEFENVTKRYGGGKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQEFDQLPPWkTVLENTlfPLVASRQA-TRAEAEERARYFLNKVGL--AKFADAYPHTLSGGMKQRVAIARALTMQP 165
Cdd:cd03295 78 gYVIQQIGLFPHM-TVEENI--ALVPKLLKwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 166 KVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
34-221 |
5.36e-55 |
|
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: 176.89 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQEFD-QL--PpwkTVL 105
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrkvgLVFQNPDdQFfgP---TVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFPLVaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:cd03225 95 EEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRREL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316062753 186 QEELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:cd03225 174 LELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
30-228 |
4.90e-54 |
|
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: 174.75 E-value: 4.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DR--IMVFQEFdQLPPWKTVLE 106
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRdiAMVFQNY-ALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:cd03301 92 NIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVR 228
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQIQ 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-205 |
6.92e-54 |
|
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: 177.55 E-value: 6.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP---VDGEIRLDGQPVTRPGPDRI 89
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ---------MVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL---AKFADAYPHTLSGGMKQRVA 156
Cdd:COG0444 81 rkirgreiqMIFQDpMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316062753 157 IARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-230 |
1.30e-53 |
|
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: 174.23 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03261 1 IELRGLTKSFGGRTVL----KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ----MVFQE---FDQLppwkTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALT 162
Cdd:cd03261 77 rrmgMLFQSgalFDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 163 MQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL--YDGKIVAE 218
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
32-227 |
1.87e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 176.05 E-value: 1.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD---RIM--VFQE---FdqlpPWKT 103
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrRRIgyVIQQiglF----PHMT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLEN-TLFPLVasRQATRAEAEERARYFLNKVGL--AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAL 180
Cdd:COG1125 93 VAENiATVPRL--LGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316062753 181 TRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:COG1125 171 TREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
30-220 |
3.27e-53 |
|
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: 171.22 E-value: 3.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-------MVFQEFdQLPPWK 102
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplrrrigMVFQDF-ALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFPLvasrqatraeaeeraryflnkvglakfadayphtlSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTR 182
Cdd:cd03229 92 TVLENIALGL-----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316062753 183 RKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-227 |
4.87e-53 |
|
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: 172.91 E-value: 4.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DRIM--VFQEFdQLPPWKTVLEN 107
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERNVgfVFQHY-ALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 108 TLFPLVASRQATR---AEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRK 184
Cdd:cd03296 95 VAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316062753 185 MQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:cd03296 175 LRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM--NKGRI 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
34-217 |
9.74e-53 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 175.65 E-value: 9.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQEFdQLPPWKTVLENTLF 110
Cdd:NF040840 17 RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKrgiAYVYQNY-MLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 PLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELL 190
Cdd:NF040840 96 GL-KLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMK 174
|
170 180
....*....|....*....|....*..
gi 2316062753 191 ALWEEVRFTLLFVTHSIEEALIVGSRV 217
Cdd:NF040840 175 RWHREFGFTAIHVTHNFEEALSLADRV 201
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
32-220 |
2.16e-52 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 175.04 E-value: 2.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---------MVFQEFdQLPPWK 102
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrrkkigMVFQQF-ALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFPLVASRqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTR 182
Cdd:TIGR01186 87 TILQNTSLGPELLG-WPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIR 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316062753 183 RKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:TIGR01186 166 DSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIM 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-230 |
3.09e-52 |
|
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: 178.17 E-value: 3.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYRTRRslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP---VDGEIRLDGQPVTRPGPD 87
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RI-----MVFQEFD-QLPPWkTVLENTLFPLVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARAL 161
Cdd:COG1123 80 LRgrrigMVFQDPMtQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 162 TMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVED 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-208 |
1.50e-51 |
|
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: 169.21 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 --MVFQE-FDQLPPWKTVLENTLFPLvasRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARALTMQP 165
Cdd:COG1124 81 vqMVFQDpYASLHPRHTVDRILAEPL---RIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316062753 166 KVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIE 208
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLA 200
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
30-230 |
1.58e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD---RI-MVFQEFDqLPPWKTVL 105
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrRIgYVPQEPA-LYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFplVAS-RQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRK 184
Cdd:COG1131 92 ENLRF--FARlYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 185 MQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:COG1131 170 LWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAII--DKGRIVAD 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-220 |
5.96e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 167.15 E-value: 5.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRslvRATHDVSFDVFPAErFVLL-GPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:COG2884 2 IRFENVSKRYPGGR---EALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -----MVFQEFdQLPPWKTVLENTLFPLVASRqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQ 164
Cdd:COG2884 78 rrrigVVFQDF-RLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 165 PKVLLMDEPFAALDALTRRkmqeELLALWEEVR---FTLLFVTHsiEEALI--VGSRVLLL 220
Cdd:COG2884 156 PELLLADEPTGNLDPETSW----EIMELLEEINrrgTTVLIATH--DLELVdrMPKRVLEL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
35-220 |
8.46e-51 |
|
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: 167.13 E-value: 8.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQEFdQLPPWKTVLENTLFP 111
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNY-ALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLA 191
Cdd:cd03299 96 L-KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180
....*....|....*....|....*....
gi 2316062753 192 LWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-220 |
4.68e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 169.36 E-value: 4.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 8 TVTQPLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGP 86
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVI----SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 DRIM--VFQEFdQLPPWKTVLENTLFPLvasRQATRAEAEERARYF--LNKVGLAKFADAYPHTLSGGMKQRVAIARALT 162
Cdd:PRK09452 85 NRHVntVFQSY-ALFPHMTVFENVAFGL---RMQKTPAAEITPRVMeaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 163 MQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-227 |
1.04e-49 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 164.29 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD----- 87
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 --RI-MVFQEFDQLPPwKTVLENTLFPLVASRQAtRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQ 164
Cdd:cd03258 81 rrRIgMIFQHFNLLSS-RTVFENVALPLEIAGVP-KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 165 PKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVM--EKGEV 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-205 |
5.96e-49 |
|
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: 162.22 E-value: 5.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG---- 85
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 86 ----PDRI-MVFQEFdQLPPWKTVLENTLFPLvasRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARA 160
Cdd:COG4181 85 arlrARHVgFVFQSF-QLLPTLTALENVMLPL---ELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316062753 161 LTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTH 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-223 |
1.47e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPD-R--- 88
Cdd:COG4619 1 LELEGLSFRVGGKPIL----SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwRrqv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 IMVFQEfdqlPPW--KTVLENTLFPLvasRQATRAEAEERARYFLNKVGLAK-FADAYPHTLSGGMKQRVAIARALTMQP 165
Cdd:COG4619 77 AYVPQE----PALwgGTVRDNLPFPF---QLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 166 KVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPH 223
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
37-247 |
3.39e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 160.31 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 37 SFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQE---FDQLppwkTVLENTLF 110
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvSMLFQEnnlFPHL----TVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 PLvasRQATRAEAEERARYF--LNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEE 188
Cdd:COG3840 95 GL---RPGLKLTAEQRAQVEqaLERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 189 LLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQFaLSDQGSEAFQ 247
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLV--ADGRIAADGPTAAL-LDGEPPPALA 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-218 |
5.96e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.22 E-value: 5.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRslvRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-- 89
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ------MVFQEFdQLPPWKTVLENTLFPLVASRQATRA------EAE-ERARYFLNKVGLAKFADAYPHTLSGGMKQRVA 156
Cdd:COG3638 78 lrrrigMIFQQF-NLVPRLSVLTNVLAGRLGRTSTWRSllglfpPEDrERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 157 IARALTMQPKVLLMDEPFAALD-ALTRRKMqEELLALWEEVRFTLLFVTHSIEEALIVGSRVL 218
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
31-217 |
9.91e-48 |
|
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: 162.51 E-value: 9.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP---DRIMVFQEFdQLPPWKTVLEN 107
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPqkrDYGIVFQSY-ALFPNLTVADN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 108 TLFPLVaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQE 187
Cdd:TIGR03265 97 IAYGLK-NRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRT 175
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 188 ELLALWEEVRFTLLFVTHSIEEALIVGSRV 217
Cdd:TIGR03265 176 EIRQLQRRLGVTTIMVTHDQEEALSMADRI 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-220 |
1.69e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 158.72 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD-RI------MVFQEFDqLPPWKTVLE 106
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLirqeagMVFQQFY-LFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:PRK09493 97 NVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 187 EELLALWEEvRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK09493 177 KVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFI 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
48-221 |
1.81e-47 |
|
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: 161.12 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---MVFQEFdQLPPWKTVLENTLFPLvASRQATRAEAE 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhinMVFQSY-ALFPHMTVEENVAFGL-KMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 125 ERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVT 204
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170
....*....|....*..
gi 2316062753 205 HSIEEALIVGSRVLLLS 221
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIMR 175
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-236 |
2.59e-47 |
|
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: 157.73 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFL-----SPVDGEIRLDGQPVTRPGPDR 88
Cdd:cd03260 1 IELRDLNVYYGDKHAL----KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 I-------MVFQEFDQLPpwKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-AKFAD-AYPHTLSGGMKQRVAIAR 159
Cdd:cd03260 77 LelrrrvgMVFQKPNPFP--GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwDEVKDrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 160 ALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQF 236
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFL--LNGRLVEFGPTEQI 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
42-220 |
1.36e-46 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 156.76 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 42 PAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEfDQLPPWKTVLENTLFPLvasrqatR 120
Cdd:PRK11247 36 PAGQFVaVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQD-ARLLPWKKVIDNVGLGL-------K 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 121 AEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTL 200
Cdd:PRK11247 108 GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTV 187
|
170 180
....*....|....*....|
gi 2316062753 201 LFVTHSIEEALIVGSRVLLL 220
Cdd:PRK11247 188 LLVTHDVSEAVAMADRVLLI 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-227 |
7.97e-46 |
|
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: 154.26 E-value: 7.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRtrrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ----MVFQEFdQLPPWKTVLENTLFPLVASRQATRA-------EAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIA 158
Cdd:cd03256 78 rqigMIFQQF-NLIERLSVLENVLSGRLGRRSTWRSlfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 159 RALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSphPGRV 227
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLK--DGRI 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-205 |
4.89e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 154.89 E-value: 4.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSL-------VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT 82
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGGLfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 83 RPGPDRI--------MVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMK 152
Cdd:COG4608 84 GLSGRELrplrrrmqMVFQDpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 153 QRVAIARALTMQPKVLLMDEPFAALDAltrrKMQEELLALWEEVR----FTLLFVTH 205
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDV----SIQAQVLNLLEDLQdelgLTYLFISH 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-175 |
8.27e-45 |
|
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: 148.95 E-value: 8.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQEfDQLPPWKTVLENT 108
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeigYVFQD-PQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 109 LFPLVASRQaTRAEAEERARYFLNKVGLAKFAD----AYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFA 175
Cdd:pfam00005 81 RLGLLLKGL-SKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-221 |
8.93e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 154.86 E-value: 8.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPDRIM--VFQEFdQLPPWKTVLENTLF 110
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRKVgfVFQHY-ALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 PL-VASRQA--TRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQE 187
Cdd:PRK10851 98 GLtVLPRRErpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 188 ELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK10851 178 WLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-221 |
1.26e-44 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.99 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---MVFQEFdQLPPWKTVLENT 108
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinMMFQSY-ALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 109 LFPLVASRQAtRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEE 188
Cdd:PRK11607 113 AFGLKQDKLP-KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170 180 190
....*....|....*....|....*....|...
gi 2316062753 189 LLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK11607 192 VVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
30-236 |
1.61e-44 |
|
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: 151.16 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP---DRIMVFQEFDQLPPWKTVLE 106
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRearRQIGVLPDERGLYDRLTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFpLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:COG4555 94 NIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316062753 187 EELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQF 236
Cdd:COG4555 173 EILRALKKEGK-TVLFSSHIMQEVEALCDRVVIL--HKGKVVAQGSLDEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-255 |
3.03e-44 |
|
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: 150.58 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:COG1120 1 MLEAENLSVGYGGRPVL----DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 --MVFQEFDQLPPWkTVLENTL---FPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQ 164
Cdd:COG1120 77 iaYVPQEPPAPFGL-TVRELVAlgrYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 165 PKVLLMDEPFAALDAltrrKMQEELL----ALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQFALSD 240
Cdd:COG1120 156 PPLLLLDEPTSHLDL----AHQLEVLellrRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRIVAQGPPEEVLTPE 229
|
250
....*....|....*
gi 2316062753 241 QGSEAFQTTAQRIHH 255
Cdd:COG1120 230 LLEEVYGVEARVIED 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-229 |
3.54e-44 |
|
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: 149.37 E-value: 3.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDvFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV--TRPGPD------RI-MVFQEFdQLPPWKTVL 105
Cdd:cd03297 16 KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINlppqqrKIgLVFQQY-ALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFPLvasRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:cd03297 94 ENLAFGL---KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316062753 186 QEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRA 229
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME--DGRLQY 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-229 |
5.68e-44 |
|
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: 152.95 E-value: 5.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV--TRPGPD------RI-MVFQEfDQLPPWKTVL 105
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFlpphrrRIgYVFQE-ARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFPLVASRQATRAEAEERARYFLnkvGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:COG4148 96 GNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316062753 186 QEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRA 229
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLL--EQGRVVA 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-255 |
8.40e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.77 E-value: 8.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRslvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPdRI 89
Cdd:COG1121 3 MMPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-RI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQ--EFD-QLPPwkTVLEntlfpLVAS-RQATR-------AEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAI 157
Cdd:COG1121 78 gYVPQraEVDwDFPI--TVRD-----VVLMgRYGRRglfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 158 ARALTMQPKVLLMDEPFAALDAltrrKMQEELLALWEEVR---FTLLFVTHSIEEALIVGSRVLLLSphpGRVRAEINCH 234
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDA----ATEEALYELLRELRregKTILVVTHDLGAVREYFDRVLLLN---RGLVAHGPPE 223
|
250 260
....*....|....*....|.
gi 2316062753 235 QFALSDQGSEAFQTTAQRIHH 255
Cdd:COG1121 224 EVLTPENLSRAYGGPVALLAH 244
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
32-220 |
9.59e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.31 E-value: 9.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV---TRPGPDRI--------MVFQEFDqLPP 100
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIrllrqkvgMVFQQYN-LWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 WKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAL 180
Cdd:COG4161 96 HLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316062753 181 TRRKMQEELLALwEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:COG4161 176 ITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-224 |
1.50e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 144.93 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLeYRTRRSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP---VDGEIRLDGQPVTR--PGPDR 88
Cdd:COG4136 2 LSLENLTI-TLGGRPLLA---PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlpAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 I-MVFQEfDQLPPWKTVLENTLFPLVASRqaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKV 167
Cdd:COG4136 78 IgILFQD-DLLFPHLSVGENLAFALPPTI--GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 168 LLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPHP 224
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
30-220 |
4.92e-42 |
|
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: 144.75 E-value: 4.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--------MVFQEFdQLPPW 101
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrrrigMIFQHY-NLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 102 KTVLENTLFPLVASRQATRA-------EAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPF 174
Cdd:TIGR02315 94 LTVLENVLHGRLGYKPTWRSllgrfseEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 175 AALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-208 |
7.32e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 146.76 E-value: 7.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPD----- 87
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 -RI-MVFQEFDQLPPwKTVLENTLFPLVASRqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQP 165
Cdd:COG1135 82 rKIgMIFQHFNLLSS-RTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316062753 166 KVLLMDEPFAALDALTRRkmqeELLALWEEVR----FTLLFVTHSIE 208
Cdd:COG1135 160 KVLLCDEATSALDPETTR----SILDLLKDINrelgLTIVLITHEMD 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-205 |
9.24e-42 |
|
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: 144.41 E-value: 9.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTrrslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ----MV--FQ---EFDQLppwkTVLEN---------------TLFPLVASRqATRAEAEERARYFLNKVGLAKFADAYPH 145
Cdd:COG0411 77 arlgIArtFQnprLFPEL----TVLENvlvaaharlgrgllaALLRLPRAR-REEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 146 TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-220 |
2.97e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.46 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV---TRPGPDRI- 89
Cdd:PRK11124 3 IQLNGINCFYGAHQAL----FDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -------MVFQEFDqLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALT 162
Cdd:PRK11124 79 elrrnvgMVFQQYN-LWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 163 MQPKVLLMDEPFAALDA-LTRR--KMQEELlalwEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPeITAQivSIIREL----AETGITQVIVTHEVEVARKTASRVVYM 214
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
14-220 |
3.05e-41 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 145.91 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP--VDGEIRLDGQPVTRPGPDR--- 88
Cdd:TIGR03258 6 IRIDHLRVAYGANTVL----DDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKrgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 IMVFQEFdQLPPWKTVLENTLFPLVASRQaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVL 168
Cdd:TIGR03258 82 ALLFQNY-ALFPHLKVEDNVAFGLRAQKM-PKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 169 LMDEPFAALDALTRRKMQEELLALWEEV-RFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:TIGR03258 160 LLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIM 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-227 |
3.82e-41 |
|
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: 140.23 E-value: 3.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD---RIM 90
Cdd:cd03230 1 IEVRNLSKRYGKKTAL----DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 91 VFQEFDQLPPWKTVLENtlfplvasrqatraeaeeraryfLNkvglakfadayphtLSGGMKQRVAIARALTMQPKVLLM 170
Cdd:cd03230 77 YLPEEPSLYENLTVREN-----------------------LK--------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 171 DEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAIL--NNGRI 173
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
34-205 |
5.66e-41 |
|
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: 141.31 E-value: 5.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--------MVFQEFDqLPPWKTVL 105
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLvqlrrrigYIFQAHN-LLGFLTAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:TIGR02982 101 QNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDV 180
|
170 180
....*....|....*....|
gi 2316062753 186 QEELLALWEEVRFTLLFVTH 205
Cdd:TIGR02982 181 VELMQKLAKEQGCTILMVTH 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-220 |
6.73e-41 |
|
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: 138.92 E-value: 6.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 15 QVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI----- 89
Cdd:cd00267 1 EIENLSFRYGGRTAL----DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELrrrig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVFQefdqlppwktvlentlfplvasrqatraeaeeraryflnkvglakfadayphtLSGGMKQRVAIARALTMQPKVLL 169
Cdd:cd00267 77 YVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 170 MDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVL 153
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-210 |
1.05e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 140.56 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ------MVFQeFDQLPPWKTVLENTLFPLVASRQaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTM 163
Cdd:TIGR02211 81 rnkklgFIYQ-FHHLLPDFTALENVAMPLLIGKK-SVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316062753 164 QPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEA 210
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-230 |
1.17e-40 |
|
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: 141.04 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI------MVFQ---EFDQLpp 100
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigRTFQiprLFPEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 wkTVLEN---------TLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:cd03219 91 --TVLENvmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVTVL--DQGRVIAE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-220 |
1.24e-40 |
|
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: 139.98 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 15 QVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRpGPDRI-MVFQ 93
Cdd:cd03235 1 EVEDLTVSYGGHPVL----EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-ERKRIgYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 94 --EFDQLPP---WKTVLENTLFPLVASRQATRAEaEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVL 168
Cdd:cd03235 76 rrSIDRDFPisvRDVVLMGLYGHKGLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 169 LMDEPFAALDAltrrKMQEELLALWEEVRF---TLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03235 155 LLDEPFAGVDP----KTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-221 |
8.81e-40 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 137.76 E-value: 8.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRrslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -----MVFQEFdQLPPWKTVLENTLFPLVASRQATRaEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQ 164
Cdd:TIGR02673 78 rrrigVVFQDF-RLLPDRTVYENVALPLEVRGKKER-EIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 165 PKVLLMDEPFAALDAltrrKMQEELLALWEEVR---FTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:TIGR02673 156 PPLLLADEPTGNLDP----DLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILD 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-219 |
1.23e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 138.18 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 37 SFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQEfDQLPPWKTVLENT---LF 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQE-NNLFSHLTVAQNIglgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 PLVASRQATRAEAEERARyflnKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMqeelL 190
Cdd:PRK10771 98 PGLKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM----L 169
|
170 180 190
....*....|....*....|....*....|...
gi 2316062753 191 ALWEEV----RFTLLFVTHSIEEALIVGSRVLL 219
Cdd:PRK10771 170 TLVSQVcqerQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-230 |
6.17e-39 |
|
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: 134.49 E-value: 6.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 15 QVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPdrimvfqe 94
Cdd:cd03214 1 EVENLSVGYGGRTVL----DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 fdqlppwktvlentlfplvasrqatraeaEERARYF------LNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVL 168
Cdd:cd03214 69 -----------------------------KELARKIayvpqaLELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 169 LMDEPFAALDAltrrKMQEELL----ALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03214 120 LLDEPTSHLDI----AHQIELLellrRLARERGKTVVMVLHDLNLAARYADRVILL--KDGRIVAQ 179
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
48-220 |
7.50e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 139.47 E-value: 7.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG---PDRIMVFQEFdQLPPWKTVLENTLFPLVASRQAtRAEAE 124
Cdd:PRK11432 37 LLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqRDICMVFQSY-ALFPHMSLGENVGYGLKMLGVP-KEERK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 125 ERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVT 204
Cdd:PRK11432 115 QRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVT 194
|
170
....*....|....*.
gi 2316062753 205 HSIEEALIVGSRVLLL 220
Cdd:PRK11432 195 HDQSEAFAVSDTVIVM 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-223 |
2.07e-38 |
|
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: 134.14 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRsLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD--RI 89
Cdd:COG4133 1 MMLEAENLSCRRGERL-LFS---GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVFqeFDQLPPWK---TVLENTLFplvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:COG4133 77 LAY--LGHADGLKpelTVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 167 VLLMDEPFAALDALTRRKMqEELLALWEEVRFTLLFVTHsiEEALIVGSRVLLLSPH 223
Cdd:COG4133 152 LWLLDEPFTALDAAGVALL-AELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDF 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-230 |
4.57e-38 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 133.39 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 43 AERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQEfDQLPPWKTVLENTLFPLVASRQAT 119
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQE-NNLFAHLTVEQNVGLGLSPGLKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 120 rAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFT 199
Cdd:cd03298 103 -AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMT 181
|
170 180 190
....*....|....*....|....*....|.
gi 2316062753 200 LLFVTHSIEEALIVGSRVLLLSphPGRVRAE 230
Cdd:cd03298 182 VLMVTHQPEDAKRLAQRVVFLD--NGRIAAQ 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-227 |
1.86e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 133.73 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVfPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--------MVFQ--EfDQLp 99
Cdd:TIGR04521 19 KALDDVSLTI-EDGEFVaIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkvgLVFQfpE-HQL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 100 pwktvLENTLFPLVA----SRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPF 174
Cdd:TIGR04521 96 -----FEETVYKDIAfgpkNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 175 AALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVM--HKGKI 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
37-221 |
2.50e-37 |
|
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: 131.52 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 37 SFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR---IMVFQEfDQLPPWKTVLENTLFPLV 113
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQE-NNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 114 ASRQATrAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALW 193
Cdd:TIGR01277 97 PGLKLN-AEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180
....*....|....*....|....*...
gi 2316062753 194 EEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-220 |
1.54e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 134.39 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---------MVFQEFdQLPPWKTVL 105
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrkkiaMVFQSF-ALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFPLVASRQATrAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:PRK10070 125 DNTAFGMELAGINA-EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*
gi 2316062753 186 QEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
34-220 |
1.93e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 130.26 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIR-----LDGQPVTRPGPDRI--------MVFQEFDqLPP 100
Cdd:PRK11264 20 HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTARSLSQQKGLIrqlrqhvgFVFQNFN-LFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 WKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAL 180
Cdd:PRK11264 99 HRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316062753 181 TRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFM 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
5.73e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.39 E-value: 5.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 1 MThhSPDTVTQPLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKS-------IGGFLspVDGE 73
Cdd:COG1117 1 MT--APASTLEPKIEVRNLNVYYGDKQAL----KDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGAR--VEGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 74 IRLDGQPVTRPGPD------RI-MVFQEFDQLPpwKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-----AKFaD 141
Cdd:COG1117 73 ILLDGEDIYDPDVDvvelrrRVgMVFQKPNPFP--KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevkDRL-K 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 142 AYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMqEELLalwEEVR--FTLLFVTHSIEEAlivgSRV 217
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELI---LELKkdYTIVIVTHNMQQA----ARV 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-205 |
6.85e-36 |
|
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: 134.43 E-value: 6.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKS----SLLKSIGGFLSPVDGEIRLDGQPVTRPG 85
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 86 P--------DRI-MVFQEfdqlP-----PWKTVlENTLF-PLVASRQATRAEAEERARYFLNKVGL---AKFADAYPHTL 147
Cdd:COG4172 83 ErelrrirgNRIaMIFQE----PmtslnPLHTI-GKQIAeVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 148 SGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-230 |
7.65e-36 |
|
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: 129.09 E-value: 7.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPgpDRI--------MVFQEFD-QL-- 98
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE--ENLweirkkvgMVFQNPDnQFvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 99 PpwkTV-------LENTLFPlvasrqatRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:TIGR04520 93 A---TVeddvafgLENLGVP--------REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEAlIVGSRVLLLspHPGRVRAE 230
Cdd:TIGR04520 162 EATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVM--NKGKIVAE 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-230 |
7.86e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 7.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT------- 82
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 83 --RPGpdriMVFQEFDQLPPWKTVLENTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARA 160
Cdd:PRK13635 80 rrQVG----MVFQNPDNQFVGATVQDDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 161 LTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALiVGSRVLLLSphPGRVRAE 230
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMN--KGEILEE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-208 |
1.90e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.92 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 15 QVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD------- 87
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RI-MVFQEFDQLPPwKTVLENTLFPLVASRQaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:PRK11153 83 QIgMIFQHFNLLSS-RTVFDNVALPLELAGT-PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316062753 167 VLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIE 208
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMD 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
30-229 |
2.90e-35 |
|
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: 126.24 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVLENTL 109
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FpLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03269 93 Y-LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316062753 190 LALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRA 229
Cdd:cd03269 172 RELARAGK-TVILSTHQMELVEELCDRVLLL--NKGRAVL 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-242 |
3.81e-35 |
|
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: 132.96 E-value: 3.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRslvRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI 89
Cdd:COG4988 333 GPPSIELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 M-----VFQEfDQLPPWkTVLENTLFplvASRQATRAEAEERARyflnKVGLAKFADAYPH-----------TLSGGMKQ 153
Cdd:COG4988 410 RrqiawVPQN-PYLFAG-TIRENLRL---GRPDASDEELEAALE----AAGLDEFVAALPDgldtplgeggrGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 154 RVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTHSIeEALIVGSRVLLLspHPGRVrAEINC 233
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRL-ALLAQADRILVL--DDGRI-VEQGT 554
|
....*....
gi 2316062753 234 HQFALSDQG 242
Cdd:COG4988 555 HEELLAKNG 563
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-229 |
1.02e-34 |
|
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: 124.92 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRpgpDRIMVFQ 93
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 94 E------FDQLPPWKTVLEN-TLFPLVasRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:cd03263 76 SlgycpqFDALFDELTVREHlRFYARL--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 167 VLLMDEPFAALDALTRRKMQEELLALwEEVRfTLLFVTHSIEEALIVGSRVLLLSphPGRVRA 229
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEALCDRIAIMS--DGKLRC 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-205 |
1.07e-34 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 131.35 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 6 PDTVTQPLLQVDSVGLEYRTRRSL-------VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGfLSPVDGEIRLDG 78
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFPIKRGLfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 79 QPVT-------RPGPDRI-MVFQE-FDQLPPWKTVLENTLFPL-VASRQATRAEAEERARYFLNKVGL-AKFADAYPHTL 147
Cdd:COG4172 347 QDLDglsrralRPLRRRMqVVFQDpFGSLSPRMTVGQIIAEGLrVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEF 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 148 SGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH 484
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
34-208 |
1.64e-34 |
|
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: 122.88 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQE---FDQlppwkTVL 105
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniaYVPQDpflFSG-----TIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLfplvasrqatraeaeeraryflnkvglakfadayphtlSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:cd03228 94 ENIL--------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180
....*....|....*....|...
gi 2316062753 186 QEELLALWEEVrfTLLFVTHSIE 208
Cdd:cd03228 136 LEALRALAKGK--TVIVIAHRLS 156
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-205 |
1.77e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 127.00 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSL------VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR 83
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 PGPDRI--------MVFQE-FDQLPPWKTV---LENtlfPLVASRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGG 150
Cdd:PRK11308 82 ADPEAQkllrqkiqIVFQNpYGSLNPRKKVgqiLEE---PLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 151 MKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-229 |
2.80e-34 |
|
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: 124.81 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDG-EIRLDGQpvTRPGPD-- 87
Cdd:COG1119 1 DPLLELRNVTVRRGGKTIL----DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE--RRGGEDvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 ----RI-MVFQEF-DQLPPWKTVLEntlfpLVAS---------RQATrAEAEERARYFLNKVGLAKFADAYPHTLSGGMK 152
Cdd:COG1119 75 elrkRIgLVSPALqLRFPRDETVLD-----VVLSgffdsiglyREPT-DEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 153 QRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRA 229
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK--DGRVVA 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-205 |
5.44e-34 |
|
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: 129.50 E-value: 5.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLVraTHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI 89
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -----MVFQE---FDQlppwkTVLENtLfpLVASRQATRAEAEErAryfLNKVGLAKFADAYPH-----------TLSGG 150
Cdd:COG4987 408 rrriaVVPQRphlFDT-----TLREN-L--RLARPDATDEELWA-A---LERVGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 151 MKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEvRfTLLFVTH 205
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-R-TVLLITH 528
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-230 |
9.51e-34 |
|
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: 125.99 E-value: 9.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 21 LEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDG-------QPVTRPGPDRIM--V 91
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEKRRIgyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 FQEfDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLnkvGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:TIGR02142 81 FQE-ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRAE 230
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE--DGRVAAA 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
34-205 |
1.65e-33 |
|
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: 129.18 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQE---FDQlppwkTVL 105
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrrqigVVLQDvflFSG-----TIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 EN-TLFplvaSRQATRAEAEERARyflnKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:COG2274 567 ENiTLG----DPDATDEEIIEAAR----LAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190
....*....|....*....|....*....|..
gi 2316062753 174 FAALDALTRRKMQEELLALWEEVrfTLLFVTH 205
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGR--TVIIIAH 668
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
30-230 |
1.84e-33 |
|
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: 121.77 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI------MVFQE---FDQLpp 100
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigYVPEGrriFPEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 wkTVLENTLFPLVASRQATRAEAEERA-RYFLNkvgLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:cd03224 91 --TVEENLLLGAYARRRAKRKARLERVyELFPR---LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 180 LTRRKMQEELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRAE 230
Cdd:cd03224 166 KIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLE--RGRVVLE 213
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-207 |
2.71e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 122.64 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLVR-----ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTrPGP 86
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE-YGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 DRI------MVFQE-FDQLPPWKTV---LEntlFPLvasRQATRAEAEER-ARYF--LNKVGL-AKFADAYPHTLSGGMK 152
Cdd:COG4167 82 YKYrckhirMIFQDpNTSLNPRLNIgqiLE---EPL---RLNTDLTAEEReERIFatLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 153 QRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSI 207
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHL 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-217 |
6.60e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.90 E-value: 6.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR------IMVFQEFDqLPPWKT 103
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaagiAIIHQELN-LVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLEN-------TLFPLVaSRQATRAEAEEraryFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAA 176
Cdd:COG1129 96 VAENiflgrepRRGGLI-DWRAMRRRARE----LLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316062753 177 LDaltrRKMQEELLALWEEVR---FTLLFVTHSIEEALIVGSRV 217
Cdd:COG1129 171 LT----EREVERLFRIIRRLKaqgVAIIYISHRLDEVFEIADRV 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-219 |
1.14e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.75 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTrrslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRImvfq 93
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 94 efDQLP------PWKTVLENTLFpLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKV 167
Cdd:COG4152 74 --GYLPeerglyPKMKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 168 LLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTH---SIEE-----ALIVGSRVLL 219
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHqmeLVEElcdriVIINKGRKVL 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
30-230 |
1.37e-32 |
|
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: 119.40 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD---RI-MVFQEF---DQLPPWK 102
Cdd:cd03265 13 FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvrrRIgIVFQDLsvdDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLentLFPLVASrqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTR 182
Cdd:cd03265 93 NLY---IHARLYG--VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316062753 183 RKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII--DHGRIIAE 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
30-210 |
3.42e-32 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 117.52 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV--TRPGPDRI-----MVFQEFDQLPPWK 102
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERrqrvgLVFQDPDDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLF-PLvaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:TIGR01166 85 DVDQDVAFgPL--NLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*....
gi 2316062753 182 RRKMQEELLALWEEVRfTLLFVTHSIEEA 210
Cdd:TIGR01166 163 REQMLAILRRLRAEGM-TVVISTHDVDLA 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-208 |
3.82e-32 |
|
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: 118.28 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--------MVFQEFdQLPPW 101
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylrrkigVVFQDF-RLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 102 KTVLENTLFPLVASrQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:cd03292 93 RNVYENVAFALEVT-GVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 182 RRkmqeELLALWEEVR---FTLLFVTHSIE 208
Cdd:cd03292 172 TW----EIMNLLKKINkagTTVVVATHAKE 197
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
30-220 |
8.86e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 120.72 E-value: 8.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DR-I-MVFQEFdQLPPWKTVLE 106
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRdIaMVFQNY-ALYPHMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:PRK11650 96 NMAYGL-KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR 174
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK11650 175 LEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
34-208 |
9.22e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 116.95 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIM---------VFQEFdQLPPWKTV 104
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrreklgyLFQNF-ALIENETV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 105 LENTLFPLVASRQaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRK 184
Cdd:TIGR03608 94 EENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
|
170 180
....*....|....*....|....
gi 2316062753 185 MQEELLALWEEVRfTLLFVTHSIE 208
Cdd:TIGR03608 173 VLDLLLELNDEGK-TIIIVTHDPE 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-210 |
1.08e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIG--GFLSP---VDGEIRLDGQPVTRP 84
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKAL----NSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 85 GPDRI-------MVFQEFDQLPpwKTVLENTLFPL----VASRQATRAEAEE--RARYFLNKVGLAKFADAYphTLSGGM 151
Cdd:PRK14239 78 RTDTVdlrkeigMVFQQPNPFP--MSIYENVVYGLrlkgIKDKQVLDEAVEKslKGASIWDEVKDRLHDSAL--GLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 152 KQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEvrFTLLFVTHSIEEA 210
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQA 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-230 |
1.26e-31 |
|
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: 116.52 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVrathDVSFdVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRpGPDRI---- 89
Cdd:cd03264 1 LQLENLTKRYGKKRALD----GVSL-TLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLrrri 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQEFDQLPPWkTVLENTLFPLVASRQATRaEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVL 168
Cdd:cd03264 75 gYLPQEFGVYPNF-TVREFLDYIAWLKGIPSK-EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 169 LMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVL--NKGKLVFE 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-210 |
1.65e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.84 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP---- 86
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 ----DRIMVFQEFDQLPPWKTVLENTLFPLVASRQAtRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALT 162
Cdd:PRK11629 83 elrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKK-PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316062753 163 MQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEA 210
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-230 |
2.08e-31 |
|
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: 116.31 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD---RI 89
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEarrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVFQEFDQLPPWKTVLENTLFpLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLL 169
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEY-FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 170 MDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVL--HRGRVVYE 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-226 |
2.20e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.35 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD--RI 89
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKIL----NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVFQEFdQLPPW--KTVLENTLFPLVASRQAT--RAEAEERARYFLNKVGLAKFADAyphtLSGGMKQRVAIARALTMQP 165
Cdd:PRK10247 82 QVSYCA-QTPTLfgDTVYDNLIFPWQIRNQQPdpAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 166 KVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEaLIVGSRVLLLSPHPGR 226
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGE 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-220 |
7.46e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 118.21 E-value: 7.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 33 THDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPDRI--MVFQEFdQLPPWKTVLENTL 109
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERGvgMVFQSY-ALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PRK11000 98 FGLKLAG-AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
|
170 180 190
....*....|....*....|....*....|.
gi 2316062753 190 LALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK11000 177 SRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-220 |
1.26e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 115.32 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 46 FVLLGPSGCGKSSLLKSIGGFL-----SPVDGEIRLDGQPVTRPGPDRI-------MVFQEFDQLPPWkTVLENT----- 108
Cdd:PRK14267 33 FALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDPIevrrevgMVFQYPNPFPHL-TIYDNVaigvk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 109 LFPLVASRQatraEAEERARYFLNKVGL-----AKFADaYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRR 183
Cdd:PRK14267 112 LNGLVKSKK----ELDERVEWALKKAALwdevkDRLND-YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316062753 184 KMQEELLALWEEvrFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK14267 187 KIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFL 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
48-229 |
1.34e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 117.28 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQ------------PVTRpgpdRI-MVFQEfDQLPPWKTVLENTLFPLVA 114
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclpPEKR----RIgYVFQD-ARLFPHYKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 SRQAtraeaeerarYFLNKV---GLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDaLTRRKmqeELLA 191
Cdd:PRK11144 104 SMVA----------QFDKIVallGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR---ELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316062753 192 ----LWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRA 229
Cdd:PRK11144 170 ylerLAREINIPILYVSHSLDEILRLADRVVVL--EQGKVKA 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
34-210 |
2.29e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.50 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD----RI-MVFQE---FDqlppwKTVL 105
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslrrQIgVVPQDtflFS-----GTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFplvASRQATRAEAEERARyflnKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPF 174
Cdd:COG1132 432 ENIRY---GRPDATDEEVEEAAK----AAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316062753 175 AALDALTRRKMQEELLALWEEVrfTLLFVTH---SIEEA 210
Cdd:COG1132 505 SALDTETEALIQEALERLMKGR--TTIVIAHrlsTIRNA 541
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
35-220 |
2.87e-30 |
|
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: 112.74 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPvtRPGPDRI----MVFQEFD-QLPPwKTVLENTL 109
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRksigYVMQDVDyQLFT-DSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASrqatrAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDaltRRKMQE-- 187
Cdd:cd03226 95 LGLKEL-----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKNMERvg 166
|
170 180 190
....*....|....*....|....*....|...
gi 2316062753 188 ELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03226 167 ELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
32-257 |
4.01e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.56 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV--TRPGPDRI-----MVFQEFDQLPPWKTV 104
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLresvgMVFQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 105 LENTLFPLVaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRK 184
Cdd:PRK13636 101 YQDVSFGAV-NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 185 MQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRAEINCHQFALSDQGSEAFQTTAQRIHHLL 257
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK--EGRVILQGNPKEVFAEKEMLRKVNLRLPRIGHLM 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-230 |
4.27e-30 |
|
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: 113.15 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVgleyRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-- 89
Cdd:COG0410 2 PMLEVENL----HAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ----MVFQE---FDQLppwkTVLENtlfpLVASRQATRAEAEERAR------YFLNkvgLAKFADAYPHTLSGGMKQRVA 156
Cdd:COG0410 78 lgigYVPEGrriFPSL----TVEEN----LLLGAYARRDRAEVRADlervyeLFPR---LKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 157 IARALTMQPKVLLMDEP------------FAALDALTRRKMqeellalweevrfTLLFVTHSIEEALIVGSRVLLLspHP 224
Cdd:COG0410 147 IGRALMSRPKLLLLDEPslglapliveeiFEIIRRLNREGV-------------TILLVEQNARFALEIADRAYVL--ER 211
|
....*.
gi 2316062753 225 GRVRAE 230
Cdd:COG0410 212 GRIVLE 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-220 |
4.57e-30 |
|
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: 118.37 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 9 VTQPLLQVDSVGLEY-RTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGE--IRLDGQPV--TR 83
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVdmTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 PGPD---RI-----MVFQEFDqLPPWKTVLENTL------FPL-VASRQA-----TRAEAEERARYFLNKvglakfadaY 143
Cdd:TIGR03269 355 PGPDgrgRAkryigILHQEYD-LYPHRTVLDNLTeaigleLPDeLARMKAvitlkMVGFDEEKAEEILDK---------Y 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 144 PHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-231 |
6.03e-30 |
|
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: 113.75 E-value: 6.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRrSLVRAT------HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP 86
Cdd:TIGR02769 2 LLEVRDVTHTYRTG-GLFGAKqrapvlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 --------DRIMVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVA 156
Cdd:TIGR02769 81 kqrrafrrDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 157 IARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEI 231
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM--DKGQIVEEC 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
48-230 |
8.02e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 113.14 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT----RPGPDRI--------------MVFQEFDqLPPWKTVLENTL 109
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKVadknqlrllrtrltMVFQHFN-LWSHMTVLENVM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRQATRAEAEERARYFLNKVGLAKFA-DAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD----ALTRRK 184
Cdd:PRK10619 115 EAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelvGEVLRI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 185 MQEellaLWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:PRK10619 195 MQQ----LAEEGK-TMVVVTHEMGFARHVSSHVIFL--HQGKIEEE 233
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
31-230 |
3.71e-29 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 112.48 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPgPDRI-----MVFQE---FDQLPPWK 102
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVRE-PRKVrrsigIVPQYasvDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 T-VLENTLFPLvasrqaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:TIGR01188 86 NlEMMGRLYGL------PKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316062753 182 RRKMQEELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRAE 230
Cdd:TIGR01188 160 RRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIID--HGRIIAE 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-220 |
7.15e-29 |
|
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: 107.90 E-value: 7.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPdrimvfqefdqlppwktvlentl 109
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP----------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 fplvasRQATRAeaeeraryflnKVGLAkfadaypHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAltrrKMQEEL 189
Cdd:cd03216 70 ------RDARRA-----------GIAMV-------YQLSVGERQMVEIARALARNARLLILDEPTAALTP----AEVERL 121
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 190 LALWEEVR---FTLLFVTHSIEEALIVGSRVLLL 220
Cdd:cd03216 122 FKVIRRLRaqgVAVIFISHRLDEVFEIADRVTVL 155
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
35-210 |
1.18e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.05 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD---RIMVFQEFDQLPPWKTVLENTLfp 111
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHarqRVGVVPQFDNLDPDFTVRENLL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 lVASRQ--ATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PRK13537 103 -VFGRYfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL 181
|
170 180
....*....|....*....|.
gi 2316062753 190 LALWEEVRfTLLFVTHSIEEA 210
Cdd:PRK13537 182 RSLLARGK-TILLTTHFMEEA 201
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-205 |
2.56e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.92 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDsvGLEYRTRRSLvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQP--------V 81
Cdd:PRK11300 2 SQPLLSVS--GLMMRFGGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 82 TRPGPDRimVFQE---FDQLppwkTVLENT---------------LFPLVASRQATRaEAEERARYFLNKVGLAKFADAY 143
Cdd:PRK11300 78 ARMGVVR--TFQHvrlFREM----TVIENLlvaqhqqlktglfsgLLKTPAFRRAES-EALDRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 144 PHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-237 |
3.79e-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: 108.01 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 23 YRTRRslvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR------IMVFQE-- 94
Cdd:cd03218 10 YGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlgiGYLPQEas 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 -FDQLppwkTVLENTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:cd03218 86 iFRKL----TVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 174 FAALDALTRRKMQeELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQFA 237
Cdd:cd03218 161 FAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYII--YEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-227 |
5.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.98 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT-----------RPGpdriMVFQEfdqlp 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvklsdirkKVG----LVFQY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 100 PWKTVLENTLFPLVA----SRQATRAEAEERARYFLNKVGLA--KFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:PRK13637 92 PEYQLFEETIEKDIAfgpiNLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 174 FAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM--NKGKC 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-208 |
7.57e-28 |
|
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: 111.99 E-value: 7.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD----RI 89
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALR---PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswrdQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVFQEFDQLPPwKTVLENTLFplvASRQATRAEAEERARyflnKVGLAKFADAYP-----------HTLSGGMKQRVAIA 158
Cdd:TIGR02857 399 AWVPQHPFLFA-GTIAENIRL---ARPDASDAEIREALE----RAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316062753 159 RALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEevRFTLLFVTHSIE 208
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA 518
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-178 |
8.25e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.42 E-value: 8.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRsLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-------- 83
Cdd:COG1137 2 MTLEAENLVKSYGKRT-VVK---DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 ------PgpdrimvfQE---FDQLppwkTVLENTLfpLVAS-RQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQ 153
Cdd:COG1137 78 lgigylP--------QEasiFRKL----TVEDNIL--AVLElRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180
....*....|....*....|....*
gi 2316062753 154 RVAIARALTMQPKVLLMDEPFAALD 178
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVD 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-227 |
1.26e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 107.57 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 23 YRT---RRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT----RPGPDRI-MVFQE 94
Cdd:PRK15112 16 YRTgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIrMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 -FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:PRK15112 96 pSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 173 PFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM--HQGEV 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
34-191 |
2.02e-27 |
|
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: 105.98 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRL--DGQPV--TRPGPDRIM---------VFQeFDQLPP 100
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASPREILalrrrtigyVSQ-FLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 WKTVLENTLFPLVAsRQATRAEAEERARYFLNKVGLA-KFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:COG4778 107 RVSALDVVAEPLLE-RGVDREEARARARELLARLNLPeRLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170
....*....|....*
gi 2316062753 180 LTRRK---MQEELLA 191
Cdd:COG4778 186 ANRAVvveLIEEAKA 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
31-236 |
2.31e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.64 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFL---SPVDGEIRLDGQPVTRPGpdRIM------------VFQEF 95
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREG--RLArdirksrantgyIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 96 DqLPPWKTVLENTLFPLVASRQATRA-------EAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVL 168
Cdd:PRK09984 96 N-LVNRLSVLENVLIGALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 169 LMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQF 236
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHVFYDGSSQQF 240
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-178 |
4.29e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVtrpgpdrimvf 92
Cdd:COG4559 1 MLEAENLSVRLGGRTLL----DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 93 qefDQLPPWK-----TVL--ENTL-FPL---------VASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRV 155
Cdd:COG4559 66 ---AAWSPWElarrrAVLpqHSSLaFPFtveevvalgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRV 142
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 156 AIARALT-------MQPKVLLMDEPFAALD 178
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-221 |
4.43e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.24 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRL----------DGQPVTRPGPDRI---------- 89
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIknfkelrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQeFDQLPPWKTVLE-NTLFPLVASRQaTRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:PRK13631 119 sMVFQ-FPEYQLFKDTIEkDIMFGPVALGV-KKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 167 VLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMD 250
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
31-206 |
4.58e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 109.76 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD----RIMVFQE----FDQlppwk 102
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrrRVSVCAQdahlFDT----- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTlfpLVASRQATRAEAEERARyflnKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:TIGR02868 424 TVRENL---RLARPDATDEELWAALE----RVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEvrFTLLFVTHS 206
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
35-210 |
5.07e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.61 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV---TRPGPDRIMVFQEFDQLPPWKTVLENTLFP 111
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparARLARARIGVVPQFDNLDLEFTVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LVASRQATRaEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLA 191
Cdd:PRK13536 139 GRYFGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRS 217
|
170
....*....|....*....
gi 2316062753 192 LWEEVRfTLLFVTHSIEEA 210
Cdd:PRK13536 218 LLARGK-TILLTTHFMEEA 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
30-217 |
6.52e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.35 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DRI-----MVFQEFdQLPPWKT 103
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIalgigMVHQHF-MLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLEN------TLFPLVASRQATRAEAEERARyflnKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAAL 177
Cdd:COG3845 97 VAENivlglePTKGGRLDRKAARARIRELSE----RYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316062753 178 -----DAL--TRRKMQEELLalweevrfTLLFVTHSIEEALIVGSRV 217
Cdd:COG3845 173 tpqeaDELfeILRRLAAEGK--------SIIFITHKLREVMAIADRV 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-232 |
1.00e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.19 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--------MVFQEFDQLPPwK 102
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflrrqigMIFQDHHLLMD-R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFPLVASrQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAltr 182
Cdd:PRK10908 95 TVYDNVAIPLIIA-GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD--- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 183 rKMQEELLALWEE---VRFTLLFVTHSIeeALIVGSRVLLLSPHPGRVRAEIN 232
Cdd:PRK10908 171 -ALSEGILRLFEEfnrVGVTVLMATHDI--GLISRRSYRMLTLSDGHLHGGVG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
36-221 |
1.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-------MVFQEFDQLPPWKTVLENT 108
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrktvgIVFQNPDDQLFAPTVEEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 109 LF-PLvaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQE 187
Cdd:PRK13639 101 AFgPL--NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK 178
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 188 ELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK13639 179 LLYDLNKE-GITIIISTHDVDLVPVYADKVYVMS 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-231 |
1.81e-26 |
|
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: 103.07 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD--RIMV 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVL----DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 FQEFDQLPPWKTVLENtlfpLVASRQATRAEaEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:cd03268 77 LIEAPGFYPNLTAREN----LRLLARLLGIR-KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEI 231
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGI-TVLISSHLLSEIQKVADRIGII--NKGKLIEEG 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-221 |
1.86e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.69 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 7 DTVTQPLLQVDSVGLEYRTRRSLvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP 86
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 DRI-----MVFQEFDQLPPWKTV-------LENTLFPlvasRQATRAEAEERARyflnKVGLAKFADAYPHTLSGGMKQR 154
Cdd:PRK13632 79 KEIrkkigIIFQNPDNQFIGATVeddiafgLENKKVP----PKKMKDIIDDLAK----KVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 155 VAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEAlIVGSRVLLLS 221
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFS 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-210 |
1.89e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 103.32 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---------MVFQEFdQLPPWKTVLE 106
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvgFVFQSF-MLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:PRK10584 108 NVELPALL-RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180
....*....|....*....|....
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEA 210
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQLA 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-178 |
2.79e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDsvGLEYRTRRSLVraTHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTrpgpdrimv 91
Cdd:PRK13548 1 AMLEAR--NLSVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 fqefdQLPPWK-----TVL--ENTL-FPL---------VASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQR 154
Cdd:PRK13548 68 -----DWSPAElarrrAVLpqHSSLsFPFtveevvamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQR 142
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 155 VAIARALT------MQPKVLLMDEPFAALD 178
Cdd:PRK13548 143 VQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-220 |
3.67e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.17 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP--------DRIMVFQE-FDQLPPW 101
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewravrsDIQMIFQDpLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 102 KTVLENTLFPLVASR-QATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PRK15079 115 MTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316062753 180 LTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-227 |
5.44e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.23 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRrSLVRAT------HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG 85
Cdd:PRK10419 2 TLLNVSGLSHHYAHG-GLSGKHqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 86 PDRI--------MVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLA-KFADAYPHTLSGGMKQRV 155
Cdd:PRK10419 81 RAQRkafrrdiqMVFQDsISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDaltrRKMQEELLALWEEVR----FTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLD----LVLQAGVIRLLKKLQqqfgTACLFITHDLRLVERFCQRVMVM--DNGQI 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
35-227 |
5.81e-26 |
|
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: 100.75 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVF-----QEfDQLPPwKTVLENtl 109
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvgylpQD-DELFS-GSIAEN-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 fplvasrqatraeaeeraryflnkvglakfadayphTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03246 96 ------------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316062753 190 LALwEEVRFTLLFVTHSIeEALIVGSRVLLLspHPGRV 227
Cdd:cd03246 140 AAL-KAAGATRIVIAHRP-ETLASADRILVL--EDGRV 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-230 |
9.20e-26 |
|
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: 101.46 E-value: 9.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVtrpGPDRIMVFqeFDqlpPWKTVLENTL 109
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLLGLGGG--FN---PELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03220 107 LNGRLLG-LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316062753 190 LALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:cd03220 186 RELLKQGK-TVILVSHDPSSIKRLCDRALVL--EKGKIRFD 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-210 |
1.39e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.47 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT----------RPGpdriMVFQEFDQLPPW 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwdirnKAG----MVFQNPDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 102 KTVLENTLF-PLVASRQATraEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAL 180
Cdd:PRK13633 101 TIVEEDVAFgPENLGIPPE--EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 181 TRRKMQEELLALWEEVRFTLLFVTHSIEEA 210
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEA 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
32-205 |
2.04e-25 |
|
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: 100.36 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIM-----VFQEfdqlpPW---KT 103
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRrnigyVPQD-----VTlfyGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLEN-TLFPLVASRQATrAEAEERAryflnkvGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:cd03245 94 LRDNiTLGAPLADDERI-LRAAELA-------GVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 172 EPFAALDALTRRKMQEELLALWEEVrfTLLFVTH 205
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDK--TLIIITH 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-208 |
2.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 25 TRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQEFDQLP 99
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrkfvgLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 100 PWKTVLENTLFPLVaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PRK13652 92 FSPTVEQDIAFGPI-NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180
....*....|....*....|....*....
gi 2316062753 180 LTRRKMQEELLALWEEVRFTLLFVTHSIE 208
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLD 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-230 |
2.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQEFDQLPPWKTVL 105
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvgLVFQDPDDQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLF-PLvaSRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRK 184
Cdd:PRK13647 99 DDVAFgPV--NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 185 MQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLSphPGRVRAE 230
Cdd:PRK13647 177 LMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLK--EGRVLAE 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-205 |
2.91e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.94 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 7 DTVT--QPLLQVDSV--------GLEYRTRRSlVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRL 76
Cdd:PRK10261 305 DTVVdgEPILQVRNLvtrfplrsGLLNRVTRE-VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 77 DG-----------QPVTRpgpDRIMVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL-AKFADAY 143
Cdd:PRK10261 384 NGqridtlspgklQALRR---DIQFIFQDpYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRY 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 144 PHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISH 522
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-210 |
5.14e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.25 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFdVFPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLdGQPVTRPG-------PDRI---MVFQ--E--- 94
Cdd:PRK13634 21 RALYDVNV-SIPSGSYVaIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkklkPLRKkvgIVFQfpEhql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 FDQlppwkTVLENTLF-PLvaSRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:PRK13634 99 FEE-----TVEKDICFgPM--NFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316062753 173 PFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEA 210
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDA 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-230 |
5.15e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.16 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 17 DSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGqpvtrpgpdRI------- 89
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVsallelg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVFQ-EFdqlppwkTVLENTLFplVASRQ-ATRAEAEERARYFLNKVGLAKFADAyP-HTLSGGMKQRVAIARALTMQPK 166
Cdd:COG1134 97 AGFHpEL-------TGRENIYL--NGRLLgLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 167 VLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWL--EKGRLVMD 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
35-220 |
5.30e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.96 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTrpgPDRI--------MVFQEFDQLPPWKTVLE 106
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVwdirhkigMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQ 186
Cdd:PRK13650 102 DVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190
....*....|....*....|....*....|....
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEaLIVGSRVLLL 220
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
32-217 |
7.37e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVfPAERFV-LLGPSGCGKSSLLKS-------IGGFlsPVDGEIRLDGQPVTRPGPD------RI-MVFQEFD 96
Cdd:PRK14243 25 AVKNVWLDI-PKNQITaFIGPSGCGKSTILRCfnrlndlIPGF--RVEGKVTFHGKNLYAPDVDpvevrrRIgMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 97 QLPpwKTVLENTLF-PLVASRQATRAEAEERA----------RYFLNKVGLAkfadayphtLSGGMKQRVAIARALTMQP 165
Cdd:PRK14243 102 PFP--KSIYDNIAYgARINGYKGDMDELVERSlrqaalwdevKDKLKQSGLS---------LSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 166 KVLLMDEPFAALDALTRRKMQEELLALWEevRFTLLFVTHSIEEAlivgSRV 217
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQA----ARV 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-189 |
4.26e-24 |
|
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: 97.23 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 19 VGLEYRTRRSlVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP----DRI-MVFQ 93
Cdd:cd03249 6 VSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwlrSQIgLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 94 E---FDqlppwKTVLENTLFplvASRQATRAEAEERARyflnKVGLAKFADAYPH-----------TLSGGMKQRVAIAR 159
Cdd:cd03249 85 EpvlFD-----GTIAENIRY---GKPDATDEEVEEAAK----KANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIAR 152
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 160 ALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-210 |
7.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGE---IRLDGQPVTRPG----PDRI-MVFQEFDQLPPWKT 103
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTvwdiREKVgIVFQNPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLENTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRR 183
Cdd:PRK13640 102 VGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180
....*....|....*....|....*..
gi 2316062753 184 KMQEELLALWEEVRFTLLFVTHSIEEA 210
Cdd:PRK13640 181 QILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-220 |
9.47e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.91 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGFL-----SPVDGEIRLDGQPVTRPGPDRI-----MVFQEFDQLPPWkTVL 105
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELrrrvqMVFQIPNPIPNL-SIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLFPLVASRQA-TRAEAEERARYFLNKVGL----AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAL 180
Cdd:PRK14247 101 ENVALGLKLNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316062753 181 TRRKMQEELLALWEEVrfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK14247 181 NTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-225 |
1.48e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.88 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 7 DTVTQPLLQVDSVGLEYRTRRSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIrldgqpvTRPGP 86
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDGRPLLE---DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-------ARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 DRIMVfqefdqLP-----PWKTVLENTLFPlvasrQATRAEAEERARYFLNKVGLAKFAD------AYPHTLSGGMKQRV 155
Cdd:COG4178 426 ARVLF------LPqrpylPLGTLREALLYP-----ATAEAFSDAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTHsiEEALIVG-SRVLLLSPHPG 225
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGH--RSTLAAFhDRVLELTGDGS 561
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-242 |
1.53e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 95.76 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03253 1 IEFENVTFAYDPGRPVLK---DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLrrai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQE---FDQlppwkTVLENTLFplvASRQATRAEAEERARYFLNKVGLAKFADAYpHT--------LSGGMKQRVAI 157
Cdd:cd03253 78 gVVPQDtvlFND-----TIGYNIRY---GRPDATDEEVIEAAKAAQIHDKIMRFPDGY-DTivgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 158 ARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEevRFTLLFVTHSIEEalIVGS-RVLLLspHPGRVrAEINCHQF 236
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST--IVNAdKIIVL--KDGRI-VERGTHEE 221
|
....*.
gi 2316062753 237 ALSDQG 242
Cdd:cd03253 222 LLAKGG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-207 |
1.79e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFL--SPV---DGEIRLDGQPVTRP 84
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsPPVvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 85 GP--------DRI-MVFQE-FDQLPPWKTvLENTLFPLVA-----SRQATRAEAEEraryFLNKVGL---AKFADAYPHT 146
Cdd:PRK15134 82 SEqtlrgvrgNKIaMIFQEpMVSLNPLHT-LEKQLYEVLSlhrgmRREAARGEILN----CLDRVGIrqaAKRLTDYPHQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 147 LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSI 207
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
34-205 |
2.19e-23 |
|
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: 95.51 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP----VDGEIRLDGQPVTRP---GPDRIMVFQE----FDQLPPWK 102
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLsirGRHIATIMQNprtaFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFplvaSRQATRAEAEERARYFLNKVGL---AKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:TIGR02770 83 NHAIETLR----SLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180
....*....|....*....|....*.
gi 2316062753 180 LTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITH 184
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-208 |
4.92e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 93.69 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLdgqpvtrpgPDRI-MVFQEfdqlpPW---KTVLENTL 109
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---------PGSIaYVSQE-----PWiqnGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FplvasrqatrAEAEERARYflNKV----GLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPF 174
Cdd:cd03250 88 F----------GKPFDEERY--EKVikacALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 2316062753 175 AALDALTRRK-MQEELLALWEEVRfTLLFVTHSIE 208
Cdd:cd03250 156 SAVDAHVGRHiFENCILGLLLNNK-TRILVTHQLQ 189
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-232 |
5.46e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAErFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPDRIM----VFQEfdqlP---- 99
Cdd:COG1101 19 KRALDGLNLTIEEGD-FVtVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRAKyigrVFQD----Pmmgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 100 -PWKTVLENTLfpLVASRQATRA-----EAEERARYF-----LN---------KVGLakfadayphtLSGGmkQRVAIAr 159
Cdd:COG1101 94 aPSMTIEENLA--LAYRRGKRRGlrrglTKKRRELFRellatLGlglenrldtKVGL----------LSGG--QRQALS- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 160 aLTM----QPKVLLMDEPFAALD--------ALTRRKMQEELLalweevrfTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:COG1101 159 -LLMatltKPKLLLLDEHTAALDpktaalvlELTEKIVEENNL--------TTLMVTHNMEQALDYGNRLIMM--HEGRI 227
|
....*
gi 2316062753 228 RAEIN 232
Cdd:COG1101 228 ILDVS 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
36-179 |
7.81e-23 |
|
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: 93.19 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV--TRPGPDRIMVF-QEFDQLPPWKTVLENTLF-- 110
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENILYlGHLPGLKPELSALENLHFwa 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 111 PLVASRQATRAEAeeraryfLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:TIGR01189 99 AIHGGAQRTIEDA-------LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-253 |
3.40e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRSLVR-------ATHDVSFDVFPAERFVLLGPSGCGKSS----LLKSIggflsPVDGEIRLDG 78
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 79 QPVTR-------PGPDRI-MVFQE-FDQLPPWKTVLENTLFPL-VASRQATRAEAEERARYFLNKVGL-AKFADAYPHTL 147
Cdd:PRK15134 347 QPLHNlnrrqllPVRHRIqVVFQDpNSSLNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 148 SGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEalivgsrvlllsphpgrV 227
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHV-----------------V 489
|
250 260
....*....|....*....|....*.
gi 2316062753 228 RAEinCHQFALSDQGSEAFQTTAQRI 253
Cdd:PRK15134 490 RAL--CHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-205 |
5.03e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-- 89
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -------MVFQEFdQLPPWKTVLENTLFPLVASrQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALT 162
Cdd:PRK10535 83 lrrehfgFIFQRY-HLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 163 MQPKVLLMDEPFAALDALTrrkmQEELLALWEEVR---FTLLFVTH 205
Cdd:PRK10535 161 NGGQVILADEPTGALDSHS----GEEVMAILHQLRdrgHTVIIVTH 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
35-205 |
5.19e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLdGQPVtrpgpdRIMVF-QEFDQLPPWKTVLENTlfplv 113
Cdd:COG0488 333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------KIGYFdQHQEELDPDKTVLDEL----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 114 asRQATRAEAEERARYFlnkvgLAKF------ADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMqE 187
Cdd:COG0488 401 --RDGAPGGTEQEVRGY-----LGRFlfsgddAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL-E 472
|
170
....*....|....*...
gi 2316062753 188 ELLALWEEvrfTLLFVTH 205
Cdd:COG0488 473 EALDDFPG---TVLLVSH 487
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-179 |
5.52e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.02 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD--RIMVFqeFDQLPPWKTVL---ENT 108
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLY--LGHQPGIKTELtalENL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 109 LFPLVASRQATraeaEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PRK13538 96 RFYQRLHGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
31-205 |
1.26e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---------MVFQeFdqlpPW 101
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikqirkkvgLVFQ-F----PE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 102 KTVLENTLFPLVA----SRQATRAEAEERARYFLNKVGLAK-FADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAA 176
Cdd:PRK13649 96 SQLFEETVLKDVAfgpqNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|..
gi 2316062753 177 LDALTRRkmqeELLALWEEVR---FTLLFVTH 205
Cdd:PRK13649 176 LDPKGRK----ELMTLFKKLHqsgMTIVLVTH 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-181 |
1.26e-21 |
|
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: 90.41 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 19 VGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVD---GEIRLDGQPVTRPG-PDRIMVFQE 94
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQfQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 FDQLPPWKTVLENTLFPLVASRQATRAEAEERAR---YFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMD 171
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170
....*....|
gi 2316062753 172 EPFAALDALT 181
Cdd:cd03234 169 EPTSGLDSFT 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-219 |
1.47e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQpvTRPG--PDRIMVFqefDQLPpwKTVLENTL 109
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAyvPQRSEVP---DSLP--LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRQATR---AEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMq 186
Cdd:NF040873 80 MGRWARRGLWRrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI- 158
|
170 180 190
....*....|....*....|....*....|...
gi 2316062753 187 EELLALWEEVRFTLLFVTHSIEEALIVGSRVLL 219
Cdd:NF040873 159 IALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-220 |
1.56e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 46 FVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQpVTRPGPD--RI----------MVFQEFDQLPPWkTVLENTLFPLV 113
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDifQIdaiklrkevgMVFQQPNPFPHL-SIYDNIAYPLK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 114 ASRQATRAEAEERARYFLNKVGLAKFA----DAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PRK14246 117 SHGIKEKREIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLI 196
|
170 180 190
....*....|....*....|....*....|.
gi 2316062753 190 LALWEEVrfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK14246 197 TELKNEI--AIVIVSHNPQQVARVADYVAFL 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-230 |
1.97e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.89 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRtrRSLVraTHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPDRI--- 89
Cdd:TIGR03410 1 LEVSNLNVYYG--QSHI--LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHERArag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 MVF-----QEFDQLppwkTVLENTLFPLVASRQATRAEAEERARYF------LNKVGlakfADayphtLSGGMKQRVAIA 158
Cdd:TIGR03410 77 IAYvpqgrEIFPRL----TVEENLLTGLAALPRRSRKIPDEIYELFpvlkemLGRRG----GD-----LSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 159 RALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSphPGRVRAE 230
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVME--RGRVVAS 213
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-227 |
2.42e-21 |
|
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: 90.27 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYRTRRslvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRL---DGQPV---TRP 84
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGK----GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELelyQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 85 GPDRIMVFQEfdqlpPWKTVLENtlfPLVASRQATRAEAE--ER---------------ARYFLNKVGL-AKFADAYPHT 146
Cdd:TIGR02323 77 EAERRRLMRT-----EWGFVHQN---PRDGLRMRVSAGANigERlmaigarhygniratAQDWLEEVEIdPTRIDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 147 LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGR 226
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGR 226
|
.
gi 2316062753 227 V 227
Cdd:TIGR02323 227 V 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
35-211 |
2.65e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--------MVFQE---FDQLppwkT 103
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvrkrmsMLFQSgalFTDM----N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLENTLFPLvasRQATRAEAEERARYFLNK---VGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAL 180
Cdd:PRK11831 101 VFDNVAYPL---REHTQLPAPLLHSTVMMKleaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190
....*....|....*....|....*....|.
gi 2316062753 181 TRRKMQEELLALWEEVRFTLLFVTHSIEEAL 211
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVL 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-205 |
2.67e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 91.71 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 7 DTVTQPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP---VDGEIRLDGQPV-- 81
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIln 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 82 ------TRPGPDRI-MVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVglaKFADA------YPHTL 147
Cdd:PRK09473 86 lpekelNKLRAEQIsMIFQDpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAV---KMPEArkrmkmYPHEF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 148 SGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-220 |
5.18e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLV-RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT--------R 83
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkeiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 PGPDRIMVFQEFdqlpPWKTVLENTLFPLVA----SRQATRAEAEERARYFLNKVGLAK-FADAYPHTLSGGMKQRVAIA 158
Cdd:PRK13643 81 PVRKKVGVVFQF----PESQLFEETVLKDVAfgpqNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 159 RALTMQPKVLLMDEPFAALDAltrrKMQEELLALWEEVR---FTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDP----KARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLL 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
35-205 |
8.15e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEirldgqpVTRPGPDRI-MVFQEfDQLPPWKTVLENTL--FP 111
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE-------VSIPKGLRIgYLPQE-PPLDDDLTVLDTVLdgDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LVASRQATRAEAEE-----------------------------RARYFLNKVGLAKF-ADAYPHTLSGGMKQRVAIARAL 161
Cdd:COG0488 88 ELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEdLDRPVSELSGGWRRRVALARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316062753 162 TMQPKVLLMDEPFAALDALTRRKMQEELLALweevRFTLLFVTH 205
Cdd:COG0488 168 LSEPDLLLLDEPTNHLDLESIEWLEEFLKNY----PGTVLVVSH 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
34-205 |
1.19e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 86.60 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVtrpgpdrimvfqefdqlppwkTVLENTLFPLV 113
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV---------------------SDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 114 ASRQatraeaeERARYF----LNKVGLakfadayphTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03247 78 SVLN-------QRPYLFdttlRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
170
....*....|....*.
gi 2316062753 190 LALWEEVrfTLLFVTH 205
Cdd:cd03247 142 FEVLKDK--TLIWITH 155
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-179 |
1.76e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVF-QEFDQLPPWKTVLENTLFplv 113
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlGHRNAMKPALTVAENLEF--- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 114 asRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PRK13539 97 --WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-205 |
1.86e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 5 SPDTVTQPLLQVDSVGLEYRTRRSLVraTHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT-- 82
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdy 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 83 -----RPG----PDRIMVFQEfdqlppwkTVLENTLFplvASRQATraeaEERARYFLNKVGLAKFADAYP--------- 144
Cdd:PRK11160 408 seaalRQAisvvSQRVHLFSA--------TLRDNLLL---AAPNAS----DEALIEVLQQVGLEKLLEDDKglnawlgeg 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 145 -HTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTH 205
Cdd:PRK11160 473 gRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITH 532
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
34-192 |
1.94e-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: 87.28 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT-------RpgpDRI-MVFQEfdqlpPW---K 102
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdisrkslR---SMIgVVLQD-----TFlfsG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 TVLENTLFplvaSRQATRAEAEERAR------YFLNKvgLAKFADAYP----HTLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:cd03254 92 TIMENIRL----GRPNATDEEVIEAAkeagahDFIMK--LPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180
....*....|....*....|
gi 2316062753 173 PFAALDALTRRKMQEELLAL 192
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKL 185
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
34-210 |
2.33e-20 |
|
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: 90.95 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPgpDRIMVFQEFDQLP--PW---KTVLENT 108
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPqePYifsGSILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 109 LfpLVASRQATRAEAEERARYFLNKVGLAKFADAY-------PHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:TIGR01193 569 L--LGAKENVSQDEIWAACEIAEIKDDIENMPLGYqtelseeGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180
....*....|....*....|....*....
gi 2316062753 182 RRKMQEELLALWEEvrfTLLFVTHSIEEA 210
Cdd:TIGR01193 647 EKKIVNNLLNLQDK---TIIFVAHRLSVA 672
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-209 |
2.41e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTrrslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV----TRPG 85
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 86 PDR--IMVFQEFdQLPPWKTVLENTLFPLVASRQA--TRAEAEERARYFLNKVGLakfaDAYPHT----LSGGMKQRVAI 157
Cdd:PRK11288 77 LAAgvAIIYQEL-HLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGV----DIDPDTplkyLSIGQRQMVEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 158 ARALTMQPKVLLMDEPFAALDAltrRKMqEELLALWEEVRF---TLLFVTHSIEE 209
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSA---REI-EQLFRVIRELRAegrVILYVSHRMEE 202
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-227 |
2.55e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.67 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYRTRRslvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRL---DGQPV---TR 83
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRdlyAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 PGPDRIMVFQEfdqlpPWKTVLENtlfPLVASRQATRAEAE--ER-----ARYF----------LNKVGL-AKFADAYPH 145
Cdd:PRK11701 79 SEAERRRLLRT-----EWGFVHQH---PRDGLRMQVSAGGNigERlmavgARHYgdiratagdwLERVEIdAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 146 TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPG 225
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQG 228
|
..
gi 2316062753 226 RV 227
Cdd:PRK11701 229 RV 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-189 |
2.72e-20 |
|
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: 90.65 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 9 VTQPLLQVDSVGLEYRTRRSLVratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR 88
Cdd:COG5265 353 VGGGEVRFENVSFGYDPERPIL---KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 I-----MVFQEfdqlppwkTVLEN-TLFPLVA-SR-QATRAEAEERARyflnkvgLAK---FADAYP---HT-------- 146
Cdd:COG5265 430 LraaigIVPQD--------TVLFNdTIAYNIAyGRpDASEEEVEAAAR-------AAQihdFIESLPdgyDTrvgerglk 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316062753 147 LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-209 |
2.80e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLsPVDGEIRLDGQpvtrpgpdrimvfqEFDQLPP--WK----------- 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGI--------------ELRELDPesWRkhlswvgqnpq 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 ----TVLENTLFplvASRQATraeaEERARYFLNKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKV 167
Cdd:PRK11174 434 lphgTLRDNVLL---GNPDAS----DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316062753 168 LLMDEPFAALDALTRRKMQEELLALWEevRFTLLFVTHSIEE 209
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED 546
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-220 |
2.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT----RPGPDRI-----MVFQeFDQLPPWK-TV 104
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLrkkvsLVFQ-FPEAQLFEnTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 105 LENTLF-PLvaSRQATRAEAEERARYFLNKVGLAK-FADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTR 182
Cdd:PRK13641 104 LKDVEFgPK--NFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316062753 183 RKMQeELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK13641 182 KEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-210 |
3.08e-20 |
|
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: 86.90 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVraTHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLrrqi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQE---FDQlppwkTVLENTLFplvASRQATRAEAEERARyflnKVGLAKFADAYP---HT--------LSGGMKQR 154
Cdd:cd03251 79 gLVSQDvflFND-----TVAENIAY---GRPGATREEVEEAAR----AANAHEFIMELPegyDTvigergvkLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 155 VAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEevRFTLLFVTH---SIEEA 210
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHrlsTIENA 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-227 |
4.21e-20 |
|
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: 85.68 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP--VDGEIRLDGQPVTRPGPDRIM--VFQEfDQLPPWKTVLENTL 109
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIIgyVPQD-DILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FplvasrqatraEAEERAryflnkvglakfadayphtLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03213 105 F-----------AAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316062753 190 LALWEEVRfTLLFVTHSiEEALIVGS--RVLLLSphPGRV 227
Cdd:cd03213 155 RRLADTGR-TIICSIHQ-PSSEIFELfdKLLLLS--QGRV 190
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
4.49e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-- 89
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ---MVFQEFDQLPPWKTV-------LENTLFPlvasrqatRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIAR 159
Cdd:PRK13648 84 higIVFQNPDNQFVGSIVkydvafgLENHAVP--------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 160 ALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEAL 211
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-227 |
5.61e-20 |
|
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: 84.79 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVgleyrtrrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPdrimv 91
Cdd:cd03215 3 PVLEVRGL--------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 fqefdqlppwktvlentlfplvasRQATRAE----AEERARYflnkvGLakFAD-------AYPHTLSGGMKQRVAIARA 160
Cdd:cd03215 70 ------------------------RDAIRAGiayvPEDRKRE-----GL--VLDlsvaeniALSSLLSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 161 LTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGK-AVLLISSELDELLGLCDRILVM--YEGRI 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-242 |
6.20e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPL----LQVDSVGLEYRTRRSLVratHDVSFDVfPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQP---- 80
Cdd:PRK10790 333 DRPLqsgrIDIDNVSFAYRDDNLVL---QNINLSV-PSRGFVaLVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlssl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 81 ---VTRPGPdrIMVFQEfdqlppwKTVLENTLFplvASRQATRAEAEERARYFLNKVGLAKFADAYP-----------HT 146
Cdd:PRK10790 409 shsVLRQGV--AMVQQD-------PVVLADTFL---ANVTLGRDISEEQVWQALETVQLAELARSLPdglytplgeqgNN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 147 LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEevRFTLLFVTH---SIEEAlivgSRVLLLspH 223
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHrlsTIVEA----DTILVL--H 548
|
250
....*....|....*....
gi 2316062753 224 PGRVrAEINCHQFALSDQG 242
Cdd:PRK10790 549 RGQA-VEQGTHQQLLAAQG 566
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
31-220 |
8.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.06 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRL---DGQPVTRPGPDRIMVFQEFDQLPPWK----- 102
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLEKLVIQKTRFKkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 ---------------------TVLENTLFPLVaSRQATRAEAEERARYFLNKVGL-AKFADAYPHTLSGGMKQRVAIARA 160
Cdd:PRK13651 101 keirrrvgvvfqfaeyqlfeqTIEKDIIFGPV-SMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 161 LTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFF 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-209 |
1.19e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGfLSPVDGEIRLDG------QPV--TR 83
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKIL----EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGrveffnQNIyeRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 PGPDRI-----MVFQEFDQLPpwKTVLENTLFPL-------------VASRQATRAEAEERARYFLNKVGLakfadayph 145
Cdd:PRK14258 81 VNLNRLrrqvsMVHPKPNLFP--MSVYDNVAYGVkivgwrpkleiddIVESALKDADLWDEIKHKIHKSAL--------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 146 TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEE 209
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-205 |
1.20e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.10 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGG---FLSPVDGE-IRLDGQPVTR----- 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidYPGRVMAEkLEFNGQDLQRiseke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 ----PGPDRIMVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGL---AKFADAYPHTLSGGMKQRV 155
Cdd:PRK11022 83 rrnlVGAEVAMIFQDpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITH 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-220 |
1.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRtRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--- 89
Cdd:PRK13642 4 ILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 --MVFQEFDQLPPWKTVLENTLFPLvASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKV 167
Cdd:PRK13642 83 igMVFQNPDNQFVGATVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 168 LLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEAlIVGSRVLLL 220
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-220 |
1.47e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 4 HSPDTVTQPLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR 83
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 P-------------------GPDRIMVFQE-FDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAK---FA 140
Cdd:PRK10261 83 RsrqvielseqsaaqmrhvrGADMAMIFQEpMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEaqtIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 141 DAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-212 |
1.68e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.62 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 2 THHSPDTVTQPLLQV-DSVGLEYRTRRSLVRAthDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLS--PVDGEIRLDG 78
Cdd:COG2401 16 VYSSVLDLSERVAIVlEAFGVELRVVERYVLR--DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 79 QPVtrpGPDRIMVfqefDQLPPWKTVLEntlfplvasrqatraeaeerARYFLNKVGLAkfaDAY-----PHTLSGGMKQ 153
Cdd:COG2401 94 NQF---GREASLI----DAIGRKGDFKD--------------------AVELLNAVGLS---DAVlwlrrFKELSTGQKF 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 154 RVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH--SIEEALI 212
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-207 |
2.07e-19 |
|
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: 84.44 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 5 SPDTVtQPLLQVDSVGLEYRTRrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRP 84
Cdd:cd03248 4 APDHL-KGIVKFQNVTFAYPTR-PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 85 GPDRI-----MVFQE---FDqlppwKTVLENTLFPL--VASRQATRAEAEERARYFLNKV--GLAKFADAYPHTLSGGMK 152
Cdd:cd03248 82 EHKYLhskvsLVGQEpvlFA-----RSLQDNIAYGLqsCSFECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 153 QRVAIARALTMQPKVLLMDEPFAALDALTRRKMQeELLALWEEVRfTLLFVTHSI 207
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQ-QALYDWPERR-TVLVIAHRL 209
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
32-209 |
2.82e-19 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 83.99 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVLENtlfp 111
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPPLYENLTAREN---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 lVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALtrrKMQE--EL 189
Cdd:TIGR03740 91 -LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPI---GIQElrEL 166
|
170 180
....*....|....*....|
gi 2316062753 190 LALWEEVRFTLLFVTHSIEE 209
Cdd:TIGR03740 167 IRSFPEQGITVILSSHILSE 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
36-179 |
3.10e-19 |
|
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: 83.31 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVL---ENTLF-- 110
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLsvlENLRFwh 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 111 PLVASRQATRAeaeeraryfLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:cd03231 99 ADHSDEQVEEA---------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-178 |
4.34e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG-----------PDRIMVFQEFDQl 98
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaraasrrvasvPQDTSLSFEFDV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 99 ppwKTVLENTLFPLVaSRQATRAEAEERA-RYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAAL 177
Cdd:PRK09536 95 ---RQVVEMGRTPHR-SRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
.
gi 2316062753 178 D 178
Cdd:PRK09536 171 D 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-210 |
5.17e-19 |
|
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: 86.69 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 6 PDTVTQPL------LQVDSVGLEYRTRRslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQ 79
Cdd:TIGR02203 317 KDTGTRAIerargdVEFRNVTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 80 PVTRPGPDRI-----MVFQE---FDQlppwkTVLENTLFPlvASRQATRAEAEERARyflnKVGLAKFADAYP---HT-- 146
Cdd:TIGR02203 395 DLADYTLASLrrqvaLVSQDvvlFND-----TIANNIAYG--RTEQADRAEIERALA----AAYAQDFVDKLPlglDTpi 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 147 ------LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEvRFTLLfVTH---SIEEA 210
Cdd:TIGR02203 464 gengvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLV-IAHrlsTIEKA 534
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-220 |
5.36e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGLEYrtrrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI 89
Cdd:PRK09700 2 ATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ------MVFQEF---DQLppwkTVLENtlfpLVASRQATR----------AEAEERARYFLNKVGLAKFADAYPHTLSGG 150
Cdd:PRK09700 78 aqlgigIIYQELsviDEL----TVLEN----LYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 151 MKQRVAIARALTMQPKVLLMDEPFAALDaltrRKMQEELLALWEEVR---FTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLT----NKEVDYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVM 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-221 |
1.02e-18 |
|
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: 82.77 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 23 YRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQpvtRPGPDRI-------MVFQEF 95
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKkflrrigVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 96 DQLPpWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFA 175
Cdd:cd03267 104 TQLW-WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 176 ALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-250 |
1.59e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 41 FPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDG-----EIRLDGQPV----------TRPGpdriMVFQEFDQLPpwKTV 104
Cdd:PRK14271 44 FPARAVTsLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrdvlefrRRVG----MLFQRPNPFP--MSI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 105 LENTLFPLVASRQATRAEAEERARYFLNKVGL-----AKFADAyPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PRK14271 118 MDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavkDRLSDS-PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 180 LTRRKMQEELLALWEevRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQFALSDQGSEAFQTTA 250
Cdd:PRK14271 197 TTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALF--FDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-231 |
7.28e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 1 MTHHSPDTVTQPLLQVDsvGLeyrTRRSLVratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQP 80
Cdd:COG1129 244 LFPKRAAAPGEVVLEVE--GL---SVGGVV---RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 81 VTRPGP-------------DRIM--VFQEFDqlppwktVLENTLFPLVA--------SRQATRAEAEEraryFLNKVGLa 137
Cdd:COG1129 316 VRIRSPrdairagiayvpeDRKGegLVLDLS-------IRENITLASLDrlsrggllDRRRERALAEE----YIKRLRI- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 138 KFADAYPH--TLSGGMKQRVAIARALTMQPKVLLMDEP------------FAALDALTRRKMqeellalweevrfTLLFV 203
Cdd:COG1129 384 KTPSPEQPvgNLSGGNQQKVVLAKWLATDPKVLILDEPtrgidvgakaeiYRLIRELAAEGK-------------AVIVI 450
|
250 260
....*....|....*....|....*...
gi 2316062753 204 THSIEEALIVGSRVLLLspHPGRVRAEI 231
Cdd:COG1129 451 SSELPELLGLSDRILVM--REGRIVGEL 476
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-189 |
1.56e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRslvRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQ---PVTRPGPDRI 89
Cdd:PRK13657 334 AVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 M--VFQE---FDqlppwKTVLENTLfplVASRQATRAE---AEERARY--FLNK--VGLAKFADAYPHTLSGGMKQRVAI 157
Cdd:PRK13657 411 IavVFQDaglFN-----RSIEDNIR---VGRPDATDEEmraAAERAQAhdFIERkpDGYDTVVGERGRQLSGGERQRLAI 482
|
170 180 190
....*....|....*....|....*....|..
gi 2316062753 158 ARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-222 |
2.40e-17 |
|
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: 77.58 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGfLSPV-DGEIrldgqpvTRPGPDRIMvf 92
Cdd:cd03223 1 IELENLSLATPDGRVLLK---DLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRI-------GMPEGEDLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 93 qeFdqLPpwktvlENTLFPLVASRQATraeaeeraryflnkvglakfadAYP--HTLSGGMKQRVAIARALTMQPKVLLM 170
Cdd:cd03223 68 --F--LP------QRPYLPLGTLREQL----------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 171 DEPFAALDAltrrKMQEELLALWEEVRFTLLFVTHSiEEALIVGSRVLLLSP 222
Cdd:cd03223 116 DEATSALDE----ESEDRLYQLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
34-229 |
3.06e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 81.33 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVF-----QE---FDqlppwKTVL 105
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHigylpQDvelFD-----GTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 EN-TLFPlvasrQATRAEAEERARyflnKVGL----AKFADAY-------PHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:COG4618 424 ENiARFG-----DADPEKVVAAAK----LAGVhemiLRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 174 FAALDALTRRKMQEELLALWEEVRfTLLFVTHSIeEALIVGSRVLLLspHPGRVRA 229
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKARGA-TVVVITHRP-SLLAAVDKLLVL--RDGRVQA 546
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-221 |
3.80e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRslvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT--------RP 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 85 G----PDRIMVFQEFdqlppwkTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARA 160
Cdd:PRK10895 79 GigylPQEASIFRRL-------SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 161 LTMQPKVLLMDEPFAALDALTR---RKMQEELlalwEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVidiKRIIEHL----RDSGLGVLITDHNVRETLAVCERAYIVS 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
48-230 |
5.66e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD----RIMVFQEFDQLPPWKTVLE---NTLFPLVASRQATR 120
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarRIGLLAQNATTPGDITVQElvaRGRYPHQPLFTRWR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 121 AEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTL 200
Cdd:PRK10253 118 KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTL 197
|
170 180 190
....*....|....*....|....*....|
gi 2316062753 201 LFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:PRK10253 198 AAVLHDLNQACRYASHLIAL--REGKIVAQ 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
7.60e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 1 MTHHspDTVTQPLLQVDSVGLEYrtrrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQP 80
Cdd:PRK15439 1 MQTS--DTTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 81 VTRPGPDRI------MVFQEfDQLPPWKTVLENTLFPLvasrqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQR 154
Cdd:PRK15439 75 CARLTPAKAhqlgiyLVPQE-PLLFPNLSVKENILFGL-----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 155 VAIARALTMQPKVLLMDEPFAALD-ALTRRKMQE--ELLALweevRFTLLFVTHSIEEALIVGSRV 217
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTpAETERLFSRirELLAQ----GVGIVFISHKLPEIRQLADRI 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
47-208 |
1.08e-16 |
|
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: 76.99 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 47 VLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEFD----QLPPW---KTVLENTLFPLVASRQat 119
Cdd:cd03290 31 MIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvayaAQKPWllnATVEENITFGSPFNKQ-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 120 raeaeeRARYFLNKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA-LTRRKMQE 187
Cdd:cd03290 109 ------RYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQE 182
|
170 180
....*....|....*....|.
gi 2316062753 188 ELLALWEEVRFTLLFVTHSIE 208
Cdd:cd03290 183 GILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-207 |
1.80e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 9 VTQPLLQVDSVGLEYRTRRSlvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDR 88
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 IMVFQEFDQLPPWKtvlentlFPLVASRQAT-----------RAEAEERARY--FLNKVGLAKFADAYPHTLSGGMKQRV 155
Cdd:PRK15056 79 LVAYVPQSEEVDWS-------FPVLVEDVVMmgryghmgwlrRAKKRDRQIVtaALARVDMVEFRHRQIGELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSI 207
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNL 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-230 |
1.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDG----QPVTRPGPDRI--MVFQEFDQLPPWKTVL 105
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIRKLvgIVFQNPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 106 ENTLF--------PLVASRQATRAEAEeraryflnkVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAAL 177
Cdd:PRK13644 97 EDLAFgpenlclpPIEIRKRVDRALAE---------IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 178 DALTRRKMQEELLALWEEVRfTLLFVTHSIEEaLIVGSRVLLLSphPGRVRAE 230
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMD--RGKIVLE 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
31-210 |
1.95e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 31 RATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMvfQEFDQLPPWKTVLEN-TL 109
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--RRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRQAT------RAEAEERAR--YFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDaLT 181
Cdd:PRK11231 94 RELVAYGRSPwlslwgRLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD-IN 172
|
170 180 190
....*....|....*....|....*....|..
gi 2316062753 182 RrkmQEELLALWEEVRF---TLLFVTHSIEEA 210
Cdd:PRK11231 173 H---QVELMRLMRELNTqgkTVVTVLHDLNQA 201
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
35-205 |
3.76e-16 |
|
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: 73.64 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDgqPVTRPGpdrimvfqefdqlppwktvlentlfplva 114
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--STVKIG----------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 srqatraeaeerarYFlnkvglakfadaypHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALwe 194
Cdd:cd03221 67 --------------YF--------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY-- 116
|
170
....*....|.
gi 2316062753 195 evRFTLLFVTH 205
Cdd:cd03221 117 --PGTVILVSH 125
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-208 |
6.47e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 74.84 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRtrRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI---- 89
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrsri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 -MVFQE---FDqlppwKTVLENtLFPLvasrqaTRAEAEERARYfLNKVGLAKFADAYPHTL-----------SGGMKQR 154
Cdd:cd03244 81 sIIPQDpvlFS-----GTIRSN-LDPF------GEYSDEELWQA-LERVGLKEFVESLPGGLdtvveeggenlSVGQRQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 155 VAIARALTMQPKVLLMDEPFAALDALTRRKMQEellALWEEvrF---TLLFVTHSIE 208
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQK---TIREA--FkdcTVLTIAHRLD 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-223 |
6.64e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRldgqpvtRPGPDRIMV 91
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL----SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 FqefdqlpPWKTVLENTLfPLVASRQATRAEAEERARYF--LNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLL 169
Cdd:PRK09544 72 V-------PQKLYLDTTL-PLTVNRFLRLRPGTKKEDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 170 MDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLSPH 223
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
48-185 |
1.03e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV--TRPG-----PDRIMVFQEFDQLPPWKTVLENTLFPLvasRQATR 120
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGllalrQQVATVFQDPEQQIFYTDIDSDIAFSL---RNLGV 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062753 121 AEAE--ERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKM 185
Cdd:PRK13638 109 PEAEitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-209 |
1.92e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT--------RPGPDRI-MVFQefdqLPpwk 102
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyiRPVRKRIgMVFQ----FP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 103 tvlENTLFPLVASRQATRA---------EAEERARYFLNKVGLAK-FADAYPHTLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:PRK13646 95 ---ESQLFEDTVEREIIFGpknfkmnldEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316062753 173 PFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEE 209
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNE 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-187 |
5.00e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 4 HSPDTVtQPLLQVDSVGLEYRTRRSlVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTr 83
Cdd:TIGR00958 470 LAPLNL-EGLIEFQDVSFSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 84 pgpdrimvfqEFD------------QLPPW--KTVLENTLFPLvasRQATRAEAEERARyflnKVGLAKFADAYPHT--- 146
Cdd:TIGR00958 547 ----------QYDhhylhrqvalvgQEPVLfsGSVRENIAYGL---TDTPDEEIMAAAK----AANAHDFIMEFPNGydt 609
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316062753 147 --------LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQE 187
Cdd:TIGR00958 610 evgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE 658
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-189 |
1.46e-14 |
|
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: 71.36 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 20 GLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQE 94
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLrrqvgVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 fdqlppwktvleNTLFP-LVASRQATRAEAEERARYflnkVGLAKFADAYPHT-----------------LSGGMKQRVA 156
Cdd:cd03252 85 ------------NVLFNrSIRDNIALADPGMSMERV----IEAAKLAGAHDFIselpegydtivgeqgagLSGGQRQRIA 148
|
170 180 190
....*....|....*....|....*....|...
gi 2316062753 157 IARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNM 181
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
34-205 |
1.91e-14 |
|
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: 70.25 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLS--PVDGEIRLDGQPVTrpgpdrimvfqefdQLPPwktvlentlfp 111
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDIT--------------DLPP----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 lvasrqatraeaEERAR--YFL--------NKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD--A 179
Cdd:cd03217 72 ------------EERARlgIFLafqyppeiPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidA 139
|
170 180
....*....|....*....|....*.
gi 2316062753 180 LtrrKMQEELLALWEEVRFTLLFVTH 205
Cdd:cd03217 140 L---RLVAEVINKLREEGKSVLIITH 162
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-179 |
2.00e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP---VDGEIRLDGQPVTRPGPDRIMVF-QEFDQLPPWKTVLENTL 109
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYvQQDDLFIPTLTVREHLM 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 110 FP--LVASRQATRAEAEERARYFLNKVGLAKFAD------AYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:TIGR00955 122 FQahLRMPRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-178 |
3.11e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.50 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDvFPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTR-PGPD---RIMVFQEFDQLPPWKTVLEnt 108
Cdd:COG4604 18 DDVSLT-IPKGGITaLIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRElakRLAILRQENHINSRLTVRE-- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 109 lfpLVA------SRQATRAEAEE---RARYFLNkvgLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD 178
Cdd:COG4604 95 ---LVAfgrfpySKGRLTAEDREiidEAIAYLD---LEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
38-178 |
4.07e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 38 FDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFqeFDQLPPWK---TVLENTLFplVA 114
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY--LGHLPGLKadlSTLENLHF--LC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 115 SRQATRAEaeERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD 178
Cdd:PRK13543 108 GLHGRRAK--QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-258 |
4.31e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTrrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG-PDRIMV 91
Cdd:PLN03232 1234 SIKFEDVHLRYRP--GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 92 FQEFDQLPP-WKTVLENTLFPLVASRQATRAEAEERARY----FLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:PLN03232 1312 LSIIPQSPVlFSGTVRFNIDPFSEHNDADLWEALERAHIkdviDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 167 VLLMDEPFAAL----DALTRRKMQEELLALweevrfTLLFVTHSIeEALIVGSRVLLLSphPGRVrAEINCHQFALSDQG 242
Cdd:PLN03232 1392 ILVLDEATASVdvrtDSLIQRTIREEFKSC------TMLVIAHRL-NTIIDCDKILVLS--SGQV-LEYDSPQELLSRDT 1461
|
250 260
....*....|....*....|...
gi 2316062753 243 SEAFQ-------TTAQRIHHLLF 258
Cdd:PLN03232 1462 SAFFRmvhstgpANAQYLSNLVF 1484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-220 |
4.97e-14 |
|
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: 72.35 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 40 VFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDrimVFQEFDQLPPWKTVLE-----NTLFPLVA 114
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQNMGYCPQFDAIDDlltgrEHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 SRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWE 194
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170 180
....*....|....*....|....*.
gi 2316062753 195 EVRFTLLfVTHSIEEALIVGSRVLLL 220
Cdd:TIGR01257 2119 EGRAVVL-TSHSMEECEALCTRLAIM 2143
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-260 |
5.17e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.87 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGfLSPVDGEIRLDGQPVTR-PGPD----RIMVFQefDQLPPwktvlenTLF 110
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDwSAAElarhRAYLSQ--QQSPP-------FAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 P------LVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALtMQ--------PKVLLMDEPFAA 176
Cdd:COG4138 85 PvfqylaLHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVL-LQvwptinpeGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 177 LD-----ALTRrkmqeeLLAlweevRFTLLFVT-----HSIEEALIVGSRVLLLspHPGRVRAEINCHQFALSDQGSEAF 246
Cdd:COG4138 164 LDvaqqaALDR------LLR-----ELCQQGITvvmssHDLNHTLRHADRVWLL--KQGKLVASGETAEVMTPENLSEVF 230
|
250
....*....|....*...
gi 2316062753 247 QTTAQRI----HHLLFPT 260
Cdd:COG4138 231 GVKFRRLevegHRWLIPT 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
42-192 |
5.94e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 42 PAERFVLLGPSGCGKSSLLKSIGGFL--SPVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVLENTLFP--LVASRQ 117
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCslLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 118 ATRAEAEERARYFLNKVGLAK-----FADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLAL 192
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-177 |
8.39e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKsiggFLSPV------DGEIRLDGQPVT----RPGPDR--IMVFQEFdQ 97
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMK----VLSGVyphgsyEGEILFDGEVCRfkdiRDSEALgiVIIHQEL-A 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 98 LPPWKTVLENtLFplVASRQATR-----AEAEERARYFLNKVGLakfaDAYPHTLSG----GMKQRVAIARALTMQPKVL 168
Cdd:NF040905 89 LIPYLSIAEN-IF--LGNERAKRgvidwNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLL 161
|
....*....
gi 2316062753 169 LMDEPFAAL 177
Cdd:NF040905 162 ILDEPTAAL 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-221 |
1.43e-13 |
|
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: 68.21 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 20 GLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMvfQEFDQLP 99
Cdd:cd03369 11 NLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR--SSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 100 PWKTVLENTLfplvasrqatRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:cd03369 89 QDPTLFSGTI----------RSNLDPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316062753 180 LTRRKMQEELLALWEEVrfTLLFVTHSIeEALIVGSRVLLLS 221
Cdd:cd03369 159 ATDALIQKTIREEFTNS--TILTIAHRL-RTIIDYDKILVMD 197
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-205 |
2.18e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 15 QVDSVGLEYRTRRSLVratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP----VDGEIRLDGQPV---TRPGPD 87
Cdd:PRK10418 4 QIELRNIALQAAQPLV---HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapcALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RIMVFQE----FDQLPPWKTVLENTLfplvasRQATRAEAEERARYFLNKVGL---AKFADAYPHTLSGGMKQRVAIARA 160
Cdd:PRK10418 81 IATIMQNprsaFNPLHTMHTHARETC------LALGKPADDATLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316062753 161 LTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTH 199
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-208 |
3.72e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.39 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP-----VDgEIRLDGQPVTRPGP 86
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtAD-RFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 ---------DRIMVFQE-----------FDQL----PPWKtvLENTLFplvaSRQATRAEaeeRARYFLNKVGLAKFAD- 141
Cdd:COG4170 81 rerrkiigrEIAMIFQEpsscldpsakiGDQLieaiPSWT--FKGKWW----QRFKWRKK---RAIELLHRVGIKDHKDi 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 142 --AYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIE 208
Cdd:COG4170 152 mnSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLE 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-216 |
3.86e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYrtrrSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIM 90
Cdd:PRK11614 3 KVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 91 -----VFQEFDQLPPWKTVLENTLfplVASRQATRAEAEERaryflnkvgLAKFADAYPH----------TLSGGMKQRV 155
Cdd:PRK11614 79 reavaIVPEGRRVFSRMTVEENLA---MGGFFAERDQFQER---------IKWVYELFPRlherriqragTMSGGEQQML 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEvRFTLLFVTHSIEEALIVGSR 216
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADR 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-181 |
3.91e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 10 TQPLLQVDSVGleyrtrRSL--VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPD 87
Cdd:PRK10762 1 MQALLQLKGID------KAFpgVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RI------MVFQEFDqLPPWKTVLENTLFplvaSRQATRA-------EAEERARYFLNKVGLAKFADAYPHTLSGGMKQR 154
Cdd:PRK10762 75 SSqeagigIIHQELN-LIPQLTIAENIFL----GREFVNRfgridwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQM 149
|
170 180
....*....|....*....|....*..
gi 2316062753 155 VAIARALTMQPKVLLMDEPfaaLDALT 181
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEP---TDALT 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-220 |
4.56e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPgpdrimvfqefdQLPPWKT---VLENT 108
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL------------QLDSWRSrlaVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 109 LFPL---VASR------QATRAEAEERARYFLNKVGLAKFADAYPH-------TLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:PRK10789 398 PFLFsdtVANNialgrpDATQQEIEHVARLASVHDDILRLPQGYDTevgergvMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316062753 173 PFAALDALTRRKMQEElLALWEEVRfTLLFVTHSIeEALIVGSRVLLL 220
Cdd:PRK10789 478 ALSAVDGRTEHQILHN-LRQWGEGR-TVIISAHRL-SALTEASEILVM 522
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-221 |
1.31e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRpgpDRIMVF 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLL----QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK---DLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 93 QEF------DQLPPWKTVLENTLFPLVASrqATRAEAEERARYFlnkvGLAKFADAYPHTLSGGMKQRVAIARALTMQPK 166
Cdd:PRK13540 74 KQLcfvghrSGINPYLTLRENCLYDIHFS--PGAVGITELCRLF----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 167 VLLMDEPFAALDALtrrkmqeellalweevrfTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK13540 148 LWLLDEPLVALDEL------------------SLLTIITKIQEHRAKGGAVLLTS 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-209 |
1.50e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKsiggFLSPV------DGEIRLDGQPVT--------RPGPdrIMVFQEF 95
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMK----VLSGVyphgtyEGEIIFEGEELQasnirdteRAGI--AIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 96 dQLPPWKTVLENtLFplvASRQATR------AEAEERARYFLNKVGLakfaDAYPHT----LSGGMKQRVAIARALTMQP 165
Cdd:PRK13549 92 -ALVKELSVLEN-IF---LGNEITPggimdyDAMYLRAQKLLAQLKL----DINPATpvgnLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316062753 166 KVLLMDEPFAALDAltrrKMQEELLALWEEVR---FTLLFVTHSIEE 209
Cdd:PRK13549 163 RLLILDEPTASLTE----SETAVLLDIIRDLKahgIACIYISHKLNE 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-227 |
1.69e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.65 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 22 EYRTrrslVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGqpvTRPGPDRI-------MVF-- 92
Cdd:COG4586 31 EYRE----VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKefarrigVVFgq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 93 --QEFDQLPPWKTvlentlFPLVAS-RQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLL 169
Cdd:COG4586 104 rsQLWWDLPAIDS------FRLLKAiYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 170 MDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIE--EALIvgSRVLLLspHPGRV 227
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEALC--DRVIVI--DHGRI 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
48-221 |
1.79e-12 |
|
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: 67.73 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTrpgPDRIMVFQEFDQLPPWK------TVLENTLFpLVASRQATRA 121
Cdd:TIGR01257 961 FLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE---TNLDAVRQSLGMCPQHNilfhhlTVAEHILF-YAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 122 EAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLAlWEEVRfTLL 201
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK-YRSGR-TII 1114
|
170 180
....*....|....*....|
gi 2316062753 202 FVTHSIEEALIVGSRVLLLS 221
Cdd:TIGR01257 1115 MSTHHMDEADLLGDRIAIIS 1134
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-205 |
2.12e-12 |
|
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: 66.88 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLdgqpvtRPGPDRIMVFQEfDQLPPWKTVLENtLFPLVA 114
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------QPGIKVGYLPQE-PQLDPTKTVREN-VEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 SRQATRAE--------AEERARY---------------------FLNKVGLAKFA------DAYPHTLSGGMKQRVAIAR 159
Cdd:TIGR03719 95 EIKDALDRfneisakyAEPDADFdklaaeqaelqeiidaadawdLDSQLEIAMDAlrcppwDADVTKLSGGERRRVALCR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 160 ALTMQPKVLLMDEPFAALDAltrrkmqeELLAlWEEvRF------TLLFVTH 205
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDA--------ESVA-WLE-RHlqeypgTVVAVTH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-284 |
2.12e-12 |
|
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: 67.24 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGqpvtrpgpdRIMVFQEFDQLPPwKTVLENTLFPLVA 114
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG---------RISFSPQTSWIMP-GTIKDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 SrqatraeaEERARYFLNKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRR 183
Cdd:TIGR01271 514 D--------EYRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 184 KMQEELLALWeEVRFTLLFVTHSIEEaLIVGSRVLLLspHPGRVR-----AEINCHQFALSDQ--GSEAF-QTTAQRIHH 255
Cdd:TIGR01271 586 EIFESCLCKL-MSNKTRILVTSKLEH-LKKADKILLL--HEGVCYfygtfSELQAKRPDFSSLllGLEAFdNFSAERRNS 661
|
250 260 270
....*....|....*....|....*....|....*.
gi 2316062753 256 LLFPT-------DVAAPSSVTSTQGKLYEHPAPRAA 284
Cdd:TIGR01271 662 ILTETlrrvsidGDSTVFSGPETIKQSFKQPPPEFA 697
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-210 |
2.81e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvrATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVT-------Rpgp 86
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytlaslR--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 DRI-MVFQE---FDQlppwkTVLENTLFPlvASRQATRAEAEERARY-----FLNKV--GLAKFADAYPHTLSGGMKQRV 155
Cdd:PRK11176 417 NQVaLVSQNvhlFND-----TIANNIAYA--RTEQYSREQIEEAARMayamdFINKMdnGLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTH---SIEEA 210
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHrlsTIEKA 545
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-192 |
4.98e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 2 THHSPDTVTQPLLQVDsvGLEYRTRRSlVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV 81
Cdd:COG3845 246 VEKAPAEPGEVVLEVE--NLSVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 82 TRPGPDRIM---------------VFQEFdqlppwkTVLENTLFPLVASRQATRaeaeeraRYFLNKVGLAKFA----DA 142
Cdd:COG3845 323 TGLSPRERRrlgvayipedrlgrgLVPDM-------SVAENLILGRYRRPPFSR-------GGFLDRKAIRAFAeeliEE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 143 Y------PHT----LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLAL 192
Cdd:COG3845 389 FdvrtpgPDTparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL 448
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-236 |
1.03e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 33 THDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DRI---MVF----QEFDQLPPWKTV 104
Cdd:PRK11288 269 REPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIragIMLcpedRKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 105 LENTLfplVASRQATRaeaeeRARYFLNKVGLAKFADAY--------PH------TLSGGMKQRVAIARALTMQPKVLLM 170
Cdd:PRK11288 349 ADNIN---ISARRHHL-----RAGCLINNRWEAENADRFirslniktPSreqlimNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 171 DEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGSRVLLLSphPGRVRAEINCHQF 236
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMR--EGRIAGELAREQA 483
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-221 |
1.40e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 13 LLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP--------VDGEIRLDGQPVTRP 84
Cdd:PRK13547 1 MLTADHLHVARRHRAIL----RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 85 GPDRIM----VFQEFDQLPPWKTVLENTL---FPLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAI 157
Cdd:PRK13547 77 DAPRLArlraVLPQAAQPAFAFSAREIVLlgrYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 158 ARAL---------TMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLS 221
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-209 |
1.48e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFL--SPVDGEIRLDGQPVTRPG---PDR---IMVFQEFdQLPPW 101
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNirdTERagiVIIHQEL-TLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 102 KTVLENTLFPLVASRQATR---AEAEERARYFLNKVGLAKFADAYP-HTLSGGMKQRVAIARALTMQPKVLLMDEPFAAL 177
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRmayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2316062753 178 DaltrRKMQEELLALWEEVR---FTLLFVTHSIEE 209
Cdd:TIGR02633 173 T----EKETEILLDIIRDLKahgVACVYISHKLNE 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
41-210 |
1.88e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 41 FPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV----TRPGPDRIMVFQEfdQLPPWK--TVLENTL---F 110
Cdd:PRK10575 34 FPAGKVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQ--QLPAAEgmTVRELVAigrY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 PLVASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAltrrKMQEELL 190
Cdd:PRK10575 112 PWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI----AHQVDVL 187
|
170 180
....*....|....*....|....
gi 2316062753 191 ALWEEVR----FTLLFVTHSIEEA 210
Cdd:PRK10575 188 ALVHRLSqergLTVIAVLHDINMA 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
35-225 |
2.22e-11 |
|
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: 62.95 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGqpvtrpgpdRIMVFQEFDQLPPwKTVLENTLFPLva 114
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---------RISFSSQFSWIMP-GTIKENIIFGV-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 srqatrAEAEERARYFLNKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRR 183
Cdd:cd03291 123 ------SYDEYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316062753 184 KMQEELLALWEEVRfTLLFVTHSIEEaLIVGSRVLLLspHPG 225
Cdd:cd03291 197 EIFESCVCKLMANK-TRILVTSKMEH-LKKADKILIL--HEG 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-227 |
3.30e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.33 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 16 VDSVGLEYRTRRSL-VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIrLDGQPVTRPGPDRI----- 89
Cdd:PRK13645 9 LDNVSYTYAKKTPFeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANLKKIkevkr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 90 ------MVFQeFDQLPPWKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAK-FADAYPHTLSGGMKQRVAIARALT 162
Cdd:PRK13645 88 lrkeigLVFQ-FPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 163 MQPKVLLMDEPFAALDAltrrKMQEELLALWE----EVRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDP----KGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVIVM--HEGKV 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-181 |
3.54e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 8 TVTQPLLQVDSVGLeyrtrRSLVRATHDVSFDVF--------PAERFVLLGPSGCGKSSLLKSIG----GFLSPVDGEIR 75
Cdd:TIGR00956 49 TFPNALLKILTRGF-----RKLKKFRDTKTFDILkpmdglikPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVIT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 76 LDGQPvtrpgPDRIMVF--------QEFDQLPPWKTVLENTLFPLVASRQATRAE-------AEERARYFLNKVGLA--- 137
Cdd:TIGR00956 124 YDGIT-----PEEIKKHyrgdvvynAETDVHFPHLTVGETLDFAARCKTPQNRPDgvsreeyAKHIADVYMATYGLShtr 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316062753 138 --KFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:TIGR00956 199 ntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-181 |
3.90e-11 |
|
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: 61.12 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSP---VDGEIRLDGQPV----TRPGPDRIMVFQEfDQLPPWKTVLE 106
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYkefaEKYPGEIIYVSEE-DVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 107 NTLFPLvasrqatraeaeeRARyflnkvglakfADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:cd03233 103 TLDFAL-------------RCK-----------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-262 |
4.84e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 24 RTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGpdrIMVFQEFDQLPPWKT 103
Cdd:PLN03130 1246 RYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAP 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLEN-----TLFPLVASRQATRAEAEERARY----FLNKVGL-AKFADAyPHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:PLN03130 1323 VLFSgtvrfNLDPFNEHNDADLWESLERAHLkdviRRNSLGLdAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 174 FAAL----DALTRRKMQEELLALweevrfTLLFVTHSIeEALIVGSRVLLLSphPGRVrAEINCHQFALSDQGSeAF--- 246
Cdd:PLN03130 1402 TAAVdvrtDALIQKTIREEFKSC------TMLIIAHRL-NTIIDCDRILVLD--AGRV-VEFDTPENLLSNEGS-AFskm 1470
|
250 260
....*....|....*....|.
gi 2316062753 247 -QTT----AQRIHHLLFPTDV 262
Cdd:PLN03130 1471 vQSTgaanAQYLRSLVFGGDE 1491
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
34-235 |
5.55e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAErfvLLGPSG---CGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-------------DRimvfqEFDQ 97
Cdd:PRK10762 269 NDVSFTLRKGE---ILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdglangivyiseDR-----KRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 98 LPPWKTVLENtlFPLVASRQATRA-----EAEERA------RYFLNK-------VGLakfadayphtLSGGMKQRVAIAR 159
Cdd:PRK10762 341 LVLGMSVKEN--MSLTALRYFSRAggslkHADEQQavsdfiRLFNIKtpsmeqaIGL----------LSGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 160 ALTMQPKVLLMDEPFAALDALTRRKMQeELLALWEEVRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAEINCHQ 235
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIY-QLINQFKAEGLSIILVSSEMPEVLGMSDRILVM--HEGRISGEFTREQ 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-225 |
8.51e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 44 ERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPgPDRImvfqEFDQlppwktvlENTLFPLVASRQATRAEA 123
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-PQYI----KADY--------EGTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 124 EERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFV 203
Cdd:cd03237 93 PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVV 172
|
170 180
....*....|....*....|..
gi 2316062753 204 THSIEEALIVGSRVLLLSPHPG 225
Cdd:cd03237 173 EHDIIMIDYLADRLIVFEGEPS 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
45-215 |
9.44e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 45 RFVLLGPSGCGKSSLLKSIGGFLSPVDGEirldgqpVTRPGPDRIMVFQEFDQlppwkTVLENTLFPLVASRQATRAEAE 124
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGT-------VFRSAKVRMAVFSQHHV-----DGLDLSSNPLLYMMRCFPGVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 125 ERARYFLNKVGLAKFADAYP-HTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDaLTRRKMQEELLALWEEvrfTLLFV 203
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVEALIQGLVLFQG---GVLMV 680
|
170
....*....|..
gi 2316062753 204 THsiEEALIVGS 215
Cdd:PLN03073 681 SH--DEHLISGS 690
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-173 |
1.05e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPV------TRpgpDRI--MVfQEFD---QLppwkT 103
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiaTR---RRVgyMS-QAFSlygEL----T 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 104 VLEN-----TLFPLVASRQATR-AEAEERaryFlnkvGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:NF033858 356 VRQNlelhaRLFHLPAAEIAARvAEMLER---F----DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-183 |
1.11e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 15 QVDSVGLEYRTrrslVRATHDVSFDVfPAERFV-LLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRP------GPd 87
Cdd:NF033858 3 RLEGVSHRYGK----TVALDDVSLDI-PAGCMVgLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrravCP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 88 RI--MvfqefDQ-----LPPWKTVLEN-----TLFPLvasrqaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRV 155
Cdd:NF033858 77 RIayM-----PQglgknLYPTLSVFENldffgRLFGQ------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180
....*....|....*....|....*...
gi 2316062753 156 AIARALTMQPKVLLMDEPFAALDALTRR 183
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-236 |
1.26e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSpVDGEIRLDGqpvtrpgpdrimVFQEFDQLPPWKT---VLENTLFP 111
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG------------VSWNSVTLQTWRKafgVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LVASrqaTRAEAEERARY-------FLNKVGLAKFADAYP-----------HTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:TIGR01271 1304 FSGT---FRKNLDPYEQWsdeeiwkVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 174 FAALDALTrrkmqeellalWEEVRFTLlfvTHSIEEALIVgsrvllLSPHpgRVRAEINCHQF 236
Cdd:TIGR01271 1381 SAHLDPVT-----------LQIIRKTL---KQSFSNCTVI------LSEH--RVEALLECQQF 1421
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-179 |
3.95e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLdgQPVTRPGpdriMVFQEfDQLPPWKTVLEN------- 107
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIKVG----YLPQE-PQLDPEKTVRENveegvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 108 -----TLFPLVASRQATR-----AEAEERARyfL-------------NKVGLAKFA------DAYPHTLSGGMKQRVAIA 158
Cdd:PRK11819 98 vkaalDRFNEIYAAYAEPdadfdALAAEQGE--LqeiidaadawdldSQLEIAMDAlrcppwDAKVTKLSGGERRRVALC 175
|
170 180
....*....|....*....|.
gi 2316062753 159 RALTMQPKVLLMDEPFAALDA 179
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDA 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-241 |
4.75e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 143 YPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIeeALIVGSRVLLLSP 222
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI--ASIKRSDKIVVFN 1432
|
90 100
....*....|....*....|...
gi 2316062753 223 HPGR----VRAEiNCHQFALSDQ 241
Cdd:PTZ00265 1433 NPDRtgsfVQAH-GTHEELLSVQ 1454
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-210 |
7.46e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 11 QPLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGG------------F------------ 66
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPIL----HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFgrrrgsgetiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 67 ----LSPVDGEIRLDGQPVTRPgpdrimvfqefdqlppwKTVLENTLFPLVASRQATRAEAEERARYFLNKVGLAK-FAD 141
Cdd:PRK10938 334 ikkhIGYVSSSLHLDYRVSTSV-----------------RNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTAD 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 142 AYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIEEA 210
Cdd:PRK10938 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
35-205 |
1.50e-09 |
|
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: 58.61 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGfLSPVDGEIRldgqpvTRPGPDRIMVfqefdqLP--PW---KTVLENTL 109
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRL------TKPAKGKLFY------VPqrPYmtlGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRQATRAEAEERARYFLNKV----------GLAKFADaYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:TIGR00954 537 YPDSSEDMKRRGLSDKDLEQILDNVqlthileregGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*.
gi 2316062753 180 ltrrKMQEELLALWEEVRFTLLFVTH 205
Cdd:TIGR00954 616 ----DVEGYMYRLCREFGITLFSVSH 637
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-209 |
1.66e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 42 PAERFVLLGPSGCGKSSLLKSIGGFLSPVDGE-IRLDGqpvtrpgpdrimvfqefdqlppwktvlentlfplvasrqatr 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 121 aeaeERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEE-----LLALWEE 195
Cdd:smart00382 39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114
|
170
....*....|....
gi 2316062753 196 VRFTLLFVTHSIEE 209
Cdd:smart00382 115 KNLTVILTTNDEKD 128
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-207 |
1.94e-09 |
|
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: 58.42 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 27 RSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVfqefdqlppwKTVLE 106
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQN----------DSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 107 NTLFplvasrqaTRAEAEERARYFLNKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPFA 175
Cdd:TIGR00957 718 NILF--------GKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316062753 176 ALDALTRRKMQEELLA----LWEEVRftlLFVTHSI 207
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHGI 822
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-205 |
2.61e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGF--LSPVDGEI----------------R 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL----KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 76 LDGQP---------------------VTRPGPDRI-MVFQEFDQLPPWKTVLENTLFPLVASRQATRaEAEERARYFLNK 133
Cdd:TIGR03269 77 KVGEPcpvcggtlepeevdfwnlsdkLRRRIRKRIaIMLQRTFALYGDDTVLDNVLEALEEIGYEGK-EAVGRAVDLIEM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 134 VGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-178 |
3.38e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGfLSPVDGEIRLDGQPV-TRPGPD----RIMVFQEfdQLPPwktvlenTLF 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLeAWSAAElarhRAYLSQQ--QTPP-------FAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 P----LVASRQATRAEAEERA--RYFLNKVGLAKFADAYPHTLSGGMKQRVAIA-------RALTMQPKVLLMDEPFAAL 177
Cdd:PRK03695 85 PvfqyLTLHQPDKTRTEAVASalNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL 164
|
.
gi 2316062753 178 D 178
Cdd:PRK03695 165 D 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-231 |
4.31e-09 |
|
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: 56.76 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 4 HSPDTVTQPLLQVDSVGLEYRTRRSLVRaTHDVSFDVFPAERFVLLGPSGCGKSSLLKSI-GGFLSPVDGEIRLDGQPV- 81
Cdd:TIGR02633 248 HEPHEIGDVILEARNLTCWDVINPHRKR-VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVd 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 82 TRPGPDRI-----MVFQEF--DQLPPWKTVLEN-TLFPL--VASRQATRAEAEERA-RYFLNKVGLAKFADAYPHT-LSG 149
Cdd:TIGR02633 327 IRNPAQAIragiaMVPEDRkrHGIVPILGVGKNiTLSVLksFCFKMRIDAAAELQIiGSAIQRLKVKTASPFLPIGrLSG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 150 GMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRA 229
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI--GEGKLKG 483
|
..
gi 2316062753 230 EI 231
Cdd:TIGR02633 484 DF 485
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-208 |
5.27e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 12 PLLQVDSVGLEYRTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGF----LSPVDGEIRLDGQPVTRPGP- 86
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 87 --------DRIMVFQEFDQ-LPPWKTVLENTLFPLVASRQATR-----AEAEERARYFLNKVGLAKFADA---YPHTLSG 149
Cdd:PRK15093 82 errklvghNVSMIFQEPQScLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIKDHKDAmrsFPYELTE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316062753 150 GMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTHSIE 208
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQ 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-205 |
5.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 27 RSLVRathDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIR----LDgqpvtrpgpdrimvFQEFDQ----L 98
Cdd:PRK11147 332 KQLVK---DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtkLE--------------VAYFDQhraeL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 99 PPWKTVLENtlfplVASRQATrAEAEERARYFLNKVGLAKFADAYPHT----LSGGMKQRVAIARALTMQPKVLLMDEPF 174
Cdd:PRK11147 395 DPEKTVMDN-----LAEGKQE-VMVNGRPRHVLGYLQDFLFHPKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170 180 190
....*....|....*....|....*....|.
gi 2316062753 175 AALDALTrRKMQEELLALWEEvrfTLLFVTH 205
Cdd:PRK11147 469 NDLDVET-LELLEELLDSYQG---TVLLVSH 495
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-190 |
5.86e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 6 PDTVTQPLLQVDSVGLEYRTRRSLvratHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG 85
Cdd:PRK10636 305 PESLPNPLLKMEKVSAGYGDRIIL----DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 86 PDRIMVFQEFDQLPpwktvLENTlfplvaSRQATRaEAEERARYFLNKVGLA--KFADAyPHTLSGGMKQRVAIARALTM 163
Cdd:PRK10636 381 AQHQLEFLRADESP-----LQHL------ARLAPQ-ELEQKLRDYLGGFGFQgdKVTEE-TRRFSGGEKARLVLALIVWQ 447
|
170 180
....*....|....*....|....*..
gi 2316062753 164 QPKVLLMDEPFAALDALTRRKMQEELL 190
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEALI 474
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-205 |
1.51e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 27 RSLVRATHDVSFDVFP-------AERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI-----MVFQE 94
Cdd:PRK10522 326 RNVTFAYQDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYrklfsAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 95 FDqlppwktvlentLFPLVASRQATRAEaEERARYFLNKVGLA--------KFADAyphTLSGGMKQRVAIARALTMQPK 166
Cdd:PRK10522 406 FH------------LFDQLLGPEGKPAN-PALVEKWLERLKMAhkleledgRISNL---KLSKGQKKRLALLLALAEERD 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316062753 167 VLLMDEPFAALDALTRRKMQEELLALWEEVRFTLLFVTH 205
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-210 |
1.52e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 119 TRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKmqeellaLWEEVR- 197
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE-------VWDEVRs 189
|
90
....*....|....*...
gi 2316062753 198 -----FTLLFVTHSIEEA 210
Cdd:NF000106 190 mvrdgATVLLTTQYMEEA 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
35-242 |
1.72e-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: 54.48 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSpVDGEIRLDG---QPVT----RPG----PDRIMVF-----QEFDQL 98
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswNSVPlqkwRKAfgviPQKVFIFsgtfrKNLDPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 99 PPWktvlentlfplvaSRQATRAEAEEraryflnkVGLAKFADAYP-----------HTLSGGMKQRVAIARALTMQPKV 167
Cdd:cd03289 101 GKW-------------SDEEIWKVAEE--------VGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 168 LLMDEPFAALDALTrrkmqeellalWEEVRFTLlfvTHSIEEALIVgsrvllLSPHpgRVRAEINCHQFALSDQG 242
Cdd:cd03289 160 LLLDEPSAHLDPIT-----------YQVIRKTL---KQAFADCTVI------LSEH--RIEAMLECQRFLVIEEN 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
42-178 |
1.83e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 42 PAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQpvtrpgpdriMVFQEFDQLPPwKTVlENTLFPLVASRQATRA 121
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD----------LIVARLQQDPP-RNV-EGTVYDFVAEGIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 122 EAEERARYFLNKVG----------LAKF--------------------------ADAYPHTLSGGMKQRVAIARALTMQP 165
Cdd:PRK11147 96 EYLKRYHDISHLVEtdpseknlneLAKLqeqldhhnlwqlenrinevlaqlgldPDAALSSLSGGWLRKAALGRALVSNP 175
|
170
....*....|...
gi 2316062753 166 KVLLMDEPFAALD 178
Cdd:PRK11147 176 DVLLLDEPTNHLD 188
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-213 |
2.46e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVLENTLFPLVA 114
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 115 SRQATRAEAEerARYFlnkvGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDAlTRRKMQEELLALWE 194
Cdd:PRK13541 98 YNSAETLYAA--IHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK-ENRDLLNNLIVMKA 170
|
170 180
....*....|....*....|..
gi 2316062753 195 EVRFTLLFVTH---SIEEALIV 213
Cdd:PRK13541 171 NSGGIVLLSSHlesSIKSAQIL 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-178 |
9.61e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 14 LQVDSVGLEYRTRRSlVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRP-----GPDR 88
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 89 IMVFQEfDQLPPWKTVLENTLFPLVA-----------------------SRQATRAEA-----------------EERAR 128
Cdd:PTZ00265 462 IGVVSQ-DPLLFSNSIKNNIKYSLYSlkdlealsnyynedgndsqenknKRNSCRAKCagdlndmsnttdsneliEMRKN 540
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316062753 129 YFL----------NKVGLAKFADAYP-----------HTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD 178
Cdd:PTZ00265 541 YQTikdsevvdvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-227 |
1.39e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGP-DRI---MVFqefdqLPP---------- 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLargLVY-----LPEdrqssglyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 ----WKTV-LENTLFPLVASRQATRAEAEeRARYFLNkvglAKFADAYP--HTLSGGMKQRVAIARALTMQPKVLLMDEP 173
Cdd:PRK15439 356 aplaWNVCaLTHNRRGFWIKPARENAVLE-RYRRALN----IKFNHAEQaaRTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 174 FAALDALTRRKMQEELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLspHPGRV 227
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVM--HQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
48-179 |
2.38e-07 |
|
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: 49.93 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLL------KSIGGflspVDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVLENTLFplvasrqatra 121
Cdd:cd03232 38 LMGESGAGKTTLLdvlagrKTAGV----ITGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRF----------- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316062753 122 eaeeraryflnkvglakfaDAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:cd03232 103 -------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-225 |
3.41e-07 |
|
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: 49.49 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 39 DVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDG-QPVTRPgpdrimvfQEFDqlppwktvlentlfplvasrq 117
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKP--------QYID--------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 118 atraeaeeraryflnkvglakfadayphtLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVR 197
Cdd:cd03222 72 -----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*...
gi 2316062753 198 FTLLFVTHSIEEALIVGSRVLLLSPHPG 225
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-179 |
4.18e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPV-DGEIRLDGQPVTRPGPDRImvfqeFDqlppwKTVLENTLF--P 111
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRGTVAYVPQVSWI-----FN-----ATVRDNILFgsP 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LVASR--QATRAEAEERARYFLNKVGLAKFADAYPHtLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PLN03130 705 FDPERyeRAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-191 |
5.15e-07 |
|
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: 50.70 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLdGQPVtrpgpDRIMVFQEFDQLPPWKTVLE-----NTL 109
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----KLAYVDQSRDALDPNKTVWEeisggLDI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRQATRAEAeerARYflN--------KVGLakfadayphtLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALT 181
Cdd:TIGR03719 414 IKLGKREIPSRAYV---GRF--NfkgsdqqkKVGQ----------LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
170
....*....|
gi 2316062753 182 RRKMQEELLA 191
Cdd:TIGR03719 479 LRALEEALLN 488
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-220 |
5.84e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.71 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 24 RTRRSLVRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPG----PDRIMVFQEFDQLp 99
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlRFKITIIPQDPVL- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 100 pWKTVLENTLFPLvasrqatRAEAEERARYFLNKVGLAKFADAYP-----------HTLSGGMKQRVAIARALTMQPKVL 168
Cdd:TIGR00957 1372 -FSGSLRMNLDPF-------SQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 169 LMDEPFAALDALTRRKMQEELLALWEEVrfTLLFVTHSIeEALIVGSRVLLL 220
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRL-NTIMDYTRVIVL 1492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-177 |
6.36e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 30 VRATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI------MVFQEFDQLPPwKT 103
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlengisMVHQELNLVLQ-RS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 VLENtlfpLVASRQATRAE-AEERARYFLNKvglAKFA----DAYPH----TLSGGMKQRVAIARALTMQPKVLLMDEPF 174
Cdd:PRK10982 90 VMDN----MWLGRYPTKGMfVDQDKMYRDTK---AIFDeldiDIDPRakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
...
gi 2316062753 175 AAL 177
Cdd:PRK10982 163 SSL 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-230 |
6.53e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSI-GGFLSPVDGEIRLDGQPVTRPGP-DRI-----MVFQEF--DQLPPWKTV 104
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPqQAIaqgiaMVPEDRkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 105 LEN-TLFPL--VASRQATRAEAEER-ARYFLNKVglaKFADAYPH----TLSGGMKQRVAIARALTMQPKVLLMDEPFAA 176
Cdd:PRK13549 359 GKNiTLAALdrFTGGSRIDDAAELKtILESIQRL---KVKTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 177 LDALTRRKMQEELLALWEEvRFTLLFVTHSIEEALIVGSRVLLLspHPGRVRAE 230
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVM--HEGKLKGD 486
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-209 |
7.67e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQpvtrpgpdrIMVFQEFDQLPPWKTVLENTLFP 111
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---------VSVIAISAGLSGQLTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LVAsRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD-ALTRR---KMQE 187
Cdd:PRK13546 110 MLC-MGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKcldKIYE 188
|
170 180
....*....|....*....|..
gi 2316062753 188 ellalWEEVRFTLLFVTHSIEE 209
Cdd:PRK13546 189 -----FKEQNKTIFFVSHNLGQ 205
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
45-189 |
1.06e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 45 RFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDgqPVTRPGPDR---------------IMVFQEFdqlppWKTVLE-NT 108
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD--PNERLGKLRqdqfafeeftvldtvIMGHTEL-----WEVKQErDR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 109 LFPL----------VASRQATRAE-----AEERARYFLNKVGLA-KFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDE 172
Cdd:PRK15064 102 IYALpemseedgmkVADLEVKFAEmdgytAEARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170
....*....|....*..
gi 2316062753 173 PFAALDALTRRKMQEEL 189
Cdd:PRK15064 182 PTNNLDINTIRWLEDVL 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
49-178 |
3.39e-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: 48.24 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 49 LGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRP---GPDRIMVFQEFdqlppwktvLENTLFPLVASrqaTRAEAEe 125
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPqyiSPDYDGTVEEF---------LRSANTDDFGS---SYYKTE- 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2316062753 126 raryFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD 178
Cdd:COG1245 439 ----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-228 |
5.75e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 32 ATHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTrpgpdrIMVFQEFD-QLppwkTVLENT-L 109
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL------IAISSGLNgQL----TGIENIeL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASrqATRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PRK13545 109 KGLMMG--LTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316062753 190 LALWEEVRfTLLFVTHSIEEALIVGSRVLLLspHPGRVR 228
Cdd:PRK13545 187 NEFKEQGK-TIFFISHSLSQVKSFCTKALWL--HYGQVK 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-189 |
5.82e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPV-DGEIRLDGQPVTRPgpdrimvfqefdQLPpW---KTVLENTLF 110
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVP------------QVS-WifnATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 111 plvasrqATRAEAEERARYfLNKVGLAKFADAYPH-----------TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PLN03232 702 -------GSDFESERYWRA-IDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170
....*....|....*
gi 2316062753 180 LTRRK-----MQEEL 189
Cdd:PLN03232 774 HVAHQvfdscMKDEL 788
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-192 |
6.88e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 37 SFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRI--MVFQEF-----DQLPPWKTVLENTL 109
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLqkLVSDEWqrnntDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 110 FPLVASRQATRAEAEERARYFlnkvGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQF----GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
...
gi 2316062753 190 LAL 192
Cdd:PRK10938 179 ASL 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
49-188 |
8.08e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 49 LGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRP---GPDRIMVFQEFdqlppwktvLENtlfplVASRQATRAEAEE 125
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPqyiKPDYDGTVEDL---------LRS-----ITDDLGSSYYKSE 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 126 raryFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALD-----ALTR--RKMQEE 188
Cdd:PRK13409 437 ----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlAVAKaiRRIAEE 502
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
48-179 |
9.83e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLL-----KSIGGFlspVDGEIRLDGQPVTRPGPDRIMVFQEFDQL-PPWKTVLENTLFPLVAsRQATRA 121
Cdd:PLN03140 911 LMGVSGAGKTTLMdvlagRKTGGY---IEGDIRISGFPKKQETFARISGYCEQNDIhSPQVTVRESLIYSAFL-RLPKEV 986
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062753 122 EAEERARYF---LNKVGLAKFADA---YPHT--LSGGMKQRVAIARALTMQPKVLLMDEPFAALDA 179
Cdd:PLN03140 987 SKEEKMMFVdevMELVELDNLKDAivgLPGVtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
146-220 |
1.95e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316062753 146 TLSGGMKQRVAIARALTMQPKVLLMDEPFAALDaLTRRKMQEELLALWEEvrfTLLFVTHSIEEALIVGSRVLLL 220
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-LHAVLWLETYLLKWPK---TFIVVSHAREFLNTVVTDILHL 414
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-205 |
2.59e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 35 DVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLD--------GQPVTRPGPDRIMVFQEFDQlppWKT--- 103
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenanigyyAQDHAYDFENDLTLFDWMSQ---WRQegd 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 104 ---VLENTLFPLVASRQATRAEAeeraryflnKVglakfadayphtLSGGMKQRVAIARALTMQPKVLLMDEPFAALDal 180
Cdd:PRK15064 414 deqAVRGTLGRLLFSQDDIKKSV---------KV------------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-- 470
|
170 180
....*....|....*....|....*...
gi 2316062753 181 trrkMQ--EEL-LALwEEVRFTLLFVTH 205
Cdd:PRK15064 471 ----MEsiESLnMAL-EKYEGTLIFVSH 493
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
53-205 |
3.06e-05 |
|
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: 45.17 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 53 GCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIM-----VFQE---FDQLPpwktvlentlfplvasrQATRAEAE 124
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRqlfsaVFSDfhlFDRLL-----------------GLDGEADP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 125 ERARYFLNKVGLA---KFADAYPHT--LSGGMKQRVAIARALTMQPKVLLMDEpFAA-LDALTRRKMQEELLALWEEVRF 198
Cdd:COG4615 431 ARARELLERLELDhkvSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDE-WAAdQDPEFRRVFYTELLPELKARGK 509
|
....*..
gi 2316062753 199 TLLFVTH 205
Cdd:COG4615 510 TVIAISH 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
41-189 |
3.33e-05 |
|
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: 43.47 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 41 FPAER-FVLLGPSGCGKSSLLKSIGgflsPVDGEIRLDGQPVTRPGPDRIMVfqefDQLppwKTVLENTLFPLVASRQAT 119
Cdd:cd03238 18 IPLNVlVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFSRNKLIFI----DQL---QFLIDVGLGYLTLGQKLS 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316062753 120 raeaeeraryflnkvglakfadayphTLSGGMKQRVAIARAL--TMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:cd03238 87 --------------------------TLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVI 132
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-181 |
4.26e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 40 VFPAERFVLLGPSGCGKSSLLKSI-----GGFLSpvDGEIRLDGQPVTRPGPDRIMVFQEFDQLPPWKTVLENTLFP--L 112
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLaervtTGVIT--GGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSayL 863
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316062753 113 VASRQATRAEAEERARYFLNKVGLAKFADAYPHTLSGGM----KQRVAIARALTMQPKVLL-MDEPFAALDALT 181
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-227 |
1.08e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 1 MTHHSPDTVTQPllqvDSVGLEYRTRRSLVRAT-HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQ 79
Cdd:PRK10982 235 LTQRFPDKENKP----GEVILEVRNLTSLRQPSiRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 80 PVTRPGPDRIMvfqefdqlppwktvleNTLFPLVAS-RQATRAEAE---------ERARYFLNKVGLAKFADAYPHT--- 146
Cdd:PRK10982 311 KINNHNANEAI----------------NHGFALVTEeRRSTGIYAYldigfnsliSNIRNYKNKVGLLDNSRMKSDTqwv 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 147 -----------------LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEE 209
Cdd:PRK10982 375 idsmrvktpghrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPE 453
|
250
....*....|....*...
gi 2316062753 210 ALIVGSRVLLLSphPGRV 227
Cdd:PRK10982 454 LLGITDRILVMS--NGLV 469
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-205 |
1.21e-04 |
|
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: 42.74 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 48 LLGPSGCGKSSLLKSIGGFLSP------------------------------VDGEIRldgqPVTRPgpdrimvfQEFDQ 97
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPnlgkfddppdwdeildefrgselqnyftklLEGDVK----VIVKP--------QYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 98 LPpwKTVLENTLFPLvasrqaTRAEAEERARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAAL 177
Cdd:cd03236 99 IP--KAVKGKVGELL------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*...
gi 2316062753 178 DALTRRKMQEELLALWEEVRFTLLfVTH 205
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLV-VEH 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-190 |
1.27e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 34 HDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQPVTRPGPDRIMVfqefdqlppwKTVLENTLF--P 111
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMN----------ATVRGNILFfdE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 112 LVASR--QATRAEAEErARYFLNKVGLAKFADAYPHTLSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEEL 189
Cdd:PTZ00243 747 EDAARlaDAVRVSQLE-ADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC 825
|
.
gi 2316062753 190 L 190
Cdd:PTZ00243 826 F 826
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-231 |
2.07e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 1 MTHHSPDTVTQPLLQVDSVgleyrTRRSLVRAtHDVSFDVFPAERFVLLGPSGCGKSSLLKSIGGFLSPVDGEIRLDGQP 80
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNV-----TSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 81 VTRPGPdrimvfqeFDQLPPWKTVL-----ENTLFPLVASRQATR-AEAEERARY-----FLNKVGLAKFADAYP----- 144
Cdd:PRK09700 327 ISPRSP--------LDAVKKGMAYItesrrDNGFFPNFSIAQNMAiSRSLKDGGYkgamgLFHEVDEQRTAENQRellal 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 145 --HT-------LSGGMKQRVAIARALTMQPKVLLMDEPFAALDALTRRKMQEELLALWEEVRfTLLFVTHSIEEALIVGS 215
Cdd:PRK09700 399 kcHSvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCD 477
|
250
....*....|....*.
gi 2316062753 216 RVLLLSphPGRVRAEI 231
Cdd:PRK09700 478 RIAVFC--EGRLTQIL 491
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
36-205 |
2.15e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 36 VSFDVFPAERFVLLGPSGCGKSSLLKSIGGF--LSPVDGEIRLDGQ------PVTRPGPDRIMVFQEFDQLPPwktvLEN 107
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllelsPEDRAGEGIFMAFQYPVEIPG----VSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 108 TLF---PLVASRQATRAEAEER---ARYFLNKVGLAKF-ADAYPHTL----SGGMKQRVAIARALTMQPKVLLMDEPFAA 176
Cdd:PRK09580 96 QFFlqtALNAVRSYRGQEPLDRfdfQDLMEEKIALLKMpEDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180
....*....|....*....|....*....
gi 2316062753 177 LDALTRRKMQEELLALWEEVRfTLLFVTH 205
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
41-207 |
2.28e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 41 FPAERFVLLGPSGCGKSSLLKSIG-GFLSPVDGEIRLDGQPVTRPGPD--------------RIMVFQ-EFDQL----PP 100
Cdd:COG0419 21 FDDGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEasvelefehggkryRIERRQgEFAEFleakPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 101 WKTVLENTLFPLVASRQATR--AEAEERARYFLNKVG---------LAKFADAYP-HTLSGGMKQRVAIARALTmqpkvL 168
Cdd:COG0419 101 ERKEALKRLLGLEIYEELKErlKELEEALESALEELAelqklkqeiLAQLSGLDPiETLSGGERLRLALADLLS-----L 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316062753 169 LMDepFAALDALTRRKMQEELLAlweevrftLLFVTHSI 207
Cdd:COG0419 176 ILD--FGSLDEERLERLLDALEE--------LAIITHVI 204
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
41-205 |
5.70e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 41 FPAERFVLL-GPSGCGKSSLLKSIGgflspvdgeirldgqpvtrpgpdrIMVFQEFdqlppwktvlENTLFPLVASRQAT 119
Cdd:cd03227 18 FGEGSLTIItGPNGSGKSTILDAIG------------------------LALGGAQ----------SATRRRSGVKAGCI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 120 RAEAEERARYFLnkvglakfadaypHTLSGGMKQRVAIARAL---TMQPKVL-LMDEPFAALDALTRRK---MQEELLAL 192
Cdd:cd03227 64 VAAVSAELIFTR-------------LQLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQAlaeAILEHLVK 130
|
170
....*....|...
gi 2316062753 193 weevRFTLLFVTH 205
Cdd:cd03227 131 ----GAQVIVITH 139
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-81 |
3.61e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062753 2 THHSPDTVTQPLLQVDSVGLEYRTRRSLVraTHDVSFDVFPAERFVLLGPSGCGKSSLLKSiggFLSPVD---GEIRLDG 78
Cdd:PTZ00243 1297 TSAAPHPVQAGSLVFEGVQMRYREGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLT---FMRMVEvcgGEIRVNG 1371
|
...
gi 2316062753 79 QPV 81
Cdd:PTZ00243 1372 REI 1374
|
|
| |
