|
Name |
Accession |
Description |
Interval |
E-value |
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-265 |
2.46e-168 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 464.98 E-value: 2.46e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIAR 99
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEIAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:COG4674 85 LGIGRKFQKPTVFEELTVFENLELALKGDRGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVI 259
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPRVI 244
|
....*.
gi 490250284 260 EVYLGR 265
Cdd:COG4674 245 EVYLGR 250
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
23-265 |
1.02e-148 |
|
urea ABC transporter, ATP-binding protein UrtD; 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: 274568 [Multi-domain] Cd Length: 242 Bit Score: 415.03 E-value: 1.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQGI 102
Cdd:TIGR03411 1 PILYLEGLSVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTMMDVITGKTRPDEGSVLFGGT-DLTGLPEHQIARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:TIGR03411 80 GRKFQKPTVFENLTVFENLELALPRDKSVFASLFFRLSAEEKDRIEEVLETIGLADEADRLAGLLSHGQKQWLEIGMLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVIEVY 262
Cdd:TIGR03411 160 QDPKLLLLDEPVAGMTDEETEKTAELLKSLAGKHSVVVVEHDMEFVRSIADKVTVLHQGSVLAEGSLDQVQADPRVIEVY 239
|
...
gi 490250284 263 LGR 265
Cdd:TIGR03411 240 LGR 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-258 |
2.42e-99 |
|
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: 289.72 E-value: 2.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQGIGR 104
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQD--DRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQV 258
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-264 |
1.91e-96 |
|
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: 283.47 E-value: 1.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQ 100
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALAM--KGDKSVWASL-----RARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQ 173
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLVAAhaRLGRGLLAALlrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLRE 251
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
250
....*....|...
gi 490250284 252 VQANEQVIEVYLG 264
Cdd:COG0411 240 VRADPRVIEAYLG 252
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-264 |
2.59e-53 |
|
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: 172.47 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQG 101
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 I-----GRKfqkptVFEALTVAENLALAMKgdksvwaslRARISSEQDDRLNEVLRLL-RLdGERYRQ-AGLLSHGQKQF 174
Cdd:COG0410 80 IgyvpeGRR-----IFPSLTVEENLLLGAY---------ARRDRAEVRADLERVYELFpRL-KERRRQrAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAG----MTDaeteytaELFRTL----AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGlaplIVE-------EIFEIIrrlnREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
250
....*....|....*...
gi 490250284 247 GSLREVQANEQVIEVYLG 264
Cdd:COG0410 218 GTAAELLADPEVREAYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
25-254 |
7.56e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.70 E-value: 7.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTlDPVAIARQgIGR 104
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-GEDVAR-DPAEVRRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:COG1131 78 VPQEPALYPDLTVRENLRF--------FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 185 PHLLLLDEPAAGMtDAET-EYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQA 254
Cdd:COG1131 150 PELLILDEPTSGL-DPEArRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-255 |
1.64e-48 |
|
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: 159.91 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQGIGR 104
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-GRDITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAmkgdksvwasLRARISSEQDDRLNEVLRLL-RLDGERYRQAGLLSHGQKQFLEIGMLLVQ 183
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLG----------AYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 184 EPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQAN 255
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-264 |
1.94e-47 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 158.23 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQ 100
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-HIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALAM--KGDKSVWASLRA-----RISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQ 173
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQhqQLKTGLFSGLLKtpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLRE 251
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|...
gi 490250284 252 VQANEQVIEVYLG 264
Cdd:PRK11300 241 IRNNPDVIKAYLG 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-262 |
2.10e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdlttldPVAIARQ 100
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-------PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGrkF--QKPTVFEA--LTVAENLALAMKGDKSVWaslrARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLE 176
Cdd:COG1121 76 RIG--YvpQRAEVDWDfpITVRDVVLMGRYGRRGLF----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 177 IGMLLVQEPHLLLLDEPAAGMtDAETEYT-AELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGqVLAEGSLREVQA 254
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGV-DAATEEAlYELLRELRREgKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
....*...
gi 490250284 255 NEQVIEVY 262
Cdd:COG1121 228 PENLSRAY 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-264 |
6.12e-41 |
|
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: 140.76 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQGIGR 104
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-QDITKLPMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLE--------IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 185 PHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVIEVYL 263
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGiGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
.
gi 490250284 264 G 264
Cdd:cd03218 232 G 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
25-247 |
6.93e-41 |
|
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: 139.96 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPvaiARQGIGR 104
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-GRDVTGVPP---ERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLK--------LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 185 PHLLLLDEPAAGMtDAET-----EYTAELFRTLagQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03259 149 PSLLLLDEPLSAL-DAKLreelrEELKELQREL--GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
25-260 |
7.00e-41 |
|
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: 140.55 E-value: 7.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgIG 103
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDITKKNLRELRRK-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPT--VFEAlTVAENLALAMKgdksvwaslRARISSEQ-DDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:COG1122 79 LVFQNPDdqLFAP-TVEEDVAFGPE---------NLGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 181 LVQEPHLLLLDEPAAGMtDAETeyTAELFRTLAG----QHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:COG1122 149 LAMEPEVLVLDEPTAGL-DPRG--RRELLELLKRlnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
....
gi 490250284 257 QVIE 260
Cdd:COG1122 226 ELLE 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
24-256 |
7.85e-41 |
|
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: 140.76 E-value: 7.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVaiARQGIG 103
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEDVRKEPRE--ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAmkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQ 183
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF--------AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 184 EPHLLLLDEPAAGMtDAE-TEYTAELFRTLAGQHSLMVVE-HDMGFVETIADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:COG4555 150 DPKVLLLDEPTNGL-DVMaRRLLREILRALKKEGKTVLFSsHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-256 |
1.86e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 145.94 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTtlDPVAIAR 99
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPVRIR--SPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEALTVAENLALAMKGDKSV---WASLRARIsSEQDDRLNevlrlLRLDGERYrqAGLLSHGQKQFLE 176
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARI-RELSERYG-----LDVDPDAK--VEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 177 IGMLLVQEPHLLLLDEPAAGMTDAETEytaELFRTL----AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEAD---ELFEILrrlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
....
gi 490250284 253 QANE 256
Cdd:COG3845 229 SEEE 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-262 |
6.02e-39 |
|
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: 136.33 E-value: 6.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQgIG 103
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASLSRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAMKGDKSVWASLrarisSEQDDRL-NEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYPHLGLFGRP-----SAEDREAvEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPaagmtdaeteyTA-----------ELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:COG1120 154 QEPPLLLLDEP-----------TShldlahqlevlELLRRLARERGRTVvmVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
250
....*....|...
gi 490250284 250 REVQANEQVIEVY 262
Cdd:COG1120 223 EEVLTPELLEEVY 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-264 |
2.86e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.00 E-value: 2.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQGI 102
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-EDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLE--------LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPAAG---MTDAETEytaELFRTLAgqhslmvvEHDMGFV-------ET--IADRVTVLHQGQVLAEGSLR 250
Cdd:COG1137 153 TNPKFILLDEPFAGvdpIAVADIQ---KIIRHLK--------ERGIGVLitdhnvrETlgICDRAYIISEGKVLAEGTPE 221
|
250
....*....|....
gi 490250284 251 EVQANEQVIEVYLG 264
Cdd:COG1137 222 EILNNPLVRKVYLG 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-258 |
2.35e-37 |
|
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: 131.47 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVA--IARQGI 102
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG-EDISGLSEAElyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLA--LAMKGDKSvwaslrariSSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAfpLREHTRLS---------EEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 181 LVQEPHLLLLDEPAAGMTDAETEYTAELFRTL--AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQA--NE 256
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDP 230
|
..
gi 490250284 257 QV 258
Cdd:cd03261 231 LV 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
24-264 |
2.99e-37 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 131.24 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQGIG 103
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQ-DITHLPMHERARLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENL--ALAMKGDKSvwaslRARISSEQDDRLNEvLRLLRLdgeRYRQAGLLSHGQKQFLEIGMLL 181
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENImaVLEIRKDLD-----RAEREERLEALLEE-FQISHL---RDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPAAGMTDAETEYTAELFRTLAgQHSLMVVEHDMGFVET--IADRVTVLHQGQVLAEGSLREVQANEQVI 259
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKHLK-ERGIGVLITDHNVRETldICDRAYIISDGKVLAEGTPAEIVANEKVR 229
|
....*
gi 490250284 260 EVYLG 264
Cdd:TIGR04406 230 RVYLG 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
26-242 |
7.17e-37 |
|
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: 129.51 E-value: 7.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFR--ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgIG 103
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELRRK-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKP-TVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:cd03225 79 LVFQNPdDQFFGPTVEEEVAFGLE--------NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQ 242
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
33-251 |
2.65e-36 |
|
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: 128.39 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 33 SFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDpvaIARQGIGRKFQKPTVF 112
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK---AARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EALTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDE 192
Cdd:cd03263 88 DELTVREHLRF--------YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 193 PAAGMtDAETEYtaELFRTLA---GQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLRE 251
Cdd:cd03263 160 PTSGL-DPASRR--AIWDLILevrKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-247 |
3.30e-36 |
|
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: 127.69 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGeLRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVdltTLDPVAIaRQGIG 103
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgQDV---LKQPQKL-RRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAmkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQ 183
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYI--------AWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 184 EPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-265 |
4.02e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTldPVAIAR 99
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPVRFRS--PRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEALTVAENLALA---MKGDKSVWASLRARISseqddrlnEVLRLLRLDGERYRQAGLLSHGQKQFLE 176
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMRRRAR--------ELLARLGLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 177 IGMLLVQEPHLLLLDEPAAGMTDAETEytaELF---RTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVE---RLFriiRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
250
....*....|...
gi 490250284 253 QAnEQVIEVYLGR 265
Cdd:COG1129 228 TE-DELVRLMVGR 239
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-257 |
5.53e-36 |
|
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: 128.08 E-value: 5.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAI-- 97
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLLSGKELrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 ARQGIGRKFQKPTVFEALTVAENLALAMKgdksVWASLRArissEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLE----IAGVPKA----EIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSLREVQAN 255
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVliTHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 490250284 256 EQ 257
Cdd:cd03258 232 PQ 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
25-262 |
9.62e-36 |
|
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: 127.68 E-value: 9.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAI--ARQG 101
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLKGKALrqLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRKFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLL 181
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVE--HDMGFVETIADRVTVLHQGQVLAEGSLREVQAnEQVI 259
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAREYADRIVGLKDGRIVFDGPPAELTD-EVLD 238
|
...
gi 490250284 260 EVY 262
Cdd:cd03256 239 EIY 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-253 |
1.66e-35 |
|
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: 126.33 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKAL---YDQSVDLTTLdpvaiaRQG 101
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvagHDVVREPREV------RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRKFQKPTVFEALTVAENLAlamkgdksVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLL 181
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLY--------IHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 182 VQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILltTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
25-243 |
1.78e-35 |
|
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: 124.82 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTlDPVAIaRQGIGR 104
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-GKDIKK-EPEEV-KRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLalamkgdksvwaslrarisseqddrlnevlrllrldgeryrqagLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03230 78 LPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 185 PHLLLLDEPAAGMtDAETEYTA-ELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:cd03230 114 PELLILDEPTSGL-DPESRREFwELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-257 |
9.91e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.41 E-value: 9.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 7 LFTRQLPGDRFREQTDPVLQLENINVSF-----DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA 81
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 82 LYDqSVDLTTLDPVAIA--RQGIGRKFQKPT--VFEALTVAENLALAMKgdksvwaSLRARISSEQDDRLNEVLRLLRLD 157
Cdd:COG1123 323 LFD-GKDLTKLSRRSLRelRRRVQMVFQDPYssLNPRMTVGDIIAEPLR-------LHGLLSRAERRERVAELLERVGLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 158 GE-RYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEYT-AELFRTLAGQH--SLMVVEHDMGFVETIAD 233
Cdd:COG1123 395 PDlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL-DVSVQAQiLNLLRDLQRELglTYLFISHDLAVVRYIAD 473
|
250 260
....*....|....*....|....
gi 490250284 234 RVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:COG1123 474 RVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
20-256 |
1.01e-34 |
|
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: 124.71 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIA- 98
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG-QDITGLSEKELYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 -RQGIGRKFQKPTVFEALTVAENLALAMK--GDKSvwaslrariSSEQDDRLNEVLRLLRLDGERYRQAGLLShGqkqfl 175
Cdd:COG1127 80 lRRRIGMLFQGGALFDSLTVFENVAFPLRehTDLS---------EAEIRELVLEKLELVGLPGAADKMPSELS-G----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 eiGML--------LVQEPHLLLLDEPAAGMtDAET-EYTAELFRTLagQHSL----MVVEHDMGFVETIADRVTVLHQGQ 242
Cdd:COG1127 145 --GMRkrvalaraLALDPEILLYDEPTAGL-DPITsAVIDELIREL--RDELgltsVVVTHDLDSAFAIADRVAVLADGK 219
|
250
....*....|....
gi 490250284 243 VLAEGSLREVQANE 256
Cdd:COG1127 220 IIAEGTPEELLASD 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
25-252 |
1.45e-34 |
|
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: 124.22 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITG-----KTRPQSGKALYD-QSVDLTTLDPVAIA 98
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDgKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQgIGRKFQKPTVFEAlTVAENLALAMKgdksvwasLRARISSEQ-DDRLNEVLRLLRLDGERYRQAGL--LSHGQKQFL 175
Cdd:cd03260 81 RR-VGMVFQKPNPFPG-SIYDNVAYGLR--------LHGIKLKEElDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
25-247 |
1.63e-34 |
|
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: 123.48 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVaiarQGIGR 104
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLalamkgdksvwaSLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03268 77 LIEAPGFYPNLTARENL------------RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 185 PHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-243 |
1.84e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.81 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSF-----DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIAR 99
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-GKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QgIGRKFQKPTV--FEALTVAENLALAMKGDKSvwASLRARISSEQDDRLNEVLRLLRLDGErYR---QAGLLSHGQKQF 174
Cdd:COG1101 81 Y-IGRVFQDPMMgtAPSMTIEENLALAYRRGKR--RGLRRGLTKKRRELFRELLATLGLGLE-NRldtKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSL--MVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLttLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-238 |
5.15e-34 |
|
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: 122.26 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdlttldPVAIARQGIGRK 105
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-------PLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 106 FQKPTV---FeALTVAENLALAMKGDKSVWaslrARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:cd03235 74 PQRRSIdrdF-PISVRDVVLMGLYGHKGLF----RRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPAAGMtDAETEytAELFRTLAGQHS----LMVVEHDMGFVETIADRVTVL 238
Cdd:cd03235 149 QDPDLLLLDEPFAGV-DPKTQ--EDIYELLRELRRegmtILVVTHDLGLVLEYFDRVLLL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-257 |
2.99e-33 |
|
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: 126.17 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDG--FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ---SGKALYDqSVDLTTLDPVA 96
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLD-GRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 97 IARQgIGRKFQKP-TVFEALTVAENLALAMKGDKSVWASLRARISseqddrlnEVLRLLRLDGERYRQAGLLSHGQKQFL 175
Cdd:COG1123 81 RGRR-IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVL--------ELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
....
gi 490250284 254 ANEQ 257
Cdd:COG1123 232 AAPQ 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
25-252 |
3.77e-33 |
|
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: 120.42 E-value: 3.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPvaiARQGIGR 104
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDITNLPP---HKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLR--------LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 185 PHLLLLDEPAAGMtDAE--TEYTAELFRTlagQHSL----MVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:cd03300 149 PKVLLLDEPLGAL-DLKlrKDMQLELKRL---QKELgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
25-252 |
5.56e-33 |
|
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: 120.14 E-value: 5.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYdQSVDLTTLDPvaiARQGIGR 104
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF-GGEDATDVPV---QERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKGDKSVWASLRARIsseqDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEI----RAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 185 PHLLLLDEPAAGMtDAETEytAELFRTLAGQH-----SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:cd03296 155 PKVLLLDEPFGAL-DAKVR--KELRRWLRRLHdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
40-195 |
1.72e-32 |
|
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: 116.21 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDltTLDPVAIARQGIGRKFQKPTVFEALTVAE 119
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--TDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 120 NLALAmkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYR----QAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAA 195
Cdd:pfam00005 79 NLRLG--------LLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-256 |
6.77e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 122.94 E-value: 6.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIAR 99
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-VDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QG--IGrkfQKPTVFEAlTVAENLALAmkgdksvwaslRARISseqDDRLNEVLRLLRLD--------------GERyrq 163
Cdd:COG4988 412 QIawVP---QNPYLFAG-TIRENLRLG-----------RPDAS---DEELEAALEAAGLDefvaalpdgldtplGEG--- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 164 AGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEytAELFRT---LAGQHSLMVVEHDMGFVEtIADRVTVLHQ 240
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHL-DAETE--AEILQAlrrLAKGRTVILITHRLALLA-QADRILVLDD 546
|
250
....*....|....*.
gi 490250284 241 GQVLAEGSLREVQANE 256
Cdd:COG4988 547 GRIVEQGTHEELLAKN 562
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-243 |
7.20e-32 |
|
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: 116.59 E-value: 7.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYDQSVDLTTLDPvaiARQGIGR 104
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR-IYIGGRDVTDLPP---KDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLK--------LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 185 PHLLLLDEPAAGMtDAETEYT--AELFRTLAGQHSLMV-VEHDMGFVETIADRVTVLHQGQV 243
Cdd:cd03301 149 PKVFLMDEPLSNL-DAKLRVQmrAELKRLQQRLGTTTIyVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-265 |
1.20e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.82 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQ 100
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALAMKGDKSV-------WASLRARiSSEQDDRLNevlrlLRLDGEryRQAGLLSHGQKQ 173
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniidWREMRVR-AAMMLLRVG-----LKVDLD--EKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV-VEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
250
....*....|...
gi 490250284 253 qANEQVIEVYLGR 265
Cdd:PRK09700 233 -SNDDIVRLMVGR 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-247 |
1.53e-31 |
|
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: 116.15 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFR--ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQGI 102
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD-GTDIRQLDPADL-RRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEAlTVAENLALAMkgdksvwaslrariSSEQDDRLNEVLRLLRLD--------------GERYRQaglLS 168
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNITLGA--------------PLADDERILRAAELAGVTdfvnkhpngldlqiGERGRG---LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 169 HGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVeTIADRVTVLHQGQVLAEG 247
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-215 |
5.63e-31 |
|
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: 114.11 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdlttldPVAIARQGI 102
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE-------PIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRK----FQKPTVFEALTVAENLALamkgdksvWASLRARISSeqDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIG 178
Cdd:COG4133 74 RRRlaylGHADGLKPELTVRENLRF--------WAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 490250284 179 MLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ 215
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
25-242 |
5.84e-31 |
|
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: 113.05 E-value: 5.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTL-DPVAIARQGIG 103
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLeDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAmkgdksvwaslrarisseqddrlnevlrllrldgeryrqaglLSHGQKQFLEIGMLLVQ 183
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 184 EPHLLLLDEPAAGMtDAETEYTA-ELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQ 242
Cdd:cd03229 118 DPDVLLLDEPTSAL-DPITRREVrALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
31-256 |
6.13e-31 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 121.09 E-value: 6.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSF----DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQgIGRKF 106
Cdd:COG2274 478 NVSFrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG-IDLRQIDPASLRRQ-IGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 107 QKPTVFEAlTVAENLALAmkgdksvwaslRARISseqDDRLNEVLRLLRLD--------------GERYRQaglLSHGQK 172
Cdd:COG2274 556 QDVFLFSG-TIRENITLG-----------DPDAT---DEEIIEAARLAGLHdfiealpmgydtvvGEGGSN---LSGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 173 QFLEIGMLLVQEPHLLLLDEPAAGMtDAETEYT-AELFRTLAGQHSLMVVEHDMgfvETI--ADRVTVLHQGQVLAEGSL 249
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSAL-DAETEAIiLENLRRLLKGRTVIIIAHRL---STIrlADRIIVLDKGRIVEDGTH 693
|
....*..
gi 490250284 250 REVQANE 256
Cdd:COG2274 694 EELLARK 700
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
22-246 |
1.21e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFD----GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAI 97
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 A---RQGIGRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQF 174
Cdd:COG1136 81 ArlrRRHIGFVFQFFNLLPELTALENVALPLL--------LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 175 LEIGMLLVQEPHLLLLDEPaagmT---DAETEYT-AELFRTLAGQH--SLMVVEHDMgFVETIADRVTVLHQGQVLAE 246
Cdd:COG1136 153 VAIARALVNRPKLILADEP----TgnlDSKTGEEvLELLRELNRELgtTIVMVTHDP-ELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
26-247 |
3.77e-30 |
|
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: 110.99 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQgigrk 105
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-KDLASLSPKELARK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 106 fqkptvfealtvaenLALamkgdksvwaslrarisseqddrLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEP 185
Cdd:cd03214 75 ---------------IAY-----------------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 186 HLLLLDEPAAGMtDAETEY-TAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03214 117 PILLLDEPTSHL-DIAHQIeLLELLRRLARERGKTVvmVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-243 |
5.96e-30 |
|
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: 111.47 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVAIARQGIGR 104
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMkgdksVWASLRARisSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAP-----IKVKGMSK--AEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 185 PHLLLLDEPAAGMtDAET-EYTAELFRTLAGQHSLMV-VEHDMGFVETIADRVTVLHQGQV 243
Cdd:cd03262 154 PKVMLFDEPTSAL-DPELvGEVLDVMKDLAEEGMTMVvVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
25-252 |
7.32e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 7.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPvaiARQGIGR 104
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG-RDVTDLPP---KDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwaslRARIS-SEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQ 183
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLK---------LRKVPkAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 184 EPHLLLLDEP-----AAGMTDAETEyTAELFRTLAgqhSLMV-VEHDMgfVE--TIADRVTVLHQGQVLAEGSLREV 252
Cdd:COG3839 151 EPKVFLLDEPlsnldAKLRVEMRAE-IKRLHRRLG---TTTIyVTHDQ--VEamTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
25-252 |
1.13e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.02 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAI--A 98
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG-VDLTALSERELraA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKPTVFEALTVAENLALAMKgdksvwaslRARIS-SEQDDRLNEVLRLLRLDG--ERY-RQaglLSHGQKQF 174
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLE---------IAGVPkAEIRKRVAELLELVGLSDkaDAYpSQ---LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMtDAETeyTA---ELFRTLAGQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSAL-DPET--TRsilDLLKDINRELGLTIVliTHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
...
gi 490250284 250 REV 252
Cdd:COG1135 226 LDV 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
21-252 |
1.39e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.04 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPvaiARQ 100
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-RDVTGLPP---EKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLA--LAMKGDKSvwaslrarisSEQDDRLNEVLRLLRLDG--ERY-RQaglLSHGQKQFL 175
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAfgLRMRGVPK----------AEIRARVAELLELVGLEGlaDRYpHQ---LSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMtDAET-EYTAELFRTLagQHSL----MVVEHDMGfvE--TIADRVTVLHQGQVLAEGS 248
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSAL-DAKLrEEMREELRRL--QRELgitfIYVTHDQE--EalALADRIAVMNDGRIEQVGT 219
|
....
gi 490250284 249 LREV 252
Cdd:COG3842 220 PEEI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
25-243 |
3.15e-29 |
|
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: 109.89 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIA-- 98
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTDISKLSEKELAaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 -RQGIGRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLL--------LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMtDAET-EYTAELFRTLAGQ--HSLMVVEHDMGFVEtIADRVTVLHQGQV 243
Cdd:cd03255 152 ARALANDPKIILADEPTGNL-DSETgKEVMELLRELNKEagTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-252 |
3.19e-29 |
|
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: 110.50 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRaLTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPvaiARQGIGR 104
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-GKDITNLPP---EKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLK--------KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 185 PHLLLLDEPAAGMtDAET-EYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:cd03299 148 PKILLLDEPFSAL-DVRTkEKLREELKKIRKEFGVTVlhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
25-247 |
3.38e-29 |
|
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: 109.76 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFD----GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTlDPVAiARQ 100
Cdd:cd03266 2 ITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVK-EPAE-ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEY--------FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 181 LVQEPHLLLLDEPAAGMTDAETEYTAELFRTL-AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
25-246 |
4.84e-29 |
|
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: 109.48 E-value: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsvdlttlDPVAIARQ 100
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-------EPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLE--------LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 181 LVQEPHLLLLDEPAAGMtDAETEYT--AELFRTLAGQHSLMV-VEHDMGfvETI--ADRVTVLHQ--GQVLAE 246
Cdd:cd03293 146 LAVDPDVLLLDEPFSAL-DALTREQlqEELLDIWRETGKTVLlVTHDID--EAVflADRVVVLSArpGRIVAE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
25-258 |
8.73e-29 |
|
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: 109.31 E-value: 8.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQGIG 103
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-GEDIREQDPVEL-RRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAMKGDKsvWasLRARIsseqDDRLNEVLRLLRLDGERYRQ--AGLLSHGQKQFLEIGMLL 181
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLK--W--PKEKI----RERADELLALVGLDPAEFADryPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPaAGMTDAET-EYTAELFRTLAGQ--HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV---QAN 255
Cdd:cd03295 151 AADPPLLLMDEP-FGALDPITrDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPAN 229
|
...
gi 490250284 256 EQV 258
Cdd:cd03295 230 DFV 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-264 |
1.22e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.21 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQGIG 103
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE-DISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQ-DDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQ--------IRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVIEV 261
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGlGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
...
gi 490250284 262 YLG 264
Cdd:PRK10895 234 YLG 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-247 |
2.35e-28 |
|
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: 107.98 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDP--VAI 97
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-GKDLLKLSRrlRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 ARQGIGRKFQKPtvFEAL----TVAENLAlamkgdKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQ-AGLLSHGQK 172
Cdd:cd03257 80 RRKEIQMVFQDP--MSSLnprmTIGEQIA------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 173 QFLEIGMLLVQEPHLLLLDEPAAGMtDAETE-YTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSAL-DVSVQaQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-243 |
6.30e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIA--RQ 100
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-QDLSRLKRREIPylRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLR--------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 181 LVQEPHLLLLDEPAAGMtDAETeyTAELFRTLAGQHSL----MVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:COG2884 152 LVNRPELLLADEPTGNL-DPET--SWEIMELLEEINRRgttvLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-262 |
7.00e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.16 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQ-G 101
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLADWSPAELARRrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRkfQKPTVFEALTVAENLALAmkgdKSVWASLRArisseQDDRL-NEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:PRK13548 80 VLP--QHSSLSFPFTVEEVVAMG----RAPHGLSRA-----EDDALvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 181 LVQ------EPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVivVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
250
....*....|
gi 490250284 253 QANEQVIEVY 262
Cdd:PRK13548 229 LTPETLRRVY 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-242 |
7.12e-28 |
|
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: 104.63 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQGIGRK 105
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLPLEEL-RRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 106 FQkptvfealtvaenlalamkgdksvwaslrarisseqddrlnevlrllrldgeryrqaglLSHGQKQFLEIGMLLVQEP 185
Cdd:cd00267 79 PQ-----------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 186 HLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQ 242
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-252 |
1.07e-27 |
|
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: 106.71 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALTDLSLAIGVGElRCVI-GPNGAGKTTLMDVITGKTRPqsgkaLYDQSVDLttldpvaiarq 100
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HWAIlGPNGAGKSTLLSLITGDLPP-----TYGNDVRL----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 gIGRKFQKPTVFEALT----VAENLALAMKGDKSVW--------AS--LRARISSEQDDRLNEVLRLLRLDGERYRQAGL 166
Cdd:COG1119 64 -FGERRGGEDVWELRKriglVSPALQLRFPRDETVLdvvlsgffDSigLYREPTDEQRERARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 167 LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHS---LMVVEHdmgfVETIAD---RVTVLHQ 240
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptlVLVTHH----VEEIPPgitHVLLLKD 218
|
250
....*....|..
gi 490250284 241 GQVLAEGSLREV 252
Cdd:COG1119 219 GRVVAAGPKEEV 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-264 |
1.45e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.12 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQGI 102
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-DITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLALAmkgdkSVWASlrariSSEQDDRLNEVLRLL-RLDGERYRQAGLLSHGQKQFLEIGMLL 181
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG-----GFFAE-----RDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVIE 260
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
....
gi 490250284 261 VYLG 264
Cdd:PRK11614 233 AYLG 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-246 |
1.47e-27 |
|
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: 104.05 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQGIGR 104
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-EVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQkptvfealtvaenlalamkgdksvwaslrarisseqddrlnevlrllrldgeryrqaglLSHGQKQFLEIGMLLVQE 184
Cdd:cd03216 80 VYQ-----------------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 185 PHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
42-247 |
1.90e-27 |
|
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: 104.88 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 42 DLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPvaiARQGIGRKFQKPTVFEALTVAENL 121
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 122 ALAMkgdksvwaSLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAE 201
Cdd:cd03298 92 GLGL--------SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490250284 202 TEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-262 |
4.01e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIARQ-GIG 103
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG-RPLAAWSPWELARRrAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RkfQKPTVFEALTVAENLALAmkgdKSVWASLRARisseQDDRLNEVLRLLRLDG--ER-YRQaglLSHGQKQFLEIGML 180
Cdd:COG4559 81 P--QHSSLAFPFTVEEVVALG----RAPHGSSAAQ----DRQIVREALALVGLAHlaGRsYQT---LSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 181 LVQ-------EPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:COG4559 148 LAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGgGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
250
....*....|
gi 490250284 253 QANEQVIEVY 262
Cdd:COG4559 228 LTDELLERVY 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-265 |
8.74e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 108.17 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALY-DQSVDLTtlDPVAIAR 99
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlGKEVTFN--GPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEALTVAENLALAmKGDKSVWASLRARISSEQDDRLnevLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKMYAEADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV-VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQaNEQV 258
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVyISHRLKEIFEICDDVTVFRDGQFIAEREVADLT-EDSL 233
|
....*..
gi 490250284 259 IEVYLGR 265
Cdd:PRK10762 234 IEMMVGR 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-265 |
2.63e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.53 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRAltDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLD----PVAIArq 100
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-GQDLTALPpaerPVSML-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 gigrkFQKPTVFEALTVAENLALAMKgdksvwASLraRISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGML 180
Cdd:COG3840 77 -----FQENNLFPHLTVAQNIGLGLR------PGL--KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 181 LVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE-- 256
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVlmVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEpp 223
|
....*....
gi 490250284 257 QVIEVYLGR 265
Cdd:COG3840 224 PALAAYLGI 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-243 |
2.97e-26 |
|
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: 101.56 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD--QSVDLTTLDPVAIARQGI 102
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTvaenlalamkgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:cd03226 81 DYQLFTDSVREELL------------------LGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
25-247 |
3.19e-26 |
|
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: 101.59 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdlttldPVAIA-RQGIG 103
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-------PLDIAaRNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQ 183
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVY--------LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 184 EPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-252 |
2.81e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.61 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 13 PGDRFREQTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTL 92
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 93 DPVaiaRQGIGRKFQKPTVFEALTVAENLALAMKGDKSVwaslRARISseqdDRLNEVLRLLRLDGERYRQAGLLSHGQK 172
Cdd:PRK11607 87 PPY---QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLP----KAEIA----SRVNEMLGLVHMQEFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 173 QFLEIGMLLVQEPHLLLLDEPAAGMTDA-----ETEYTAELFRTlaGQHSLMVVeHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKlrdrmQLEVVDILERV--GVTCVMVT-HDQEEAMTMAGRIAIMNRGKFVQIG 232
|
....*
gi 490250284 248 SLREV 252
Cdd:PRK11607 233 EPEEI 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-254 |
3.83e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.95 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdltTLDPVAIARqgIG 103
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE----PLDPEDRRR--IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 -----RK-FQKPTVFEALtvaenLALamkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:COG4152 75 ylpeeRGlYPKMKVGEQL-----VYL---------ARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAG--------MTDAETEYTAE----LFRTlagqhslmvveHDMGFVETIADRVTVLHQGQVLA 245
Cdd:COG4152 141 IAALLHDPELLILDEPFSGldpvnvelLKDVIRELAAKgttvIFSS-----------HQMELVEELCDRIVIINKGRKVL 209
|
....*....
gi 490250284 246 EGSLREVQA 254
Cdd:COG4152 210 SGSVDEIRR 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-260 |
6.22e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 17 FREQTDPVLQLENINVSFdgfRALTDLslaigvgelrcvIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLDPV 95
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSL---SPVTGL------------VGANGCGKSTLFMNLSGLLRPQKGAVLWQgKPLDYSKRGLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIaRQGIGRKFQKPtvfealtvaENLALAMKGDKSVWASLRARISSEQD--DRLNEVLRLLrlDGERYRQAGL--LSHGQ 171
Cdd:PRK13638 74 AL-RQQVATVFQDP---------EQQIFYTDIDSDIAFSLRNLGVPEAEitRRVDEALTLV--DAQHFRHQPIqcLSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 172 KQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVV-EHDMGFVETIADRVTVLHQGQVLAEGSLR 250
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEISDAVYVLRQGQILTHGAPG 221
|
250
....*....|
gi 490250284 251 EVQANEQVIE 260
Cdd:PRK13638 222 EVFACTEAME 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-259 |
8.32e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.92 E-value: 8.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLDPVAIaR 99
Cdd:PRK13636 3 DYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgKPIDYSRKGLMKL-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKP-------TVFEALTV-AENLALAMKgdksvwaslrarissEQDDRLNEVLRLLRLDGERYRQAGLLSHGQ 171
Cdd:PRK13636 82 ESVGMVFQDPdnqlfsaSVYQDVSFgAVNLKLPED---------------EVRKRVDNALKRTGIEHLKDKPTHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 172 KQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIiaTHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
250
....*....|
gi 490250284 250 REVQANEQVI 259
Cdd:PRK13636 227 KEVFAEKEML 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-252 |
1.62e-24 |
|
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: 97.68 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFR-ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLdPVAIARQGIGR 104
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-GIDIRDI-SRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEAlTVAENLALamkgdksvwASLRARisseqDDRLNEVLRLLRLD--------------GERyrqAGLLSHG 170
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRL---------GRPNAT-----DEEVIEAAKEAGAHdfimklpngydtvlGEN---GGNLSQG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEYT--AELFRTLAGQHSLMVVEHdmgfVETI--ADRVTVLHQGQVLAE 246
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNI-DTETEKLiqEALEKLMKGRTSIIIAHR----LSTIknADKILVLDDGKIIEE 218
|
....*.
gi 490250284 247 GSLREV 252
Cdd:cd03254 219 GTHDEL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-243 |
1.69e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK---------ALYDQsvDLTTL 92
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTvklgetvkiGYFDQ--HQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 93 DPvaiarqgigrkfqkptvfeALTVAENLALAMKGDKSVwaSLRArisseqddrlneVLRLLRLDGER-YRQAGLLSHGQ 171
Cdd:COG0488 391 DP-------------------DKTVLDELRDGAPGGTEQ--EVRG------------YLGRFLFSGDDaFKPVGVLSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490250284 172 KQFLEIGMLLVQEPHLLLLDEPaagmT---DAET-EYTAELFRTLAGqhSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEP----TnhlDIETlEALEEALDDFPG--TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-233 |
3.78e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLM-------DVITGkTRPQS-----GKALYDQSV 87
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPG-FRVEGkvtfhGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 88 DlttldPVAIARQgIGRKFQKPTVFEAlTVAENLA-----LAMKG--DKSVWASLR-ARISSEQDDRLnevlrllrldge 159
Cdd:PRK14243 85 D-----PVEVRRR-IGMVFQKPNPFPK-SIYDNIAygariNGYKGdmDELVERSLRqAALWDEVKDKL------------ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 160 ryRQAGL-LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIAD 233
Cdd:PRK14243 146 --KQSGLsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-257 |
5.15e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDP--VAIAR 99
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQDLTALSEkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEALTVAENLALAMKGDKSVWASLRARIsseqddrlNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARV--------TELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEpAAGMTDAET-----EYTAELFRTLagqhSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK11153 154 ALASNPKVLLCDE-ATSALDPATtrsilELLKDINREL----GLTIVliTHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
....*
gi 490250284 253 QANEQ 257
Cdd:PRK11153 229 FSHPK 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-262 |
6.32e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgIGR 104
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG-DKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAmkgdKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYG----RSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 185 PHLLLLDEPAagmTDAETEYTAELFRTL-----AGQhSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVI 259
Cdd:PRK11231 157 TPVVLLDEPT---TYLDINHQVELMRLMrelntQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR 232
|
...
gi 490250284 260 EVY 262
Cdd:PRK11231 233 TVF 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-247 |
7.60e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 96.64 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLM-------DVITG-KTrpqSGKALYD-QSVDLT 90
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGaRV---EGEILLDgEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 91 TLDPVAIARQgIGRKFQKPTVFeALTVAENLALAMK--GDKS-------VWASLR-ARISSEQDDRLNEvlrllrldger 160
Cdd:COG1117 84 DVDVVELRRR-VGMVFQKPNPF-PKSIYDNVAYGLRlhGIKSkseldeiVEESLRkAALWDEVKDRLKK----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 161 yrQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQ 240
Cdd:COG1117 151 --SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYL 228
|
....*..
gi 490250284 241 GQVLAEG 247
Cdd:COG1117 229 GELVEFG 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-252 |
1.26e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVaiAR 99
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAE--NR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QgIGRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:PRK09452 87 H-VNTVFQSYALFPHMTVFENVAFGLR--------MQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 180 LLVQEPHLLLLDEPAAGM-----TDAETEYTAeLFRTLAgqHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALdyklrKQMQNELKA-LQRKLG--ITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
25-242 |
1.44e-23 |
|
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: 93.60 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGF--RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgI 102
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-GVDLRDLDLESLRKN-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEAlTVAENlalamkgdksvwaslrarisseqddrlnevlrllrldgeryrqagLLSHGQKQFLEIGMLLV 182
Cdd:cd03228 79 AYVPQDPFLFSG-TIREN---------------------------------------------ILSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 183 QEPHLLLLDEPAAGMtDAETEY-TAELFRTLAGQHSLMVVEHDMgfvETI--ADRVTVLHQGQ 242
Cdd:cd03228 113 RDPPILILDEATSAL-DPETEAlILEALRALAKGKTVIVIAHRL---STIrdADRIIVLDDGR 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
50-247 |
2.25e-23 |
|
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: 94.28 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 50 GELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD--------QSVDLTTldpvaiARQGIGRKFQKPTVFEALTVAENL 121
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrKKINLPP------QQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 122 ALAMKGDKSvwaslrarisSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDA- 200
Cdd:cd03297 97 AFGLKRKRN----------REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAl 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490250284 201 ETEYTAELFRTLA--GQHSLMvVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIF-VTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
36-243 |
2.61e-23 |
|
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: 94.01 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 36 GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIA--RQGIGRKFQKPTVFE 113
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-GQDVSDLRGRAIPylRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 114 ALTVAENLALAMkgdKSVWASLRarissEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEP 193
Cdd:cd03292 92 DRNVYENVAFAL---EVTGVPPR-----EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490250284 194 AAGMtdaETEYTAELFRTLAGQH----SLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:cd03292 164 TGNL---DPDTTWEIMNLLKKINkagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-260 |
2.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA-LYDQSVDLTTLDPVaiaR 99
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWV---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKP--TVFeALTVAENLALAmkgdkSVWASLRArisSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:PRK13647 79 SKVGLVFQDPddQVF-SSTVWDDVAFG-----PVNMGLDK---DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMTDAETEytaELFRTLAGQH----SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSlREVQ 253
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQE---TLMEILDRLHnqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLL 225
|
....*..
gi 490250284 254 ANEQVIE 260
Cdd:PRK13647 226 TDEDIVE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-260 |
4.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 38 RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA------LYDQSVDLTTLdpvaiaRQGIGRKFQKP-- 109
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvdITDKKVKLSDI------RKKVGLVFQYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 110 TVFEAlTVAENLALamkGDKSVWASlrariSSEQDDRLNEVLRLLRLDGERYRQAGL--LSHGQKQFLEIGMLLVQEPHL 187
Cdd:PRK13637 95 QLFEE-TIEKDIAF---GPINLGLS-----EEEIENRVKRAMNIVGLDYEDYKDKSPfeLSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 188 LLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVIE 260
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIilVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
38-247 |
5.87e-23 |
|
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: 93.94 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 38 RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkalydqSVDLTTLDP----VAIARQgIGRKF-QKPTVF 112
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG------EVRVAGLVPwkrrKKFLRR-IGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EALTVAENLALamkgdksvwasLRA--RISSEQ-DDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLL 189
Cdd:cd03267 108 WDLPVIDSFYL-----------LAAiyDLPPARfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 190 LDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-248 |
2.45e-22 |
|
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: 91.05 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITG--KTRPQSGKALYDqSVDLTTLDPVAIARQGI 102
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK-GEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLalamkgdksvwaslrarisseqddrlnevlrllrldgeRYRQAGlLSHGQKQFLEIGMLLV 182
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFL--------------------------------------RYVNEG-FSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETI-ADRVTVLHQGQVLAEGS 248
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEGkSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-247 |
2.51e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVDL-TTLDPVAIA--RQ 100
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlNIAGNHFDFsKTPSDKAIRelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLalamkgdksVWASLRARISSEQD--DRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIG 178
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNL---------IEAPCRVLGLSKDQalARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 179 MLLVQEPHLLLLDEPAAGMtdaETEYTAE---LFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAAL---DPEITAQivsIIRELAETGiTQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-238 |
2.77e-22 |
|
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: 95.43 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFR-ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPvAIARQ 100
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLADADA-DSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEAlTVAENLALAmKGDKSVWASLRARISSEQDDRLNEV-LRLLRLDGERYRQaglLSHGQKQFLEIGM 179
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLA-RPDASDAEIREALERAGLDEFVAALpQGLDTPIGEGGAG---LSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEPAAGMtDAETEYTA-ELFRTLAGQHSLMVVEHDMGFVEtIADRVTVL 238
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHL-DAETEAEVlEALRALAQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-256 |
3.11e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.50 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkALYDQSVDLTTLDPVAIARQGI 102
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG-TLEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLALAMKGdksvwaslRARISSEQDDRLNEVLRLLRLDGeryrQAGLLSHGQKQFLEIGMLLV 182
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPK--------RQASMQKMKQLLAALGCQLDLDS----SAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQgVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-265 |
7.55e-22 |
|
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: 94.12 E-value: 7.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGkTRPQ---SGKALYDQSvDLTTLDPVAIARQ 100
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGS-PLKASNIRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALA----MKGDKSVWASLRARIsseqddrlNEVLRLLRLDGER-YRQAGLLSHGQKQFL 175
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRA--------KNLLRELQLDADNvTRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAgQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSLREVq 253
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVyiSHKLNEVKAVCDTICVIRDGQHVATKDMSTM- 228
|
250
....*....|..
gi 490250284 254 ANEQVIEVYLGR 265
Cdd:TIGR02633 229 SEDDIITMMVGR 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-265 |
1.08e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGkTRPQ---------SGKALYDQSVDLTt 91
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyegeiifEGEELQASNIRDT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 92 ldpvaiARQGIGRKFQKPTVFEALTVAENLALA---MKGDKSVWASLRARISseqddrlnEVLRLLRLDGERYRQAGLLS 168
Cdd:PRK13549 80 ------ERAGIAIIHQELALVKELSVLENIFLGneiTPGGIMDYDAMYLRAQ--------KLLAQLKLDINPATPVGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 169 HGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAgQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIyiSHKLNEVKAISDTICVIRDGRHIGT 224
|
250
....*....|....*....
gi 490250284 247 GSLREVQANeQVIEVYLGR 265
Cdd:PRK13549 225 RPAAGMTED-DIITMMVGR 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-252 |
1.12e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYDQSVDLTTLDpvAIARQgIGR 104
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH-IRFHGTDVSRLH--ARDRK-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMK----GDKSVWASLRARISseqddRLNEVLRLLRLdGERYrqAGLLSHGQKQFLEIGML 180
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTvlprRERPNAAAIKAKVT-----QLLEMVQLAHL-ADRY--PAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 181 LVQEPHLLLLDEPaAGMTDAETEytAELFRTLAGQHSLM-----VVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK10851 151 LAVEPQILLLDEP-FGALDAQVR--KELRRWLRQLHEELkftsvFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
35-224 |
1.44e-21 |
|
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: 89.02 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 35 DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLDPVAiARQGIGRKFQKP--TV 111
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgEPLDYSRKGLLE-RRQRVGLVFQDPddQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 112 FEAlTVAENLA-----LAMKGDksvwaslrarissEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPH 186
Cdd:TIGR01166 82 FAA-DVDQDVAfgplnLGLSEA-------------EVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 490250284 187 LLLLDEPAAGMTDAETEYTAELFRTL-AGQHSLMVVEHD 224
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLrAEGMTVVISTHD 186
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-259 |
2.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 27 LENINVSFDG-----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKAL---YDQSVDLTTLDPVAIA 98
Cdd:PRK13645 9 LDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdYAIPANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKP--TVFEAlTVAENLALA---MKGDKSvwaslrarissEQDDRLNEVLRLLRLDGERYRQAGL-LSHGQK 172
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQE-TIEKDIAFGpvnLGENKQ-----------EAYKKVPELLKLVQLPEDYVKRSPFeLSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 173 QFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHS--LMVVEHDMGFVETIADRVTVLHQGQVLAEGSLR 250
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
....*....
gi 490250284 251 EVQANEQVI 259
Cdd:PRK13645 237 EIFSNQELL 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-243 |
2.75e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 27 LENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYdqsVDLTTLDPVAIARQGIGRKF 106
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-LF---IGEKRMNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 107 QKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPH 186
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLK--------LAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 187 LLLLDEP-----AAGMTDAETEyTAELFRTLagQHSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:PRK11000 154 VFLLDEPlsnldAALRVQMRIE-ISRLHKRL--GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
57-255 |
3.22e-21 |
|
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: 91.32 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 57 GPNGAGKTTLMDVITGKTRPQSG------KALYDQSVDLTtldpVAIARQGIGRKFQKPTVFEALTVAENLALAMKgdks 130
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGrirlggEVLQDSARGIF----LPPHRRRIGYVFQEARLFPHLSVRGNLLYGRK---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 131 vwaslRARISSEQDDrLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEytAEL-- 208
Cdd:COG4148 104 -----RAPRAERRIS-FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL-DLARK--AEIlp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490250284 209 -FRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQAN 255
Cdd:COG4148 175 yLERLRDELDIPIlyVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-255 |
3.45e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITG--KTRPQ---SGKALYDQSvDLTTLDpVAIA 98
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvSGEVYLDGQ-DIFKMD-VIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKPTVFEALTVAENLALAMKGDKSV-----------WASLRARISSEQDDRLNEvlrllrldgeryrQAGLL 167
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkskkelqervrWALEKAQLWDEVKDRLDA-------------PAGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 168 SHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
....*...
gi 490250284 248 SLREVQAN 255
Cdd:PRK14247 228 PTREVFTN 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-243 |
4.73e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 27 LENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDpvaiarqgigrkf 106
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 107 QKPTVFEALTVAENLalaMKGDKSVWASLR--ARISSEQDD-------------------------RLNEVLRLLRLDGE 159
Cdd:COG0488 68 QEPPLDDDLTVLDTV---LDGDAELRALEAelEELEAKLAEpdedlerlaelqeefealggweaeaRAEEILSGLGFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 160 -RYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPaagmT---DAET-EYTAELFRTLAGqhSLMVVEHDMGFVETIADR 234
Cdd:COG0488 145 dLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP----TnhlDLESiEWLEEFLKNYPG--TVLVVSHDRYFLDRVATR 218
|
....*....
gi 490250284 235 VTVLHQGQV 243
Cdd:COG0488 219 ILELDRGKL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-255 |
4.90e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDV------------ITGKTRpQSGKALYDQSVDlttl 92
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVR-LFGRNIYSPDVD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 93 dPVAIARQgIGRKFQKPTVFEALTVAENLALAMKGDKSV-----------WASLRARISSEQDDRLNEvlrllrldgery 161
Cdd:PRK14267 80 -PIEVRRE-VGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelderveWALKKAALWDEVKDRLND------------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 162 rQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQG 241
Cdd:PRK14267 146 -YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLG 224
|
250
....*....|....
gi 490250284 242 QVLAEGSLREVQAN 255
Cdd:PRK14267 225 KLIEVGPTRKVFEN 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-262 |
4.90e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.46 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVdLTTLDPVAIAR 99
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-LESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVfEALTVAENLALAmkgdKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:PRK10575 86 KVAYLPQQLPAA-EGMTVRELVAIG----RYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTViaVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
....*
gi 490250284 258 VIEVY 262
Cdd:PRK10575 241 LEQIY 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-260 |
5.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.37 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKAL-------YDQSVDLTtldpv 95
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikYDKKSLLE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 aiARQGIGRKFQKP--TVFeALTVAENLA---LAMKGDKsvwaslrarisSEQDDRLNEVLRLLRLDGERYRQAGLLSHG 170
Cdd:PRK13639 76 --VRKTVGIVFQNPddQLF-APTVEEDVAfgpLNLGLSK-----------EEVEKRVKEALKAVGMEGFENKPPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVE-HDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
250
....*....|.
gi 490250284 250 REVQANEQVIE 260
Cdd:PRK13639 222 KEVFSDIETIR 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-264 |
6.59e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 6.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKalydqsvdLTTLD-PVA----IAR 99
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK--------ITVLGvPVPararLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEALTVAENLALAMKgdksvWASLRARissEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGR-----YFGMSTR---EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEG---SLREVQAN 255
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGrphALIDEHIG 265
|
....*....
gi 490250284 256 EQVIEVYLG 264
Cdd:PRK13536 266 CQVIEIYGG 274
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
26-262 |
7.69e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQ-GIGR 104
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATTPSRELAKRlAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 kfQKPTVFEALTVAEnlaLAMKGDksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:COG4604 82 --QENHINSRLTVRE---LVAFGR---FPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 185 PHLLLLDEP--------AAGMTDAETEYTAELFRTlagqhsLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:COG4604 154 TDYVLLDEPlnnldmkhSVQMMKLLRRLADELGKT------VVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
....*.
gi 490250284 257 QVIEVY 262
Cdd:COG4604 228 VLSDIY 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-248 |
7.84e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSF-DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYdQSVDLTTLDPVAIARQGI 102
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV-SGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKP-TVFEALTVAENLALAMKGDKSVWASLRARIsseqDDRLNEVlrllRLDGERYRQAGLLSHGQKQFLEIGMLL 181
Cdd:PRK13644 80 GIVFQNPeTQFVGRTVEEDLAFGPENLCLPPIEIRKRV----DRALAEI----GLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 182 VQEPHLLLLDEpAAGMTDAETEYTaeLFRTLAGQH----SLMVVEHDMGFVEtIADRVTVLHQGQVLAEGS 248
Cdd:PRK13644 152 TMEPECLIFDE-VTSMLDPDSGIA--VLERIKKLHekgkTIVYITHNLEELH-DADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-264 |
3.19e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGF--RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkalyDQSVDLTTLDPVAI- 97
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG----TITVGGMVLSEETVw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 -ARQGIGRKFQKP-TVFEALTVAENLALAMKGdksvwaslRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFL 175
Cdd:PRK13635 78 dVRRQVGMVFQNPdNQFVGATVQDDVAFGLEN--------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEpAAGMTDAE-TEYTAELFRTLAGQHSLMVVE--HDMGFVETiADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13635 150 AIAGVLALQPDIIILDE-ATSMLDPRgRREVLETVRQLKEQKGITVLSitHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
250
....*....|...
gi 490250284 253 -QANEQVIEVYLG 264
Cdd:PRK13635 228 fKSGHMLQEIGLD 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-257 |
3.47e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVDLT-TLDP----VAIA 98
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTiRVGDITIDTArSLSQqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKPTVFEALTVAENL---ALAMKGDKSVWASLRARisseqddrlnEVLRLLRLDGERYRQAGLLSHGQKQFL 175
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIiegPVIVKGEPKEEATARAR----------ELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMtdaETEYTAELF---RTLAGQHSLMV-VEHDMGFVETIADRVTVLHQGQVLAEGSLRE 251
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSAL---DPELVGEVLntiRQLAQEKRTMViVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
....*.
gi 490250284 252 VQANEQ 257
Cdd:PRK11264 231 LFADPQ 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-248 |
4.06e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSF---DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLTTLDPVAIaRQGIGRKFQ 107
Cdd:COG1132 344 NVSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG-VDIRDLTLESL-RRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 108 KPTVFEAlTVAENLALAMKG--DKSVWASLR-ARIS---SEQDDRLNEVLrllrldGERyrqAGLLSHGQKQFLEIGMLL 181
Cdd:COG1132 422 DTFLFSG-TIRENIRYGRPDatDEEVEEAAKaAQAHefiEALPDGYDTVV------GER---GVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPAAGMtDAETEYT-AELFRTLAGQHSLMVVEHDmgfVETI--ADRVTVLHQGQVLAEGS 248
Cdd:COG1132 492 LKDPPILILDEATSAL-DTETEALiQEALERLMKGRTTIVIAHR---LSTIrnADRILVLDDGRIVEQGT 557
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-257 |
4.89e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.37 E-value: 4.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVIT--GKTRPQ---------SGKALYDQSVDL 89
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtitgsivyNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 90 TTLdpvaiaRQGIGRKFQKPTVFeALTVAENL--ALAMKG-------DKSVWASLR-ARISSEQDDRLNEvlrllrldge 159
Cdd:PRK14239 82 VDL------RKEIGMVFQQPNPF-PMSIYENVvyGLRLKGikdkqvlDEAVEKSLKgASIWDEVKDRLHD---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 160 ryrQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLH 239
Cdd:PRK14239 145 ---SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFL 221
|
250
....*....|....*...
gi 490250284 240 QGQVLAEGSLREVQANEQ 257
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPK 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-265 |
1.63e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLT-TLDpvAIA 98
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgQEMRFAsTTA--ALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 rQGIGRKFQKPTVFEALTVAENLALAMKGDKSVW---ASLRARiSSEQDDRLNEvlrllRLDGEryRQAGLLSHGQKQFL 175
Cdd:PRK11288 79 -AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIvnrRLLNYE-AREQLEHLGV-----DIDPD--TPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAE-GSLREVQ 253
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVD 229
|
250
....*....|..
gi 490250284 254 aNEQVIEVYLGR 265
Cdd:PRK11288 230 -RDQLVQAMVGR 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-252 |
2.45e-19 |
|
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: 86.78 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 15 DRFREQTDPVLQLENIN---VSFDG--FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA---LYDQS 86
Cdd:TIGR03269 270 ECEVEVGEPIIKVRNVSkryISVDRgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEW 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 87 VDLTTLDPVAIAR--QGIGRKFQKPTVFEALTVAENLALAMKGD-KSVWASLRARISSE----QDDRLNEVLrllrldgE 159
Cdd:TIGR03269 350 VDMTKPGPDGRGRakRYIGILHQEYDLYPHRTVLDNLTEAIGLElPDELARMKAVITLKmvgfDEEKAEEIL-------D 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 160 RYRQAglLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGM---TDAETEYTAELFRTLAGQhSLMVVEHDMGFVETIADRVT 236
Cdd:TIGR03269 423 KYPDE--LSEGERHRVALAQVLIKEPRIVILDEPTGTMdpiTKVDVTHSILKAREEMEQ-TFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*.
gi 490250284 237 VLHQGQVLAEGSLREV 252
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEI 515
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-263 |
2.56e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.52 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 38 RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKAlydqSVDltTLDPV----AIARQgIGRKF-QKPTVF 112
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV----RVL--GYVPFkrrkEFARR-IGVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EALTVAENLALamkgdksvwasLRA--RISSEQ-DDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLL 189
Cdd:COG4586 109 WDLPAIDSFRL-----------LKAiyRIPDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 190 LDEPAAGMtDAET---------EYTAElFRTlagqhSLMVVEHDMGFVETIADRVTVLHQGQVLAEGS---LREVQANEQ 257
Cdd:COG4586 178 LDEPTIGL-DVVSkeaireflkEYNRE-RGT-----TILLTSHDMDDIEALCDRVIVIDHGRIIYDGSleeLKERFGPYK 250
|
....*.
gi 490250284 258 VIEVYL 263
Cdd:COG4586 251 TIVLEL 256
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-256 |
2.96e-19 |
|
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: 83.69 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSF----DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgIGRKF 106
Cdd:cd03252 5 HVRFrykpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVD-GHDLALADPAWLRRQ-VGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 107 QKPTVFEAlTVAENLALAMKGdksvwASLRARISSEQDDRLNEVLRLLRLD-----GEryRQAGlLSHGQKQFLEIGMLL 181
Cdd:cd03252 83 QENVLFNR-SIRDNIALADPG-----MSMERVIEAAKLAGAHDFISELPEGydtivGE--QGAG-LSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 182 VQEPHLLLLDEpAAGMTDAETEYT--AELFRTLAGQhSLMVVEHDMGFVETiADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:cd03252 154 IHNPRILIFDE-ATSALDYESEHAimRNMHDICAGR-TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-262 |
4.65e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSfdgfRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTrPQSGKALYDQSvDLTTLDPVAIARQgigR 104
Cdd:PRK03695 1 MQLNDVAVS----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQ-PLEAWSAAELARH---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KF---QKPTVFeALTVAENLALAMkGDKSVwaslrariSSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQ-------F 174
Cdd:PRK03695 72 AYlsqQQTPPF-AMPVFQYLTLHQ-PDKTR--------TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQrvrlaavV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:PRK03695 142 LQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
....*....
gi 490250284 254 ANEQVIEVY 262
Cdd:PRK03695 222 TPENLAQVF 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-212 |
5.83e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.60 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKalydqsvdlTTLDPVAIARQGIGR 104
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS---------ITLDGKPVEGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 K--FQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:PRK11248 73 GvvFQNEGLLPWRNVQDNVAFGLQ--------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA 144
|
170 180 190
....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPaAGMTDAeteYTAELFRTL 212
Cdd:PRK11248 145 ANPQLLLLDEP-FGALDA---FTREQMQTL 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-247 |
6.71e-19 |
|
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: 81.83 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRA------LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ--SGKALYDQsvdlTTLDPV 95
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLING----RPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIARQgIGRKFQKPTVFEALTVAENLALAmkgdksvwASLRArisseqddrlnevlrllrldgeryrqaglLSHGQKQFL 175
Cdd:cd03213 79 SFRKI-IGYVPQDDILHPTLTVRETLMFA--------AKLRG-----------------------------LSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMtDAETEYT-AELFRTLA-GQHSLMVVEHD-MGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGL-DSSSALQvMSLLRRLAdTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-223 |
6.73e-19 |
|
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: 85.88 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 11 QLPGDRFREQTDPVLQLENINVSFDG-FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDL 89
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 90 TTLDPVAIARQgIGRKFQKPTVFEAlTVAENLALAMKG--DKSVWASLRARisseqddRLNEVLRLLR--LDGERYRQAG 165
Cdd:TIGR02868 400 SSLDQDEVRRR-VSVCAQDAHLFDT-TVRENLRLARPDatDEELWAALERV-------GLADWLRALPdgLDTVLGEGGA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 166 LLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAET--EYTAELFRTLAGQHSLMVVEH 223
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHL-DAETadELLEDLLAALSGRTVVLITHH 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-262 |
9.73e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 9.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLM----DVITGKTRPQSGKALYDQSVDLT--TLDPVAI 97
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTVQREgrLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 ARQGIGRKFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVE--HDMGFVETIADRVTVLHQGQVLAEGSLREVQaN 255
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVtlHQVDYALRYCERIVALRQGHVFYDGSSQQFD-N 242
|
....*..
gi 490250284 256 EQVIEVY 262
Cdd:PRK09984 243 ERFDHLY 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-261 |
1.03e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.12 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFR--ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVDLTTLDPvaiA 98
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEiKIDGITISKENLKE---I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKP-TVFEALTVAENLALAMKgDKSVwaslrarISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:PRK13632 82 RKKIGIIFQNPdNQFIGATVEDDIAFGLE-NKKV-------PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEpAAGMTDAETEYT-AELFRTLA--GQHSLMVVEHDMGFVeTIADRVTVLHQGQVLAEGSLREVQA 254
Cdd:PRK13632 154 ASVLALNPEIIIFDE-STSMLDPKGKREiKKIMVDLRktRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
....*..
gi 490250284 255 NEQVIEV 261
Cdd:PRK13632 232 NKEILEK 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-255 |
1.04e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.45 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqsvDLTTLDPVAIA---RQ 100
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD---GLKVNDPKVDErliRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLAlamkgdksvWASLRARISSEQD--DRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIG 178
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVM---------FGPLRVRGASKEEaeKQARELLAKVGLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 179 MLLVQEPHLLLLDEPAAGMtDAETEYTA-ELFRTLAGQHSLMV-VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQAN 255
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSAL-DPELRHEVlKVMQDLAEEGMTMViVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
25-251 |
1.04e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTldpVAIARQGIGR 104
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-GEDVTH---RSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLK--------MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 185 PHLLLLDEPAAGMtDAETEYTA-ELFRTLAGQHSL--MVVEHDMGFVETIADRVTVLHQGQVLAEGSLRE 251
Cdd:PRK11432 155 PKVLLFDEPLSNL-DANLRRSMrEKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
40-244 |
1.28e-18 |
|
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: 81.60 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSG--KALYDQSVDLTTLDPVAIARQgIGRKFQKPTVFEALTV 117
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGslKVLGQELHGASKKQLVQLRRR-IGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 118 AENLALAMKgdksvwasLRARISSEQ-DDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAG 196
Cdd:TIGR02982 100 RQNVQMALE--------LQPNLSYQEaRERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490250284 197 MTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVEtIADRVTVLHQGQVL 244
Cdd:TIGR02982 172 LDSKSGRDVVELMQKLAKEQgcTILMVTHDNRILD-VADRILQMEDGKLL 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-262 |
2.17e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVdlTTLDPVAIARQG 101
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSiSLCGEPV--PSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRKFQkpTVFEALTVAENLALAMKGDKSVWASLRARISSeqddrlneVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLL 181
Cdd:PRK13537 84 VVPQFD--NLDPDFTVRENLLVFGRYFGLSAAAARALVPP--------LLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPAAGMTDAETEYTAELFRTL-AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE---Q 257
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcD 233
|
....*
gi 490250284 258 VIEVY 262
Cdd:PRK13537 234 VIEIY 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-248 |
3.16e-18 |
|
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: 84.29 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 4 DEGLFTRQLPGdrfreqTDPVLQLENINVSFD--GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA 81
Cdd:TIGR01257 914 NDSFFERELPG------LVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 82 LYDQSVDLTTLDPVaiaRQGIGRKFQKPTVFEALTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERY 161
Cdd:TIGR01257 988 LVGGKDIETNLDAV---RQSLGMCPQHNILFHHLTVAEHILF--------YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 162 RQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQG 241
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
....*..
gi 490250284 242 QVLAEGS 248
Cdd:TIGR01257 1137 RLYCSGT 1143
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-252 |
6.25e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkalYDQSVDLT-------TLDPV 95
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---YRYSGDVLlggrsifNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIARQGIGRKFQKPTVFeALTVAENLALAMKGDKSVwasLRARISSEQDDRLNEV----LRLLRLDGERYRqaglLSHGQ 171
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVglwdAVKDRLSDSPFR----LSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 172 KQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLRE 251
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
.
gi 490250284 252 V 252
Cdd:PRK14271 249 L 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-235 |
9.23e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.07 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVAIARQGIGr 104
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 kfQKPTVFEALTVAENLALamkgdksvWASLRArisseqDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:cd03231 80 --HAPGIKTTLSVLENLRF--------WHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490250284 185 PHLLLLDEPAAGMTDAETEYTAELFR--TLAGQHSLMVVEHDMGFVETIADRV 235
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAghCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-265 |
1.49e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 19 EQTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSV-----DLTTLD 93
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 94 PVAIaRQGIGRKFQKPTVFEALTVAENLALAMKgdksvwaSLRARISSEQDDRLNEVLRLLRLDGERYRQ----AGLLSH 169
Cdd:PRK14246 85 AIKL-RKEVGMVFQQPNPFPHLSIYDNIAYPLK-------SHGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 170 GQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
250
....*....|....*....
gi 490250284 250 REV---QANEQVIEVYLGR 265
Cdd:PRK14246 237 NEIftsPKNELTEKYVIGR 255
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-252 |
1.64e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.06 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 29 NINVSFDGfRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSV--------DLTTLdpvaiaRQ 100
Cdd:PRK13634 13 QYKTPFER-RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkKLKPL------RK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKP--TVFEAlTVAENLALAMK--GDKSVWASLRARisseqddrlnEVLRLLRLDGE-RYRQAGLLSHGQKQFL 175
Cdd:PRK13634 86 KVGIVFQFPehQLFEE-TVEKDICFGPMnfGVSEEDAKQKAR----------EMIELVGLPEElLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 176 EIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTvlVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-235 |
2.34e-17 |
|
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: 78.63 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSF-----DGFR--ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALY---DQSVDLTTL 92
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 93 DP---VAIARQGIG--RKFQK--PTVfEALTVAENLALAMKGDKSVwASLRARisseqddrlnEVLRLLRLDgERYRQA- 164
Cdd:COG4778 83 SPreiLALRRRTIGyvSQFLRviPRV-SALDVVAEPLLERGVDREE-ARARAR----------ELLARLNLP-ERLWDLp 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 165 -GLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV-VEHDMGFVETIADRV 235
Cdd:COG4778 150 pATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVADRV 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-243 |
3.36e-17 |
|
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: 76.87 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRA--LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQGI 102
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNEL-GDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEAlTVAENlalamkgdksvwaslrarisseqddrlnevlrllrldgeryrqagLLSHGQKQFLEIGMLLV 182
Cdd:cd03246 79 GYLPQDDELFSG-SIAEN---------------------------------------------ILSGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 183 QEPHLLLLDEPAAGM-TDAETEYTAELFRTLAGQHSLMVVEHDMGFVEtIADRVTVLHQGQV 243
Cdd:cd03246 113 GNPRILVLDEPNSHLdVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-243 |
8.44e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdlttldPVAIARQGIGR 104
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-------PLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLALAMKGDksvW--ASLRARISSEQDDRLNEvlrllrldgeryrQAGLLSHGQKQFLEIGMLLV 182
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKGQ---WrdAALQALAAVGLADRANE-------------WPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 183 QEPHLLLLDEPaAGMTDAETEY-TAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQV 243
Cdd:PRK11247 150 HRPGLLLLDEP-LGALDALTRIeMQDLIESLWQQHGFTVllVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
40-251 |
8.53e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.85 E-value: 8.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsvDLTTLDPVAIARQGIGRKFQKP-TVFEALTVA 118
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG--DLLTEENVWDIRHKIGMVFQNPdNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 119 ENLALAMKgDKSVwaslrarISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEpAAGMT 198
Cdd:PRK13650 101 DDVAFGLE-NKGI-------PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE-ATSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 199 DAETEYtaELFRTLAG---QHSLMVVE--HDMGFVeTIADRVTVLHQGQVLAEGSLRE 251
Cdd:PRK13650 172 DPEGRL--ELIKTIKGirdDYQMTVISitHDLDEV-ALSDRVLVMKNGQVESTSTPRE 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-262 |
8.88e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 8.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSfdgfRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTrPQSGKALYDQSvDLTTLDPVAIARQgigR 104
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGR-PLSDWSAAELARH---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KF---QKPTVFeALTVAENLALAMKGDKSvwaslrariSSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQ-------F 174
Cdd:COG4138 72 AYlsqQQSPPF-AMPVFQYLALHQPAGAS---------SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQrvrlaavL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:COG4138 142 LQVWPTINPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
....*....
gi 490250284 254 ANEQVIEVY 262
Cdd:COG4138 222 TPENLSEVF 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-248 |
1.53e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.60 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ--SGKALYDQSvDLTTLDPVAIA 98
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGE-SILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKPTVFEALTVAENLALAMKgdksvwASLRARISSEQD-----DRLNEVLRLLRLDG---ERYRQAGlLSHG 170
Cdd:CHL00131 83 HLGIFLAFQYPIEIPGVSNADFLRLAYN------SKRKFQGLPELDpleflEIINEKLKLVGMDPsflSRNVNEG-FSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGM-TDAeTEYTAELFRTLAGQ-HSLMVVEHDMGFVETIA-DRVTVLHQGQVLAEG 247
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLdIDA-LKIIAEGINKLMTSeNSIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
.
gi 490250284 248 S 248
Cdd:CHL00131 235 D 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-262 |
2.74e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQgIGR 104
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-HIQHYASKEVARR-IGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAEnlaLAMKGdKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:PRK10253 86 LAQNATTPGDITVQE---LVARG-RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 185 PHLLLLDEPAAGMTDAET----EYTAELFRTLAgqHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQVIE 260
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQidllELLSELNREKG--YTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
..
gi 490250284 261 VY 262
Cdd:PRK10253 240 IY 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-256 |
3.54e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 44 SLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYDQSVDLTTLDPvaiARQGIGRKFQKPTVFEALTVAENLAL 123
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGS-LTLNGQDHTTTPP---SRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 124 AMKgdksvwASLraRISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETE 203
Cdd:PRK10771 95 GLN------PGL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 204 YTAELFRTLAG--QHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:PRK10771 167 EMLTLVSQVCQerQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-261 |
4.19e-16 |
|
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: 77.54 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITG--KTRPQSGKALY------------------- 83
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 84 ----------DQSVDLTTLDPVAIA--RQGIGRKFQKP-TVFEALTVAENLALAM-----KGDKSVwaslrarisseqdD 145
Cdd:TIGR03269 81 pcpvcggtlePEEVDFWNLSDKLRRriRKRIAIMLQRTfALYGDDTVLDNVLEALeeigyEGKEAV-------------G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 146 RLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPaAGMTDAET-EYTAELFRTLAGQH--SLMVVE 222
Cdd:TIGR03269 148 RAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEP-TGTLDPQTaKLVHNALEEAVKASgiSMVLTS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490250284 223 HDMGFVETIADRVTVLHQGQVLAEGSLREVQAN--EQVIEV 261
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVfmEGVSEV 267
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-252 |
4.24e-16 |
|
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: 76.25 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ---SGKALYDqSVDLTTLDPVA 96
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFD-GEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 97 IaRQGIGRK----FQKP--------TVFEalTVAENLALAMKGDKSvwaslrarissEQDDRLNEVLRLLRLDGERYR-- 162
Cdd:COG0444 80 L-RKIRGREiqmiFQDPmtslnpvmTVGD--QIAEPLRIHGGLSKA-----------EARERAIELLERVGLPDPERRld 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 163 ----QaglLSHGQKQFLEIGMLLVQEPHLLLLDEPAagmtdaeteyTA----------ELFRTLAGQH--SLMVVEHDMG 226
Cdd:COG0444 146 ryphE---LSGGMRQRVMIARALALEPKLLIADEPT----------TAldvtiqaqilNLLKDLQRELglAILFITHDLG 212
|
250 260
....*....|....*....|....*.
gi 490250284 227 FVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:COG0444 213 VVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-230 |
5.97e-16 |
|
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: 73.93 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDpvaIARQGIGR 104
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD---EPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFEALTVAENLalamkgdkSVWaslrARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQE 184
Cdd:TIGR01189 78 LGHLPGLKPELSALENL--------HFW----AAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490250284 185 PHLLLLDEPAAGMTDAETEYTAELFRTLAGQHS--LMVVEHDMGFVET 230
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAHLARGGivLLTTHQDLGLVEA 193
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-254 |
6.67e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.92 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFR-ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDpVAIARQGIGR 104
Cdd:PRK13657 336 EFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID-GTDIRTVT-RASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 KFQKPTVFeALTVAENLALAMKG--DKSVWASLRARISSE----QDDRLNEVLrllrldGERYRQaglLSHGQKQFLEIG 178
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGRPDatDEEMRAAAERAQAHDfierKPDGYDTVV------GERGRQ---LSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 179 MLLVQEPHLLLLDEpAAGMTDAETEYTAEL-FRTLAGQHSLMVVEHDMGFVETiADRVTVLHQGQVLAEGSLREVQA 254
Cdd:PRK13657 484 RALLKDPPILILDE-ATSALDVETEAKVKAaLDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-254 |
7.29e-16 |
|
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: 76.71 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRA--LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgI 102
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-GADLSQWDREELGRH-I 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEAlTVAENLalamkgdksvwaslrARISSEQDDRLNEVLRL-------LRL-DGerYR-----QAGLLSH 169
Cdd:COG4618 409 GYLPQDVELFDG-TIAENI---------------ARFGDADPEKVVAAAKLagvhemiLRLpDG--YDtrigeGGARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 170 GQKQflEIGM--LLVQEPHLLLLDEPAAGMtDAETEytAELFRTLAG----QHSLMVVEHDMGFVEtIADRVTVLHQGQV 243
Cdd:COG4618 471 GQRQ--RIGLarALYGDPRLVVLDEPNSNL-DDEGE--AALAAAIRAlkarGATVVVITHRPSLLA-AVDKLLVLRDGRV 544
|
250
....*....|.
gi 490250284 244 LAEGSLREVQA 254
Cdd:COG4618 545 QAFGPRDEVLA 555
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
55-252 |
7.64e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 55 VIGPNGAGKTTLMDVITGKTRPQSGKALYDQsvDLTTLDPVAIARQGIGRKFQKP--TVFEAlTVAENLALA---MKGDK 129
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--EPITKENIREVRKFVGLVFQNPddQIFSP-TVEQDIAFGpinLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 130 SVWASlrarisseqddRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELF 209
Cdd:PRK13652 112 ETVAH-----------RVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490250284 210 RTLAGQHSLMVV--EHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13652 181 NDLPETYGMTVIfsTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
25-242 |
1.11e-15 |
|
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: 71.71 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkalydqsvdlttldpvaiarqgigr 104
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 105 kfqKPTVFEALTVAenlalamkgdksvwaslrarisseqddrlnevlrllrldgeRYRQaglLSHGQKQFLEIGMLLVQE 184
Cdd:cd03221 56 ---IVTWGSTVKIG-----------------------------------------YFEQ---LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 185 PHLLLLDEPaagmT---DAET-EYTAELFRTLAGqhSLMVVEHDMGFVETIADRVTVLHQGQ 242
Cdd:cd03221 89 PNLLLLDEP----TnhlDLESiEALEEALKEYPG--TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-251 |
1.25e-15 |
|
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: 73.80 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSF----DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD----QSVDLTTLdpvaiaRQGI 102
Cdd:cd03251 5 NVTFrypgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASL------RRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEAlTVAENLALAMKG--DKSVWASLRARISSEQDDRLNEvlrllRLD---GERyrqAGLLSHGQKQFLEI 177
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAYGRPGatREEVEEAARAANAHEFIMELPE-----GYDtviGER---GVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490250284 178 GMLLVQEPHLLLLDEpAAGMTDAETEY--TAELFRTLAGQHSLmVVEHDMGFVETiADRVTVLHQGQVLAEGSLRE 251
Cdd:cd03251 150 ARALLKDPPILILDE-ATSALDTESERlvQAALERLMKNRTTF-VIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
55-257 |
1.31e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 55 VIGPNGAGKTTLMDVITGKTRPQSGK------ALYD--QSVDLTTldpvaiARQGIGRKFQKPTVFEALTVAENLALAMK 126
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFDaeKGICLPP------EKRRIGYVFQDARLFPHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 127 gdksvwaslraRISSEQDDRlneVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtdaeteyta 206
Cdd:PRK11144 103 -----------KSMVAQFDK---IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL--------- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 207 ELFR---------TLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:PRK11144 160 DLPRkrellpyleRLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-256 |
1.37e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 11 QLPGDRFREQTDPVLQLENINVSFDG--FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVD 88
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-QP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 89 LTTLDPVAIaRQGIGRKFQKPTVFEAlTVAENLALAmkgdksvwaslrarISSEQDDRLNEVLR------LL----RLD- 157
Cdd:PRK11160 404 IADYSEAAL-RQAISVVSQRVHLFSA-TLRDNLLLA--------------APNASDEALIEVLQqvglekLLeddkGLNa 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 158 --GERYRQaglLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEYTA-ELFRTLAGQHSLMVVEHDMGFVETIaDR 234
Cdd:PRK11160 468 wlGEGGRQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGL-DAETERQIlELLAEHAQNKTVLMITHRLTGLEQF-DR 542
|
250 260
....*....|....*....|..
gi 490250284 235 VTVLHQGQVLAEGSLREVQANE 256
Cdd:PRK11160 543 ICVMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-248 |
1.41e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSF---DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPvAIARQGIGRKFQ 107
Cdd:PRK10790 345 NVSFayrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR-PLSSLSH-SVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 108 KPTVFeALTVAENLALAMK-GDKSVWASLRARisseqddRLNEVLRLLRlDGERYR---QAGLLSHGQKQFLEIGMLLVQ 183
Cdd:PRK10790 423 DPVVL-ADTFLANVTLGRDiSEEQVWQALETV-------QLAELARSLP-DGLYTPlgeQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 184 EPHLLLLDEPAAGMtDAETEYT-AELFRTLAGQHSLMVVEHDMgfvETI--ADRVTVLHQGQVLAEGS 248
Cdd:PRK10790 494 TPQILILDEATANI-DSGTEQAiQQALAAVREHTTLVVIAHRL---STIveADTILVLHRGQAVEQGT 557
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-252 |
1.97e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgi 102
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVA-GDDVEALSARAASRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 grkfqkptvfeALTVAENLALAMKGDKSVWASL-----RARISSEQDDRLNEVLRLL-RLDGERY--RQAGLLSHGQKQF 174
Cdd:PRK09536 79 -----------VASVPQDTSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAAVERAMeRTGVAQFadRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVE-HDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-257 |
2.00e-15 |
|
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: 75.49 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKT----TLMDVITGKTRPQSGKALYDqSVDLTTL 92
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFD-GQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 93 DPVAIAR---QGIGRKFQKPTVfeALT--------VAENLAL--AMKGdksvwASLRARISseqddrlnEVLRLLRLDGE 159
Cdd:COG4172 82 SERELRRirgNRIAMIFQEPMT--SLNplhtigkqIAEVLRLhrGLSG-----AAARARAL--------ELLERVGIPDP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 160 RYR------QaglLSHGQKQFLEIGMLLVQEPHLLLLDEPaagmtdaeTeyTA----------ELFRTLAGQH--SLMVV 221
Cdd:COG4172 147 ERRldayphQ---LSGGQRQRVMIAMALANEPDLLIADEP--------T--TAldvtvqaqilDLLKDLQRELgmALLLI 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 490250284 222 EHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:COG4172 214 THDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-252 |
2.25e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFD-----GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVAI- 97
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 -ARQGIGRKFQKP--TVFEAlTVAENLALAMKgdksvwaslRARISSEQDDRL-NEVLRLLRLDGERYRQAGL-LSHGQK 172
Cdd:PRK13643 81 pVRKKVGVVFQFPesQLFEE-TVLKDVAFGPQ---------NFGIPKEKAEKIaAEKLEMVGLADEFWEKSPFeLSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 173 QFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTL--AGQhSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLR 250
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhqSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS 229
|
..
gi 490250284 251 EV 252
Cdd:PRK13643 230 DV 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-242 |
3.69e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.15 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTL------MDVITGKTRPQS-----GKALYDQSVDLTT 91
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFlkclnrMNELESEVRVEGrveffNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 92 LdpvaiaRQGIGRKFQKPTVFeALTVAENLALAMKgdksvwaSLRARISSEQDDRLNEVLRLLRLDGE----RYRQAGLL 167
Cdd:PRK14258 86 L------RRQVSMVHPKPNLF-PMSVYDNVAYGVK-------IVGWRPKLEIDDIVESALKDADLWDEikhkIHKSALDL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 168 SHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRT--LAGQHSLMVVEHDMGFVETIADRVTVLHQGQ 242
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-258 |
4.07e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.76 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQgIGRKFQKPTVFeALTVAE 119
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLVQYDHHYLHRQ-VALVGQEPVLF-SGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 120 NLA--LAMKGDKSVWASLRArisSEQDDRLNEVLRllRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEpAAGM 197
Cdd:TIGR00958 574 NIAygLTDTPDEEIMAAAKA---ANAHDFIMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE-ATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 198 TDAETEYTAELFRTLAGQhSLMVVEHDMGFVETiADRVTVLHQGQVLAEGSLREVQANEQV 258
Cdd:TIGR00958 648 LDAECEQLLQESRSRASR-TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
40-211 |
5.67e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsvDLTTLDPVAIARQGIG-RKFQKPtvfeALTVA 118
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--GDIDDPDVAEACHYLGhRNAMKP----ALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 119 ENLALamkgdksvWASLRARisseQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMT 198
Cdd:PRK13539 92 ENLEF--------WAAFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170
....*....|...
gi 490250284 199 DAETEYTAELFRT 211
Cdd:PRK13539 160 AAAVALFAELIRA 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-245 |
5.87e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.38 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSF----DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkALYDQSVDLTTLDPVAIA 98
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG-TYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 ---RQGIGRKFQKPTVFEALTVAENLALAmkgdkSVWASLRARissEQDDRLNEVLRLLRLdGER-YRQAGLLSHGQKQF 174
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVP-----AVYAGLERK---QRLLRAQELLQRLGL-EDRvEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDmGFVETIADRVTVLHQGQVLA 245
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
39-260 |
7.25e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.53 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 39 ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGkalyDQS---VDLTTL--DPVAIARQGIGRKFQKP-TVF 112
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDN----PNSkitVDGITLtaKTVWDIREKVGIVFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EALTVAENLALAMKGDksvwASLRARISSEQDDRLNEVLRLLRLDGEryrqAGLLSHGQKQFLEIGMLLVQEPHLLLLDE 192
Cdd:PRK13640 98 VGATVGDDVAFGLENR----AVPRPEMIKIVRDVLADVGMLDYIDSE----PANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 193 PAAGMTDAETEYTAELFRTLAGQHSLMVVE--HDMGFVEtIADRVTVLHQGQVLAEGSLREVQANEQVIE 260
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISitHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-252 |
8.13e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALT--DLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALY-DQSVDLTTLDPVaia 98
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnNQAITDDNFEKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKP-TVFEALTVAENLALAMKgDKSVWASLRARISSEQddrLNEVLRLLRLDGERYRqaglLSHGQKQFLEI 177
Cdd:PRK13648 82 RKHIGIVFQNPdNQFVGSIVKYDVAFGLE-NHAVPYDEMHRRVSEA---LKQVDMLERADYEPNA----LSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 178 GMLLVQEPHLLLLDEpAAGMTDAET-EYTAELFRTLAGQHSLMVVE--HDMgfVETI-ADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13648 154 AGVLALNPSVIILDE-ATSMLDPDArQNLLDLVRKVKSEHNITIISitHDL--SEAMeADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-243 |
8.99e-15 |
|
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: 70.54 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSfdgfRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQG 101
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-GKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IG-----RKfqKPTVFEALTVAENLALAMkgdksvwaslrarisseqddrlnevlrllrldgeryrqagLLSHGQKQFLE 176
Cdd:cd03215 77 IAyvpedRK--REGLVLDLSVAENIALSS----------------------------------------LLSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 177 IGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-248 |
1.13e-14 |
|
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: 70.99 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 16 RFREQTDPVLQleniNVSFDgfraltdlslaIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPV 95
Cdd:cd03244 11 RYRPNLPPVLK----NISFS-----------IKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID-GVDISKIGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIaRQGIGRKFQKPTVFEAlTVAENLA-LAMKGDKSVW-----ASLRARISSeQDDRLNEVLRLlrlDGEryrqagLLSH 169
Cdd:cd03244 75 DL-RSRISIIPQDPVLFSG-TIRSNLDpFGEYSDEELWqalerVGLKEFVES-LPGGLDTVVEE---GGE------NLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 170 GQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVVEHDmgfVETIA--DRVTVLHQGQVLAEG 247
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHR---LDTIIdsDRILVLDKGRVVEFD 219
|
.
gi 490250284 248 S 248
Cdd:cd03244 220 S 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
38-212 |
1.19e-14 |
|
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: 71.15 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 38 RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGktRPQSGKALYDQsvdlTTLDPVAIARQgigrKFQKPTVF----- 112
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTSGQ----ILFNGQPRKPD----QFQKCVAYvrqdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 ---EALTVAENLALAMKgdksvwASLRARISSEQDDRLNEVLRLL-----RLDGERYRQaglLSHGQKQFLEIGMLLVQE 184
Cdd:cd03234 91 illPGLTVRETLTYTAI------LRLPRKSSDAIRKKRVEDVLLRdlaltRIGGNLVKG---ISGGERRRVSIAVQLLWD 161
|
170 180
....*....|....*....|....*...
gi 490250284 185 PHLLLLDEPAAGMtDAETEYtaELFRTL 212
Cdd:cd03234 162 PKVLILDEPTSGL-DSFTAL--NLVSTL 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-243 |
1.67e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 12 LPGDRFREQTD-PVLQLENInvSFDGFRaltDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsVDLT 90
Cdd:PRK15439 255 LPGNRRQQAAGaPVLTVEDL--TGEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG-KEIN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 91 TLDPVAIARQGI---GRKFQKPTVFEALTVAENLALAMKGDKSVWAslrarisseQDDRLNEVLrllrldgERYRQA--- 164
Cdd:PRK15439 329 ALSTAQRLARGLvylPEDRQSSGLYLDAPLAWNVCALTHNRRGFWI---------KPARENAVL-------ERYRRAlni 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 165 ---------GLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADR 234
Cdd:PRK15439 393 kfnhaeqaaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNvAVLFISSDLEEIEQMADR 472
|
....*....
gi 490250284 235 VTVLHQGQV 243
Cdd:PRK15439 473 VLVMHQGEI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-232 |
1.73e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.66 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 13 PGDRFreqTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK---------ALY 83
Cdd:TIGR03719 314 PGPRL---GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTieigetvklAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 84 DQSVDltTLDPvaiarqgigrkfqKPTVFEAltVAENLALAMKGDKSVWAslRARISseqddRLNevlrllRLDGERYRQ 163
Cdd:TIGR03719 391 DQSRD--ALDP-------------NKTVWEE--ISGGLDIIKLGKREIPS--RAYVG-----RFN------FKGSDQQKK 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 164 AGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAET----EYTAELFrtlAGqhSLMVVEHDMGFVETIA 232
Cdd:TIGR03719 441 VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL-DVETlralEEALLNF---AG--CAVVISHDRWFLDRIA 507
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-252 |
1.93e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 34 FDGfRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDP---VAIARQGIGRKFQKP- 109
Cdd:PRK13649 18 FEG-RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD-DTLITSTSKnkdIKQIRKKVGLVFQFPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 110 -TVFEAlTVAENLALAMKGdksvwaslrARISSEQDDRL-NEVLRLLRLDGERYRQAGL-LSHGQKQFLEIGMLLVQEPH 186
Cdd:PRK13649 96 sQLFEE-TVLKDVAFGPQN---------FGVSQEEAEALaREKLALVGISESLFEKNPFeLSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 187 LLLLDEPAAGMTDAETEYTAELFRTL-AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-237 |
1.95e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.51 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 19 EQTDPVLQLENINVSFDGFraltdlSLAIGVGELRC-----VIGPNGAGKTTLMDVITGKTRPQSGkalydqSVDLTtld 93
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGF------SLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEG------EVDED--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 94 pVAIArqgigrkfQKPTVFEAltvaenlalamKGDKSVWASLRARISSEQDDRL--NEVLRLLRLDGERYRQAGLLSHGQ 171
Cdd:COG1245 401 -LKIS--------YKPQYISP-----------DYDGTVEEFLRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGE 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 172 KQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEY-TAELFRTLAGQH--SLMVVEHDMGFVETIADRVTV 237
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHL-DVEQRLaVAKAIRRFAENRgkTAMVVDHDIYLIDYISDRLMV 528
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
23-247 |
2.49e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD----QSVDLTTL---DPV 95
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrdgQLRDLYALseaERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIARQGIGRKFQKPtvfealtvAENLALAMKGDKSVWASLRA-------RISSEQDDRLNEV-LRLLRLDGeryrQAGLL 167
Cdd:PRK11701 85 RLLRTEWGFVHQHP--------RDGLRMQVSAGGNIGERLMAvgarhygDIRATAGDWLERVeIDAARIDD----LPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 168 SHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLHQGQVLA 245
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVviVTHDLAVARLLAHRLLVMKQGRVVE 232
|
..
gi 490250284 246 EG 247
Cdd:PRK11701 233 SG 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
41-256 |
2.60e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.95 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 41 TDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLDPVAIARQGIGRKFQKPTVFEALTVAE 119
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 120 NLALAMKgdksvwaslrarisseQDDRLNEVLR----LLRLDGERYRQAGL-----LSHGQKQFLEIGMLLVQEPHLLLL 190
Cdd:PRK11831 104 NVAYPLR----------------EHTQLPAPLLhstvMMKLEAVGLRGAAKlmpseLSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 191 DEPAAGMTDAETEYTAELFRTLagQHSL----MVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANE 256
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISEL--NSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-243 |
3.45e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.52 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFR-ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLD--PVAIARQ 100
Cdd:PRK10908 1 MIRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH-DITRLKnrEVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQDdrlnevlRLLRLDGERYRQAGlLSHGQKQFLEIGML 180
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALD-------KVGLLDKAKNFPIQ-LSGGEQQRVGIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 181 LVQEPHLLLLDEPAAGMTDAETEYTAELFRTL--AGQHSLMVVeHDMGFVETIADRVTVLHQGQV 243
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFnrVGVTVLMAT-HDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
37-247 |
3.81e-14 |
|
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: 69.48 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 37 FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLttldPVAIarqGIGrkFQkptvfEALT 116
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS----LLGL---GGG--FN-----PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 117 VAENLAlamkgdksvwasLRARIS----SEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDE 192
Cdd:cd03220 101 GRENIY------------LNGRLLglsrKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 193 P-AAGmtDAET-EYTAELFRTL-AGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:cd03220 169 VlAVG--DAAFqEKCQRRLRELlKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-254 |
5.95e-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: 71.58 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 20 QTDpVLQLENINVSFDGFRALTDLSLAIGV--GELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVai 97
Cdd:TIGR01257 1934 KTD-ILRLNELTKVYSGTSSPAVDRLCVGVrpGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 aRQGIGRKFQKPTVFEALTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYL--------YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMtdaETEYTAELFRTLAG----QHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGM---DPQARRMLWNTIVSiireGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
.
gi 490250284 254 A 254
Cdd:TIGR01257 2159 S 2159
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-262 |
1.01e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDG-FRALTDLSLAIGVGELrCVI-GPNGAGKTTLMDVITGKTRPQSGKALYDQSVdLTTLDPvaiARQGI 102
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEF-IVLvGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-VNELEP---ADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEALTVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDG---ERYRQaglLSHGQKQFLEIGM 179
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLK--------IRGMPKAEIEERVAEAARILELEPlldRKPRE---LSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 180 LLVQEPHLLLLDEPAAGMtDA--------ETEytaELFRTLaGQHSLMVVeHDMgfVE--TIADRVTVLHQGQVlaegsl 249
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNL-DAklrvqmrlEIQ---RLHRRL-KTTSLYVT-HDQ--VEamTLADRVVVMNGGVA------ 213
|
250
....*....|....*.
gi 490250284 250 revqanEQV---IEVY 262
Cdd:PRK11650 214 ------EQIgtpVEVY 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-256 |
1.13e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 32 VSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTrPQSGKaLYDQSVDLTTLDPvAIARQGIGRKFQKPTV 111
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGS-LKINGIELRELDP-ESWRKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 112 FEAlTVAENLALAMK--GDKSVWASLrarisseQDDRLNEVLRLLR--LDGERYRQAGLLSHGQKQFLEIGMLLVQEPHL 187
Cdd:PRK11174 435 PHG-TLRDNVLLGNPdaSDEQLQQAL-------ENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 188 LLLDEPAAGMtDAETE--YTAELFRTLAGQHSLMVVeHDMGFVETIaDRVTVLHQGQVLAEGSLREVQANE 256
Cdd:PRK11174 507 LLLDEPTASL-DAHSEqlVMQALNAASRRQTTLMVT-HQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-257 |
1.25e-13 |
|
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: 70.10 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 19 EQTDPVLQLENINVSF-----------DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLmdvitGKT--R--PQSGKALY 83
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL-----GLAllRliPSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 84 DqSVDLTTLDPVAI--ARQGIGRKFQKP--------TVFEalTVAENLALAMKGdksvwasLRARissEQDDRLNEVLRL 153
Cdd:COG4172 345 D-GQDLDGLSRRALrpLRRRMQVVFQDPfgslsprmTVGQ--IIAEGLRVHGPG-------LSAA---ERRARVAEALEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 154 LRLDGE-RYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPaagmtdaeteyTA-----------ELFRTLAGQHSL--M 219
Cdd:COG4172 412 VGLDPAaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP-----------TSaldvsvqaqilDLLRDLQREHGLayL 480
|
250 260 270
....*....|....*....|....*....|....*...
gi 490250284 220 VVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:COG4172 481 FISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
31-251 |
1.25e-13 |
|
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: 68.41 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSF---DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLDPVaiaRQGIGRKF 106
Cdd:cd03253 5 NVTFaydPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDIREVTLDSL---RRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 107 QKPTVFEAlTVAENLALAMKG---DKSVWASLRARIsseqDDRLnevlrlLRLD-------GERyrqaGL-LSHGQKQFL 175
Cdd:cd03253 82 QDTVLFND-TIGYNIRYGRPDatdEEVIEAAKAAQI----HDKI------MRFPdgydtivGER----GLkLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 176 EIGMLLVQEPHLLLLDEpAAGMTDAETEytAELFRTL---AGQHSLMVVEHDmgfVETI--ADRVTVLHQGQVLAEGSLR 250
Cdd:cd03253 147 AIARAILKNPPILLLDE-ATSALDTHTE--REIQAALrdvSKGRTTIVIAHR---LSTIvnADKIIVLKDGRIVERGTHE 220
|
.
gi 490250284 251 E 251
Cdd:cd03253 221 E 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
40-243 |
1.46e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 67.88 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQgIGRKFQKPTVFeALTVAE 119
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK-PISQYEHKYLHSK-VSLVGQEPVLF-ARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 120 NLALAMkGDKSVWASLRARISSEQDDRLNEVLRLLRLD-GERyrqAGLLSHGQKQFLEIGMLLVQEPHLLLLDEpAAGMT 198
Cdd:cd03248 107 NIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEvGEK---GSQLSGGQKQRVAIARALIRNPQVLILDE-ATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490250284 199 DAETEYTAE-LFRTLAGQHSLMVVEHDMGFVETiADRVTVLHQGQV 243
Cdd:cd03248 182 DAESEQQVQqALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-257 |
1.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.70 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 38 RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVDLTTLDP-VAIARQGIGRKFQKPTV--FE 113
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTiTIAGYHITPETGNKnLKKLRKKVSLVFQFPEAqlFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 114 AlTVAENLalaMKGDKSVWASlrariSSEQDDRLNEVLRLLRLDGERYRQAGL-LSHGQKQFLEIGMLLVQEPHLLLLDE 192
Cdd:PRK13641 101 N-TVLKDV---EFGPKNFGFS-----EDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 193 PAAGMTDAETEYTAELFRTL--AGqHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYqkAG-HTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
37-263 |
1.70e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 37 FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSV----DLTT-LDPvaiarqgigrkfqkptv 111
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsallELGAgFHP----------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 112 feALTVAENlalamkgdksvwASLRARI----SSEQDDRLNEVLRLlrldgeryrqAGLlshgqKQFLE-------IGML 180
Cdd:COG1134 102 --ELTGREN------------IYLNGRLlglsRKEIDEKFDEIVEF----------AEL-----GDFIDqpvktysSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 181 --------LVQEPHLLLLDEP-AAGmtDAE-TEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:COG1134 153 arlafavaTAVDPDILLVDEVlAVG--DAAfQKKCLARIRELRESGrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
250
....*....|....
gi 490250284 250 REvqaneqVIEVYL 263
Cdd:COG1134 231 EE------VIAAYE 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
40-257 |
2.41e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSG---------KALYDQSVDLTTLDP--VAIARQGIGRKFQK 108
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtiNLVRDKDGQLKVADKnqLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 109 PTVFEALTVAENLalamkgdksVWASLRARISSEQDDRLNEVLRLLRL---DGERYRQAGLLSHGQKQFLEIGMLLVQEP 185
Cdd:PRK10619 101 FNLWSHMTVLENV---------MEAPIQVLGLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490250284 186 HLLLLDEPAAGMtdaETEYTAELFR---TLAGQHSLMVV-EHDMGFVETIADRVTVLHQGQVLAEGSLREVQANEQ 257
Cdd:PRK10619 172 EVLLFDEPTSAL---DPELVGEVLRimqQLAEEGKTMVVvTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
39-255 |
2.45e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.91 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 39 ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPV---AIARQGIGRKFQKPTVFEAL 115
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAelrEVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 116 TVAENLALAMKgdksvwasLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAA 195
Cdd:PRK10070 122 TVLDNTAFGME--------LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 196 GMTD-AETEYTAELFRTLAG-QHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQAN 255
Cdd:PRK10070 194 ALDPlIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-256 |
3.15e-13 |
|
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: 67.18 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSFD-----GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQGIGRK 105
Cdd:cd03249 5 NVSFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLNLRWL-RSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 106 FQKPTVFEAlTVAENLALamkGDKSVWASLRARISSEQD---------DRLNEVLrllrldGERYRQaglLSHGQKQFLE 176
Cdd:cd03249 83 SQEPVLFDG-TIAENIRY---GKPDATDEEVEEAAKKANihdfimslpDGYDTLV------GERGSQ---LSGGQKQRIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 177 IGMLLVQEPHLLLLDEpAAGMTDAETEYTAE--LFRTLAGQHSLmVVEHDMgfvETI--ADRVTVLHQGQVLAEGSLREV 252
Cdd:cd03249 150 IARALLRNPKILLLDE-ATSALDAESEKLVQeaLDRAMKGRTTI-VIAHRL---STIrnADLIAVLQNGQVVEQGTHDEL 224
|
....
gi 490250284 253 QANE 256
Cdd:cd03249 225 MAQK 228
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-257 |
6.42e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ-SGKALYDQSVDLTTLDPVAIARQGI 102
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTvfEALTVAENLALamkgDKSVWASLRARISSEQD-----DRLNEVLRLLRLDGE---RYRQAGlLSHGQKQF 174
Cdd:PRK09580 81 FMAFQYPV--EIPGVSNQFFL----QTALNAVRSYRGQEPLDrfdfqDLMEEKIALLKMPEDlltRSVNVG-FSGGEKKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLA-GQHSLMVVEHDMGFVETIA-DRVTVLHQGQVLAEGSLREV 252
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDFTLV 233
|
....*
gi 490250284 253 QANEQ 257
Cdd:PRK09580 234 KQLEE 238
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-259 |
6.73e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.89 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGkTRPQ---SGKALYDQSV----DLTtldpvA 96
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVcrfkDIR-----D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 97 IARQGIGRKFQKPTVFEALTVAENLAL----AMKG--DksvWaslrarisseqDDRLNEVLRLLRLDGERYRQAGLLSH- 169
Cdd:NF040905 75 SEALGIVIIHQELALIPYLSIAENIFLgnerAKRGviD---W-----------NETNRRARELLAKVGLDESPDTLVTDi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 170 --GQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:NF040905 141 gvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
250
....*....|...
gi 490250284 247 GSLREVQANEQVI 259
Cdd:NF040905 221 LDCRADEVTEDRI 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-196 |
6.98e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKalydqsvdLTTLD-PVAIAR--- 99
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR--------VEVLGgDMADARhrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 ----------QGIGRKFQkPTvfeaLTVAENLALamkgdksvWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSH 169
Cdd:NF033858 73 avcpriaympQGLGKNLY-PT----LSVFENLDF--------FGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSG 139
|
170 180
....*....|....*....|....*..
gi 490250284 170 GQKQFLEIGMLLVQEPHLLLLDEPAAG 196
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTG 166
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
16-237 |
7.96e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 16 RFREQTDPVLQLENINVSFDGFraltdlSLAIGVGELRC-----VIGPNGAGKTTLMDVITGKTRPQSGKAlyDQSVDlt 90
Cdd:PRK13409 332 RDESERETLVEYPDLTKKLGDF------SLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELK-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 91 tldpVAIARQGIGRKFQkptvfeaLTVAENLAlamkgdksvwaSLRARISSEQDDrlNEVLRLLRLDGERYRQAGLLSHG 170
Cdd:PRK13409 402 ----ISYKPQYIKPDYD-------GTVEDLLR-----------SITDDLGSSYYK--SEIIKPLQLERLLDKNVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEYT-AELFRTLAGQH--SLMVVEHDMGFVETIADRVTV 237
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHL-DVEQRLAvAKAIRRIAEEReaTALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-224 |
9.85e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIaRQG 101
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE-DISTLKPEIY-RQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRKFQKPTVFeALTVAENLALAmkgdksvWaslRARISSEQDDRLNEVLRLLRLDGERYRQA-GLLSHGQKQFLEIGML 180
Cdd:PRK10247 83 VSYCAQTPTLF-GDTVYDNLIFP-------W---QIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490250284 181 LVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHD 224
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-246 |
1.03e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 18 REQTDPVLQLENINVSfdgfRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTldPVA 96
Cdd:COG1129 250 AAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgKPVRIRS--PRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 97 IARQGIG-----RKFQkpTVFEALTVAENLALAMKGDKSVWASLRARissEQDDRLNEVLRLLRLD-GERYRQAGLLSHG 170
Cdd:COG1129 324 AIRAGIAyvpedRKGE--GLVLDLSIRENITLASLDRLSRGGLLDRR---RERALAEEYIKRLRIKtPSPEQPVGNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMtD--AETE-YtaELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGI-DvgAKAEiY--RLIRELAAEgKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-243 |
1.42e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 45 LAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTL--DPvaiarqgigRKFQKPTVFEalTVAENLA 122
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLqqDP---------PRNVEGTVYD--FVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 123 LAMKGDKSVWASLR--ARISSEQ--------------------DDRLNEVLRLLRLDGERyrQAGLLSHGQKQFLEIGML 180
Cdd:PRK11147 93 EQAEYLKRYHDISHlvETDPSEKnlnelaklqeqldhhnlwqlENRINEVLAQLGLDPDA--ALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 181 LVQEPHLLLLDEPAAGMtDAET-EYTAELFRTLAGqhSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHL-DIETiEWLEGFLKTFQG--SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
39-252 |
1.80e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 39 ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYDQSVDLTTLDPVAIARQGIGRKFQKP------TVF 112
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK-VYVDGLDTSDEENLWDIRNKAGMVFQNPdnqivaTIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EAlTVA---ENLALAMKgdksvwaSLRARIsseqDDRLNEVlrllrlDGERYRQAG--LLSHGQKQFLEIGMLLVQEPHL 187
Cdd:PRK13633 104 EE-DVAfgpENLGIPPE-------EIRERV----DESLKKV------GMYEYRRHAphLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 188 LLLDEPAAGMTDAETEYTAELFRTLAGQHSLMVV--EHDMGfvETI-ADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIIliTHYME--EAVeADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
37-257 |
2.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 37 FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA--LYDQSVDLTTLDPVAIA---------------- 98
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 ----RQGIGRKFQ--KPTVFEAlTVAENL---ALAMKGDKSvwaslrarissEQDDRLNEVLRLLRLDgERY--RQAGLL 167
Cdd:PRK13651 100 ikeiRRRVGVVFQfaEYQLFEQ-TIEKDIifgPVSMGVSKE-----------EAKKRAAKYIELVGLD-ESYlqRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 168 SHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKD 246
|
250
....*....|.
gi 490250284 247 GSLREVQANEQ 257
Cdd:PRK13651 247 GDTYDILSDNK 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-263 |
3.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.11 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFD---GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQsvDLTTLDPVAIA 98
Cdd:PRK13642 2 NKILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG--ELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIGRKFQKP-TVFEALTVAENLALAMKGdksvwaslRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEI 177
Cdd:PRK13642 80 RRKIGMVFQNPdNQFVGATVEDDVAFGMEN--------QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETiADRVTVLHQGQVLAEGSLREVQA- 254
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVlsITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAt 230
|
....*....
gi 490250284 255 NEQVIEVYL 263
Cdd:PRK13642 231 SEDMVEIGL 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
50-237 |
4.00e-12 |
|
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: 64.35 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 50 GELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqsvdlttLDPVAIARQGIGRKFQkptvfeaLTVAENLA--LAMKG 127
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-------LDTVSYKPQYIKADYE-------GTVRDLLSsiTKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 128 DKSVWASlrarisseqddrlnEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAE 207
Cdd:cd03237 91 THPYFKT--------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|..
gi 490250284 208 LFRTLAGQH--SLMVVEHDMGFVETIADRVTV 237
Cdd:cd03237 157 VIRRFAENNekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-235 |
4.35e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 9 TRQLPGDRFrEQTDPV----LQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD 84
Cdd:PRK15064 301 SRQNPFIRF-EQDKKLhrnaLEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 85 QSVDlttldpvaiarqgIGRKFQKPTV-FEA-LTVAEnlalamkgdksvWASlraRISSEQDDRL--NEVL-RLLRLDGE 159
Cdd:PRK15064 380 ENAN-------------IGYYAQDHAYdFENdLTLFD------------WMS---QWRQEGDDEQavRGTLgRLLFSQDD 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 160 RYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAET----EYTAELFrtlagQHSLMVVEHDMGFVETIADRV 235
Cdd:PRK15064 432 IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM-DMESieslNMALEKY-----EGTLIFVSHDREFVSSLATRI 505
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
36-252 |
4.38e-12 |
|
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: 65.53 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 36 GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD----QSVDLTTLdpvaiaRQGIGRKFQKPTV 111
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTL------RQFINYLPQEPYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 112 FEAlTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLrlLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLD 191
Cdd:TIGR01193 560 FSG-SILENLLLGAKENVSQDEIWAACEIAEIKDDIENMP--LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 192 EPAAGMtDAETEYTAeLFRTLAGQH-SLMVVEHDMGfVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:TIGR01193 637 ESTSNL-DTITEKKI-VNNLLNLQDkTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-252 |
4.60e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 19 EQTDPVLQLENINVSF-----------DGFRALTDLSLAIGVGELRCVIGPNGAGKTT----LMDVItgktrPQSGKALY 83
Cdd:PRK15134 270 EPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 84 D----QSVDLTTLDPVaiaRQGIGRKFQKP--TVFEALTVAENLAlamKGDKSVWASLRARissEQDDRLNEVLRLLRLD 157
Cdd:PRK15134 345 DgqplHNLNRRQLLPV---RHRIQVVFQDPnsSLNPRLNVLQIIE---EGLRVHQPTLSAA---QREQQVIAVMEEVGLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 158 GE-RYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSL--MVVEHDMGFVETIADR 234
Cdd:PRK15134 416 PEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQ 495
|
250
....*....|....*...
gi 490250284 235 VTVLHQGQVLAEGSLREV 252
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERV 513
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-260 |
5.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDG-----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSG---------KALYDQSV 87
Cdd:PRK13631 19 DIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyiGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 88 DLTTLDPVAIA-----RQGIGRKFQKP--TVFEAlTVAENLA---LAMKGDKSvwaslrarissEQDDRLNEVLRLLRLD 157
Cdd:PRK13631 99 LITNPYSKKIKnfkelRRRVSMVFQFPeyQLFKD-TIEKDIMfgpVALGVKKS-----------EAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 158 gERY--RQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDA-ETEYTAELFRTLAGQHSLMVVEHDMGFVETIADR 234
Cdd:PRK13631 167 -DSYleRSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADE 245
|
250 260
....*....|....*....|....*.
gi 490250284 235 VTVLHQGQVLAEGSLREVQANEQVIE 260
Cdd:PRK13631 246 VIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-249 |
5.92e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENI-------NVSFDgfrALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYdQSVDLTTLDPV 95
Cdd:PRK11629 4 ILLQCDNLckryqegSVQTD---VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIF-NGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIAR---QGIGRKFQKPTVFEALTVAENLA--LAMKGDKSVWASLRARisseqddrlnEVLRLLRLDGERYRQAGLLSHG 170
Cdd:PRK11629 80 AKAElrnQKLGFIYQFHHLLPDFTALENVAmpLLIGKKKPAEINSRAL----------EMLAAVGLEHRANHRPSELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIaDRVTVLHQGQVLAEGS 248
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
.
gi 490250284 249 L 249
Cdd:PRK11629 229 L 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
35-247 |
8.51e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 35 DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVDLT-TLDPVAIARQGIGRKFQKPTVF 112
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKiSILGQPTRQAlQKNLVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EALTvaenlalaMKGDKSVWASLRaRISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDE 192
Cdd:PRK15056 98 EDVV--------MMGRYGHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 193 PAAGMtDAETE-YTAELFRTLAGQHSLMVVE-HDMGFVETIADrVTVLHQGQVLAEG 247
Cdd:PRK15056 169 PFTGV-DVKTEaRIISLLRELRDEGKTMLVStHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-252 |
9.07e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKT----TLMDVI-TGKTRPQSGKALY----DQSVDLT 90
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeQAGGLVQCDKMLLrrrsRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 91 TLDPVAIAR---QGIGRKFQKP--TVFEALTVAENLAlamkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYRQAG 165
Cdd:PRK10261 92 EQSAAQMRHvrgADMAMIFQEPmtSLNPVFTVGEQIA----------ESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 166 L------LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTV 237
Cdd:PRK10261 162 LsryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEIADRVLV 241
|
250
....*....|....*
gi 490250284 238 LHQGQVLAEGSLREV 252
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-265 |
1.24e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 27 LENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLDPVaiARQGIGRK 105
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgKEIDFKSSKEA--LENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 106 FQKPTVFEALTVAENLALAMKGDKSVWAslrarissEQDDRLNEVLRL---LRLDGERYRQAGLLSHGQKQFLEIGMLLV 182
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFV--------DQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 183 QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQAnEQVIEV 261
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGcGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTM-DKIIAM 229
|
....
gi 490250284 262 YLGR 265
Cdd:PRK10982 230 MVGR 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-252 |
1.30e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.26 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 37 FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqsvDLTT--------LDPVaiaRQGIGRKFQK 108
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD---DITIthktkdkyIRPV---RKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 109 P--TVFEAlTVAENLALamkGDKSVWASLRarissEQDDRLNEVLRLLRLDGERYRQAGL-LSHGQKQFLEIGMLLVQEP 185
Cdd:PRK13646 94 PesQLFED-TVEREIIF---GPKNFKMNLD-----EVKNYAHRLLMDLGFSRDVMSQSPFqMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 186 HLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-252 |
1.51e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.39 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ---SGKALYDQSVDLTTLDPV 95
Cdd:COG4170 2 PLLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 ---AIARQGIGRKFQKPTVF--EALTVAENLALAM-----KGdkSVWASLRARIsseqddrlNEVLRLLRLDGERYRQAG 165
Cdd:COG4170 82 errKIIGREIAMIFQEPSSCldPSAKIGDQLIEAIpswtfKG--KWWQRFKWRK--------KRAIELLHRVGIKDHKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 166 L------LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtdaETEYTAELFRTLA-----GQHSLMVVEHDMGFVETIADR 234
Cdd:COG4170 152 MnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAM---ESTTQAQIFRLLArlnqlQGTSILLISHDLESISQWADT 228
|
250
....*....|....*...
gi 490250284 235 VTVLHQGQVLAEGSLREV 252
Cdd:COG4170 229 ITVLYCGQTVESGPTEQI 246
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-232 |
3.99e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 13 PGDRFreqTDPVLQLENINVSFDGfRAL-TDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK---------AL 82
Cdd:PRK11819 316 PGPRL---GDKVIEAENLSKSFGD-RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTikigetvklAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 83 YDQSVDltTLDPvaiarqgigrkfqKPTVFEAltVAENLALAMKGDKSVWAslRARIS------SEQDDRlnevlrllrl 156
Cdd:PRK11819 392 VDQSRD--ALDP-------------NKTVWEE--ISGGLDIIKVGNREIPS--RAYVGrfnfkgGDQQKK---------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 157 dgeryrqAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPaagmT---DAETeytaelFRTL-------AGqhSLMVVEHDMG 226
Cdd:PRK11819 443 -------VGVLSGGERNRLHLAKTLKQGGNVLLLDEP----TndlDVET------LRALeeallefPG--CAVVISHDRW 503
|
....*.
gi 490250284 227 FVETIA 232
Cdd:PRK11819 504 FLDRIA 509
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-213 |
6.02e-11 |
|
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: 59.95 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGF----RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGktRPQSGKALYDQSVDLTTLDPvAIA 98
Cdd:cd03232 2 SVLTWKNLNYTVPVKggkrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITGEILINGRPLDK-NFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQgIGRKFQKPTVFEALTVAENLALAmkgdksvwASLRArISSEQDDRLNevlrllrldgeryrqagllshgqkqfleIG 178
Cdd:cd03232 79 RS-TGYVEQQDVHSPNLTVREALRFS--------ALLRG-LSVEQRKRLT----------------------------IG 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 490250284 179 MLLVQEPHLLLLDEPAAGMtDAETEY-TAELFRTLA 213
Cdd:cd03232 121 VELAAKPSILFLDEPTSGL-DSQAAYnIVRFLKKLA 155
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-193 |
6.29e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvdlttldpvAIARQG-- 101
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE---------PIRRQRde 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 -------IGrkfQKPTVFEALTVAENLALAmkgdksvwaslrARISSEQD-DRLNEVLRLLRLDGERYRQAGLLSHGQKQ 173
Cdd:PRK13538 72 yhqdllyLG---HQPGIKTELTALENLRFY------------QRLHGPGDdEALWEALAQVGLAGFEDVPVRQLSAGQQR 136
|
170 180
....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEP 193
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEP 156
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-242 |
1.36e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.59 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSF---DG-FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKT----RPQSGKALYDqSVDLTTLDP 94
Cdd:PRK15093 2 PLLDIRNLTIEFktsDGwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFD-DIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 95 VAiARQGIGRK----FQKPTvfEALTVAENLALAMKGDKSVWaSLRARISSEQDDRLNEVLRLLRLDGERYRQAGL---- 166
Cdd:PRK15093 81 RE-RRKLVGHNvsmiFQEPQ--SCLDPSERVGRQLMQNIPGW-TYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMrsfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 167 --LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtdaETEYTAELFRTLA-----GQHSLMVVEHDMGFVETIADRVTVLH 239
Cdd:PRK15093 157 yeLTEGECQKVMIAIALANQPRLLIADEPTNAM---EPTTQAQIFRLLTrlnqnNNTTILLISHDLQMLSQWADKINVLY 233
|
...
gi 490250284 240 QGQ 242
Cdd:PRK15093 234 CGQ 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-215 |
1.38e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 50 GELRCVIGPNGAGKTTLMD---------VITGKTRPQSGKALyDQSvdlttldpvaIARQgIGRKFQKPTVFEALTVAEN 120
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNvlaervttgVITGGDRLVNGRPL-DSS----------FQRS-IGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 121 LALAmkgdksvwASLR--ARIS-SEQDDRLNEVLRLLRLdgERYRQA--GL----LSHGQKQFLEIGMLLVQEPHLLL-L 190
Cdd:TIGR00956 857 LRFS--------AYLRqpKSVSkSEKMEYVEEVIKLLEM--ESYADAvvGVpgegLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180
....*....|....*....|....*...
gi 490250284 191 DEPAAGMtDAETEY-TAELFRTLA--GQ 215
Cdd:TIGR00956 927 DEPTSGL-DSQTAWsICKLMRKLAdhGQ 953
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
39-254 |
2.35e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 39 ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-------------QSVDL------TTLDPvaiaR 99
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfgdysyrsQRIRMifqdpsTSLNP----R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFealtvaeNLALAmkgdksvwaslrariSSEQDDRLNEVLRL--LRLDGERYrQAGLLSHGQKQFLEI 177
Cdd:PRK15112 104 QRISQILDFPLRL-------NTDLE---------------PEQREKQIIETLRQvgLLPDHASY-YPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQA 254
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
40-246 |
2.78e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.32 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYdQSVDLTTLDPVAIA--RQGIGRKFQKP--TVFEAL 115
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRAQRKafRRDIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 116 TVAENLALAMKgdksvwaSLRARISSEQDDRLNEVLRLLRLDGERY-RQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEpa 194
Cdd:PRK10419 107 TVREIIREPLR-------HLLSLDKAERLARASEMLRAVDLDDSVLdKRPPQLSGGQLQRVCLARALAVEPKLLILDE-- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 195 aGMTDAETEYTAELFRTLAG-QHSL----MVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:PRK10419 178 -AVSNLDLVLQAGVIRLLKKlQQQFgtacLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
19-257 |
2.80e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 59.04 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 19 EQTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK-ALYDQSVDLTT------ 91
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEiRVGGEEIRLKPdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 92 --LDPVAIA--RQGIGRKFQKPTVFEALTVAENLALA----MKGDKSVwASLRARisseqddrlnevlRLLR---LDGER 160
Cdd:COG4598 83 vpADRRQLQriRTRLGMVFQSFNLWSHMTVLENVIEApvhvLGRPKAE-AIERAE-------------ALLAkvgLADKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 161 YRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPaagmTDA-ETEYTAE---LFRTLAGQHSLM-VVEHDMGFVETIADRV 235
Cdd:COG4598 149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEP----TSAlDPELVGEvlkVMRDLAEEGRTMlVVTHEMGFARDVSSHV 224
|
250 260
....*....|....*....|..
gi 490250284 236 TVLHQGQVLAEGSLREVQANEQ 257
Cdd:COG4598 225 VFLHQGRIEEQGPPAEVFGNPK 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-240 |
1.05e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDlttldpvaiarqgI 102
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR-------------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKptvfeaLTVAENLALamkgdkSVWASLRARISSEQDDRLNEvlrLLRLDGERYRQAGL--LSHGQKQFLEIGML 180
Cdd:PRK09544 70 GYVPQK------LYLDTTLPL------TVNRFLRLRPGTKKEDILPA---LKRVQAGHLIDAPMqkLSGGETQRVLLARA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 181 LVQEPHLLLLDEPAAGM----TDAETEYTAELFRTLagQHSLMVVEHDMGFVETIADRVTVLHQ 240
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVdvngQVALYDLIDQLRREL--DCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-259 |
1.26e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 14 GDRFREQTDPVLQLENinVSFDGFRAltDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTl 92
Cdd:PRK11288 247 GYRPRPLGEVRLRLDG--LKGPGLRE--PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgKPIDIRS- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 93 dPVAIARQGI-----GRKFQkpTVFEALTVAENLALAMKGDKSVWAS-LRARISSEQDDRLnevLRLLRLDGERYRQA-G 165
Cdd:PRK11288 322 -PRDAIRAGImlcpeDRKAE--GIIPVHSVADNINISARRHHLRAGClINNRWEAENADRF---IRSLNIKTPSREQLiM 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 166 LLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGM-TDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVL 244
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIdVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
250
....*....|....*
gi 490250284 245 AEgsLREVQANEQVI 259
Cdd:PRK11288 476 GE--LAREQATERQA 488
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-254 |
1.34e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA-LYDQSVDLTTLDpvaiARQ 100
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPVDAGDIA----TRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIGRKFQKPTVFEALTVAENLAlamkgdksvwasLRARI----SSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLE 176
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNLE------------LHARLfhlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 177 IGMLLVQEPHLLLLDEPAAGMT----DAETEYTAELFR----TLagqhslmvvehdmgFVET-------IADRVTVLHQG 241
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDpvarDMFWRLLIELSRedgvTI--------------FISThfmneaeRCDRISLMHAG 473
|
250
....*....|...
gi 490250284 242 QVLAEGSLREVQA 254
Cdd:NF033858 474 RVLASDTPAALVA 486
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
50-197 |
1.53e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 50 GELRCVIGPNGAGKTTLMDVITGKTRPQSgkaLYDQSVdltTLDPVAIARQGIGRK----FQKPTVFEALTVAENLA--- 122
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGV---KGSGSV---LLNGMPIDAKEMRAIsayvQQDDLFIPTLTVREHLMfqa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 123 -LAMKgdksvwaslRARISSEQDDRLNEVLRLLRLD-------GERYRQAGlLSHGQKQFLEIGMLLVQEPHLLLLDEPA 194
Cdd:TIGR00955 125 hLRMP---------RRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPT 194
|
...
gi 490250284 195 AGM 197
Cdd:TIGR00955 195 SGL 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-229 |
1.63e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK---------ALYDQSvdLTTLDP 94
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcgtklevAYFDQH--RAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 95 vaiarqgigrkfQKptvfealTVAENLAlamKGDKSVWASLRARisseqddrlnEVLRLLR---LDGERYRQ-AGLLSHG 170
Cdd:PRK11147 397 ------------EK-------TVMDNLA---EGKQEVMVNGRPR----------HVLGYLQdflFHPKRAMTpVKALSGG 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMtDAET-EYTAELfrtLAG-QHSLMVVEHDMGFVE 229
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDL-DVETlELLEEL---LDSyQGTVLLVSHDRQFVD 501
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-255 |
2.29e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 38 RALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYDQSVDLTTLDPVAIA--RQGIGRKFQKPtvFEAL 115
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGE-LYYQGQDLLKADPEAQKllRQKIQIVFQNP--YGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 116 ----TVAENLA--LAMKGDKSvwaslrariSSEQDDRLNEVLRLLRLDGERY-RQAGLLSHGQKQFLEIGMLLVQEPHLL 188
Cdd:PRK11308 106 nprkKVGQILEepLLINTSLS---------AAERREKALAMMAKVGLRPEHYdRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 189 LLDEPAAG------------MTDAETEY-TAELFrtlagqhslmvVEHDMGFVETIADRVTVLHQGQVLAEGSLREVQAN 255
Cdd:PRK11308 177 VADEPVSAldvsvqaqvlnlMMDLQQELgLSYVF-----------ISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-243 |
2.72e-09 |
|
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: 55.50 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSF--DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQGI 102
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID-GIDISTIPLEDL-RSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 GRKFQKPTVFEAlTVAENLalamkgdksvwaslraRISSEQDDRlnEVLRLLRLDGeryrqAGL-LSHGQKQFLEIGMLL 181
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNL----------------DPFDEYSDE--EIYGALRVSE-----GGLnLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 182 VQEPHLLLLDEPAAGM---TDAETEytaELFRTLAGQHSLMVVEHDMGfveTIA--DRVTVLHQGQV 243
Cdd:cd03369 141 LKRPRVLVLDEATASIdyaTDALIQ---KTIREEFTNSTILTIAHRLR---TIIdyDKILVMDAGEV 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-257 |
3.17e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 19 EQTDPVLQLENINVSFD-------------GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYdQ 85
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 86 SVDLTTLDPVAI--ARQGIGRKFQKP--TVFEALTVAENLALAMKgdksvwaSLRARISSEQ-DDRLNEVLR---LLRLD 157
Cdd:PRK15079 82 GKDLLGMKDDEWraVRSDIQMIFQDPlaSLNPRMTIGEIIAEPLR-------TYHPKLSRQEvKDRVKAMMLkvgLLPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 158 GERYRQAglLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRV 235
Cdd:PRK15079 155 INRYPHE--FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRV 232
|
250 260
....*....|....*....|..
gi 490250284 236 TVLHQGQVLAEGSLREVQANEQ 257
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHNPL 254
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-262 |
3.32e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDV----ITGKTRPQSGKALYDQSVD---LTTLDPVA 96
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRGARVTGDVTLNgepLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 97 IARqgigrkfqkptVFEALTVAENLALAMKGDKSVWASL--RARISSEQDDRLNEV----LRLLRLDGERYRQAGLLSHG 170
Cdd:PRK13547 81 LAR-----------LRAVLPQAAQPAFAFSAREIVLLGRypHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 171 QKQFLEIGMLLVQ---------EPHLLLLDEPAAGMTDAETEYTAELFRTLAGQHSLMV--VEHDMGFVETIADRVTVLH 239
Cdd:PRK13547 150 ELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVlaIVHDPNLAARHADRIAMLA 229
|
250 260
....*....|....*....|...
gi 490250284 240 QGQVLAEGSLREVQANEQVIEVY 262
Cdd:PRK13547 230 DGAIVAHGAPADVLTPAHIARCY 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-259 |
4.27e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 18 REQTDPVLQLENInVSFDgFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKaLYDQSVDLTTLDPVAI 97
Cdd:PRK09700 259 NLAHETVFEVRNV-TSRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE-IRLNGKDISPRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 ARQGIG---RKFQKPTVFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLR-LLRLDGERYRQ-AGLLSHGQK 172
Cdd:PRK09700 336 VKKGMAyitESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQReLLALKCHSVNQnITELSGGNQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 173 QFLEIGMLLVQEPHLLLLDEPAAGM-TDAETE-YTaeLFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSL 249
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIdVGAKAEiYK--VMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQILTN 493
|
250
....*....|
gi 490250284 250 REVQANEQVI 259
Cdd:PRK09700 494 RDDMSEEEIM 503
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-242 |
4.81e-09 |
|
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: 54.78 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFD-----GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTldpvaiar 99
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 qgigrkfQKPTVFEAlTVAENLALAMKGDKsvwaslrarisseqdDRLNEVLRL--LRLD------------GERyrqaG 165
Cdd:cd03250 73 -------QEPWIQNG-TIRENILFGKPFDE---------------ERYEKVIKAcaLEPDleilpdgdlteiGEK----G 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 166 L-LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEytAELFRTLAGQHsLM------VVEHDMGFVEtIADRVTVL 238
Cdd:cd03250 126 InLSGGQKQRISLARAVYSDADIYLLDDPLSAV-DAHVG--RHIFENCILGL-LLnnktriLVTHQLQLLP-HADQIVVL 200
|
....
gi 490250284 239 HQGQ 242
Cdd:cd03250 201 DNGR 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-263 |
9.30e-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: 55.60 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENI---NVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVAIA 98
Cdd:TIGR02633 255 DVILEARNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGIG-----RKfqKPTVFEALTVAENLALAMKgdKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQ 173
Cdd:TIGR02633 335 RAGIAmvpedRK--RHGIVPILGVGKNITLSVL--KSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLHQGQVLAEgSLREV 252
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGLSDRVLVIGEGKLKGD-FVNHA 489
|
250
....*....|.
gi 490250284 253 QANEQVIEVYL 263
Cdd:TIGR02633 490 LTQEQVLAAAL 500
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
39-247 |
1.05e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.49 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 39 ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYdQSVDLTTLDPVAIaRQGIGRKFQKPTVFEAlTVA 118
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSW-RSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 119 ENLALAMKGDKSVWASLRARISSEQDDrlnevlrLLRLD-------GERyrqAGLLSHGQKQFLEIGMLLVQEPHLLLLD 191
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVARLASVHDD-------ILRLPqgydtevGER---GVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 192 EpAAGMTDAETEYtaELFRTLA--GQH-SLMVVEHDMGFVeTIADRVTVLHQGQVLAEG 247
Cdd:PRK10789 477 D-ALSAVDGRTEH--QILHNLRqwGEGrTVIISAHRLSAL-TEASEILVMQHGHIAQRG 531
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-246 |
1.31e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqsVDLTTLDPVAIARQGIG 103
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPDNQFGREASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAenlalamkgdksvwaslrarisseqddRLNEVLRLLRldgeRYRQaglLSHGQKQFLEIGMLLVQ 183
Cdd:COG2401 108 RKGDFKDAVELLNAV---------------------------GLSDAVLWLR----RFKE---LSTGQKFRFRLALLLAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 184 EPHLLLLDEPAAGMtDAETEY-TAELFRTLAGQH--SLMVVEHDMGFVETIA-DRVTVLHQGQVLAE 246
Cdd:COG2401 154 RPKLLVIDEFCSHL-DRQTAKrVARNLQKLARRAgiTLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-256 |
1.68e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 16 RFREQTDPVLQleninvsfdgfraltDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPV 95
Cdd:PLN03232 1243 RYRPGLPPVLH---------------GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMID-DCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIaRQGIGRKFQKPTVFEAlTVAENL-ALAMKGDKSVWASL-RARISSEQDDRLnevlrlLRLDGERYRQAGLLSHGQKQ 173
Cdd:PLN03232 1307 DL-RRVLSIIPQSPVLFSG-TVRFNIdPFSEHNDADLWEALeRAHIKDVIDRNP------FGLDAEVSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGM---TDAETEYTA-ELFRTLagqhSLMVVEHDMgfvETI--ADRVTVLHQGQVLAEG 247
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVdvrTDSLIQRTIrEEFKSC----TMLVIAHRL---NTIidCDKILVLSSGQVLEYD 1451
|
....*....
gi 490250284 248 SLREVQANE 256
Cdd:PLN03232 1452 SPQELLSRD 1460
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
50-239 |
3.16e-08 |
|
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: 53.14 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 50 GELRCVIGPNGAGKTTLMDVITGKTRPQSGKalYDQSVDLTTldpvaIARQGIGRKFQKptVFEALtVAENLALAMKGD- 128
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDE-----ILDEFRGSELQN--YFTKL-LEGDVKVIVKPQy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 129 -----KSVWASLRArISSEQDDR--LNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAE 201
Cdd:cd03236 96 vdlipKAVKGKVGE-LLKKKDERgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 490250284 202 TEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLH 239
Cdd:cd03236 175 RLNAARLIRELAEDdNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-193 |
3.30e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 27 LENINVSFDGFRA--LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDlttlDPVAIARQGIG 103
Cdd:PRK13540 2 LDVIELDFDYHDQplLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErQSIK----KDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 104 RKFQKPTVFEALTVAENLALAMKgdksvwaslrariSSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQ 183
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIH-------------FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMS 144
|
170
....*....|
gi 490250284 184 EPHLLLLDEP 193
Cdd:PRK13540 145 KAKLWLLDEP 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-232 |
3.39e-08 |
|
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: 53.79 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDlttldpvaiarqgIGRKFQKPTVFEALTVAE 119
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK-------------VGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 120 NLALAMKGDKSVWA---SLRARISSEQDD---------RLNEVL----------RL------LRL-DGEryRQAGLLSHG 170
Cdd:TIGR03719 88 NVEEGVAEIKDALDrfnEISAKYAEPDADfdklaaeqaELQEIIdaadawdldsQLeiamdaLRCpPWD--ADVTKLSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 171 QKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETeyTAELFRTLAG-QHSLMVVEHDMGFVETIA 232
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHL-DAES--VAWLERHLQEyPGTVVAVTHDRYFLDNVA 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-212 |
3.69e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.66 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 9 TRQLPGDRFREQTDPVLQLENINVSFDGFRAL-TDLSLAIGVGElRCVI-GPNGAGKTTLMDVI-------TGK-TRPQS 78
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRTPDGRPLlEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIaglwpygSGRiARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 79 GKALYdqsvdLttldPvaiarqgigrkfQKP-----TVFEALTvaenlalamkgdksvWASLRARISseqDDRLNEVLRL 153
Cdd:COG4178 426 ARVLF-----L----P------------QRPylplgTLREALL---------------YPATAEAFS---DAELREALEA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 154 LRLD------GERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEytAELFRTL 212
Cdd:COG4178 467 VGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL-DEENE--AALYQLL 528
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-197 |
4.40e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 2 QPDEGLFTRQLPGDrfreqtDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKtRPQSgka 81
Cdd:PRK10938 244 EPDEPSARHALPAN------EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQG--- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 82 lYdqSVDLTTLDpvaiARQGIGRkfqkpTVFEALT----VAENLALamkgDKSVWASLRARI--------------SSEQ 143
Cdd:PRK10938 314 -Y--SNDLTLFG----RRRGSGE-----TIWDIKKhigyVSSSLHL----DYRVSTSVRNVIlsgffdsigiyqavSDRQ 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490250284 144 DDRLNEVLRLLRLDGeryRQAGL----LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGM 197
Cdd:PRK10938 378 QKLAQQWLDILGIDK---RTADApfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGL 432
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-246 |
6.04e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINV-SFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIARQ 100
Cdd:COG3845 255 EVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD-GEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GIG-----RkfQKPTVFEALTVAENLAL--AMKGDKSVWASLRARISSEQDDRLNEVLRlLRLDGERYRqAGLLSHGQKQ 173
Cdd:COG3845 334 GVAyipedR--LGRGLVPDMSVAENLILgrYRRPPFSRGGFLDRKAIRAFAEELIEEFD-VRTPGPDTP-ARSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETIADRVTVLHQGQVLAE 246
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-252 |
6.59e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDgfRALT-DLSLAIGVGELRCVIGPNGAGKT----TLMDVITGKTRPQSGKALydqsvdlttLDPVAIA 98
Cdd:PRK10418 4 QIELRNIALQAA--QPLVhGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVL---------LDGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 99 RQGI-GRKFQkpTVFEALTVAENLALAMKGDKSvwASLRARISSEQDDRLNEVLRLLRLDgERYRQAGL----LSHGQKQ 173
Cdd:PRK10418 73 PCALrGRKIA--TIMQNPRSAFNPLHTMHTHAR--ETCLALGKPADDATLTAALEAVGLE-NAARVLKLypfeMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAagmTDAETEYTA---ELFRTLAGQHSL--MVVEHDMGFVETIADRVTVLHQGQVLAEGS 248
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPT---TDLDVVAQArilDLLESIVQKRALgmLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
....
gi 490250284 249 LREV 252
Cdd:PRK10418 225 VETL 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-256 |
7.57e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 16 RFREQTDPVLQleninvsfdgfraltDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDpV 95
Cdd:PLN03130 1246 RYRPELPPVLH---------------GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILID-GCDISKFG-L 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIARQGIGRKFQKPTVFEAlTVAENL-ALAMKGDKSVWASL-RARisseqddrLNEVLRL--LRLDGERYRQAGLLSHGQ 171
Cdd:PLN03130 1309 MDLRKVLGIIPQAPVLFSG-TVRFNLdPFNEHNDADLWESLeRAH--------LKDVIRRnsLGLDAEVSEAGENFSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 172 KQFLEIGMLLVQEPHLLLLDEPAAGM---TDAETEYTA-ELFRTLagqhSLMVVEHDMgfvETI--ADRVTVLHQGQVLA 245
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVdvrTDALIQKTIrEEFKSC----TMLIIAHRL---NTIidCDRILVLDAGRVVE 1452
|
250
....*....|.
gi 490250284 246 EGSLREVQANE 256
Cdd:PLN03130 1453 FDTPENLLSNE 1463
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-254 |
1.00e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 4 DEG---LFTRQLPGDRFREQTDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK 80
Cdd:TIGR01271 403 DEGigeLFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 81 ALYDQSVDLTTldpvaiarqgigrkfQKPTVFEAlTVAENLALAMKGDKSVWASLRARISSEQDdrlneVLRLLRLDGER 160
Cdd:TIGR01271 483 IKHSGRISFSP---------------QTSWIMPG-TIKDNIIFGLSYDEYRYTSVIKACQLEED-----IALFPEKDKTV 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 161 YRQAGL-LSHGQKQFLEIGMLLVQEPHLLLLDEPaAGMTDAETEytAELFRT----LAGQHSLMVVEHDMGFVETiADRV 235
Cdd:TIGR01271 542 LGEGGItLSGGQRARISLARAVYKDADLYLLDSP-FTHLDVVTE--KEIFESclckLMSNKTRILVTSKLEHLKK-ADKI 617
|
250
....*....|....*....
gi 490250284 236 TVLHQGQVLAEGSLREVQA 254
Cdd:TIGR01271 618 LLLHEGVCYFYGTFSELQA 636
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
31-253 |
1.10e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.78 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 31 NVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTldPVAIARQGigrkfqkpt 110
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--QFSWIMPG--------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 111 vfealTVAENLALAMKGDKSVWASLRARISSEQDdrlneVLRLLRLDGERYRQAGL-LSHGQKQFLEIGMLLVQEPHLLL 189
Cdd:cd03291 113 -----TIKENIIFGVSYDEYRYKSVVKACQLEED-----ITKFPEKDNTVLGEGGItLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490250284 190 LDEPaAGMTDAETEytAELF-----RTLAGQHSLMV---VEHdmgfvETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:cd03291 183 LDSP-FGYLDVFTE--KEIFescvcKLMANKTRILVtskMEH-----LKKADKILILHEGSSYFYGTFSELQ 246
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-252 |
1.84e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 24 VLQLENINVSFDG----FRALTDLSLAIGVGELRCVIGPNGAGKT----TLMDVITGKTRPQSGKALYDQSvDLTTLDPV 95
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQ-DLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AiARQGIGRK----FQKP--TVFEALTVAENLALAMKGDKSvwASLRARIsseqdDRLNEVLRLL-------RLDGERYR 162
Cdd:PRK11022 82 E-RRNLVGAEvamiFQDPmtSLNPCYTVGFQIMEAIKVHQG--GNKKTRR-----QRAIDLLNQVgipdpasRLDVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 163 qaglLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQ 240
Cdd:PRK11022 154 ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAAHKIIVMYA 229
|
250
....*....|..
gi 490250284 241 GQVLAEGSLREV 252
Cdd:PRK11022 230 GQVVETGKAHDI 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-264 |
2.30e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 18 REQTDP---VLQLENINVsFD----GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITG--KTRPQSGKALYDQSVD 88
Cdd:PRK13549 250 REPHTIgevILEVRNLTA-WDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGayPGRWEGEIFIDGKPVK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 89 LTTldPVAIARQGIG-----RKfqKPTVFEALTVAENLALAMKGDKSVWASLRAriSSEQDDRLNEVLRLlRLDGERYRQ 163
Cdd:PRK13549 329 IRN--PQQAIAQGIAmvpedRK--RDGIVPVMGVGKNITLAALDRFTGGSRIDD--AAELKTILESIQRL-KVKTASPEL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 164 A-GLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETEYtaELFR---TLAGQH-SLMVVEHDMGFVETIADRVTVL 238
Cdd:PRK13549 402 AiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI-DVGAKY--EIYKlinQLVQQGvAIIVISSELPEVLGLSDRVLVM 478
|
250 260
....*....|....*....|....*.
gi 490250284 239 HQGQVLAEgSLREVQANEQVIEVYLG 264
Cdd:PRK13549 479 HEGKLKGD-LINHNLTQEQVMEAALR 503
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-252 |
3.62e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 27 LENINVSFDGfraLTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSvDLTTLDPVAIARQGI---- 102
Cdd:PRK10762 258 LKVDNLSGPG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH-EVVTRSPQDGLANGIvyis 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 103 -GRKfqKPTVFEALTVAENLAL-AMKGDKSVWASLRarisseQDDRLNEVLRLLRL----DGERYRQAGLLSHGQKQFLE 176
Cdd:PRK10762 334 eDRK--RDGLVLGMSVKENMSLtALRYFSRAGGSLK------HADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 177 IGMLLVQEPHLLLLDEPAAGM-TDAETEYTAELFRTLAGQHSLMVVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVdVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-252 |
4.08e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 18 REQTDPVLQLENINVSF---DG-FRALTDLSLAIGVGELRCVIGPNGAGKT----TLMDVITGKTRpQSGKALYD--QSV 87
Cdd:PRK09473 6 QQQADALLDVKDLRVTFstpDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNgrEIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 88 DLTTLDPVAIARQGIGRKFQKPT--------VFEALTvaENLALAMKGDKSvwaslrarisseqdDRLNEVLRLLrlDG- 158
Cdd:PRK09473 85 NLPEKELNKLRAEQISMIFQDPMtslnpymrVGEQLM--EVLMLHKGMSKA--------------EAFEESVRML--DAv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 159 ---ERYRQAGLLSH----GQKQFLEIGMLLVQEPHLLLLDEP---------AAGMTdaeteYTAEL---FRTlagqhSLM 219
Cdd:PRK09473 147 kmpEARKRMKMYPHefsgGMRQRVMIAMALLCRPKLLIADEPttaldvtvqAQIMT-----LLNELkreFNT-----AII 216
|
250 260 270
....*....|....*....|....*....|...
gi 490250284 220 VVEHDMGFVETIADRVTVLHQGQVLAEGSLREV 252
Cdd:PRK09473 217 MITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
36-197 |
4.28e-07 |
|
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: 49.25 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 36 GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSV--DLTTLDPVAIARQGIGRKFQKPTVFE 113
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 114 AlTVAENLALAMKGDKSVWASLRARISSEQDDRLnevlrLLRLDGERYRQAGL-LSHGQKQFLEIGMLLVQEPHLLLLDE 192
Cdd:cd03290 93 A-TVEENITFGSPFNKQRYKAVTDACSLQPDIDL-----LPFGDQTEIGERGInLSGGQRQRICVARALYQNTNIVFLDD 166
|
....*
gi 490250284 193 PAAGM 197
Cdd:cd03290 167 PFSAL 171
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-258 |
5.08e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSF----DGFrALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDqSVDLTTLDPVAIaRQG 101
Cdd:PRK10522 322 TLELRNVTFayqdNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD-GKPVTAEQPEDY-RKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRKFQKPTVFEALTVAENLAlamKGDKSVWASLrarisseqdDRLnEVLRLLRLDGERYRQAGlLSHGQKQFLEIGMLL 181
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPEGKP---ANPALVEKWL---------ERL-KMAHKLELEDGRISNLK-LSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 182 VQEPHLLLLDEPAAgmtDAETEYTAELFRTL-----AGQHSLMVVEHDMGFVETiADRVTVLHQGQvLAE--GSLREVQA 254
Cdd:PRK10522 465 AEERDILLLDEWAA---DQDPHFRREFYQVLlpllqEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ-LSEltGEERDAAS 539
|
....
gi 490250284 255 NEQV 258
Cdd:PRK10522 540 RDAV 543
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-200 |
7.01e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGktRPQSGKALYDQSVDLTTLDPVAIAR------ 99
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFARisgyce 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGigrKFQKPTVfealTVAENLALamkgdkSVWASLRARISSEQDDR-LNEVLRLLRLDGERYRQAGL-----LSHGQKQ 173
Cdd:PLN03140 960 QN---DIHSPQV----TVRESLIY------SAFLRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRK 1026
|
170 180
....*....|....*....|....*..
gi 490250284 174 FLEIGMLLVQEPHLLLLDEPAAGMtDA 200
Cdd:PLN03140 1027 RLTIAVELVANPSIIFMDEPTSGL-DA 1052
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
55-238 |
1.24e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 55 VIGPNGAGKTTLMDVITGKTRPQ-----------------SGKALYDQSVDLttldpvaiaRQGIGRKFQKPTVFEALtv 117
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQNYFKKL---------YNGEIKVVHKPQYVDLI-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 118 aenlALAMKGdkSVWASLRarissEQDDR--LNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPaa 195
Cdd:PRK13409 173 ----PKVFKG--KVRELLK-----KVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP-- 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490250284 196 gmtdaeTEY--------TAELFRTLAGQHSLMVVEHDMGFVETIADRVTVL 238
Cdd:PRK13409 240 ------TSYldirqrlnVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-255 |
1.56e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 23 PVLQLENINVSFDGFRA---LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSgkalyDQSVDLttldpvaiaR 99
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-----TSSVVI---------R 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 100 QGIGRKFQKPTVFEAlTVAENLALAMKGDKS-VWASLRAriSSEQDDRLNEVLRLLRLDGERyrqaGL-LSHGQKQFLEI 177
Cdd:PLN03232 679 GSVAYVPQVSWIFNA-TVRENILFGSDFESErYWRAIDV--TALQHDLDLLPGRDLTEIGER----GVnISGGQKQRVSM 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 178 GMLLVQEPHLLLLDEPAAGMtDAETEYtaELFRT-----LAGQHSLMVVeHDMGFVETIaDRVTVLHQGQVLAEGSLREV 252
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSAL-DAHVAH--QVFDScmkdeLKGKTRVLVT-NQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
...
gi 490250284 253 QAN 255
Cdd:PLN03232 827 SKS 829
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
26-195 |
2.04e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.07 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 26 QLENINVSfdGFRALTDLSLAIGvGELRCVIGPNGAGKTTLMDVIT-------------------GKTRPQSG------- 79
Cdd:COG3593 2 KLEKIKIK--NFRSIKDLSIELS-DDLTVLVGENNSGKSSILEALRlllgpsssrkfdeedfylgDDPDLPEIeieltfg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 80 ---KALYDQSVDLTTLDPVAIARQGIGRKFQKptVFEALT--VAENLALAMKGdksvwASLRARISSEQDDRLNEVLRLL 154
Cdd:COG3593 79 sllSRLLRLLLKEEDKEELEEALEELNEELKE--ALKALNelLSEYLKELLDG-----LDLELELSLDELEDLLKSLSLR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490250284 155 RLDGERYRQAgLLSHGQKQFLEIGMLLV-------QEPHLLLLDEPAA 195
Cdd:COG3593 152 IEDGKELPLD-RLGSGFQRLILLALLSAlaelkraPANPILLIEEPEA 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-243 |
2.04e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKalydqsvdlttldpVAIARqG 101
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE--------------IGLAK-G 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IgrkfqKPTVFealtvAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQA-GLLSHGQKQFLEIGML 180
Cdd:PRK10636 375 I-----KLGYF-----AQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALI 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490250284 181 LVQEPHLLLLDEPA----AGMTDAETEYTAELfrtlagQHSLMVVEHDMGFVETIADRVTVLHQGQV 243
Cdd:PRK10636 445 VWQRPNLLLLDEPTnhldLDMRQALTEALIDF------EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
242-265 |
3.54e-06 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 42.62 E-value: 3.54e-06
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-224 |
7.37e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKA-LYDQSvdLTTLDPVAIAR---QGIGRKFQKPTVFEAL 115
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQP--LHQMDEEARAKlraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 116 TVAENLALAmkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAA 195
Cdd:PRK10584 104 NALENVELP--------ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 490250284 196 GMTDAETEYTAELFRTLAGQH--SLMVVEHD 224
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHgtTLILVTHD 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-195 |
9.09e-06 |
|
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: 46.83 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 35 DGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITgktRPQSGKAlyDQSVDLTTLDPVAIA--RQGIGRKFQKPTVF 112
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL---RLLSTEG--EIQIDGVSWNSVTLQtwRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 113 EAlTVAENL-ALAMKGDKSVW-----ASLRARIssEQ-DDRLNEVLrllrLDGeryrqAGLLSHGQKQFLEIGMLLVQEP 185
Cdd:TIGR01271 1305 SG-TFRKNLdPYEQWSDEEIWkvaeeVGLKSVI--EQfPDKLDFVL----VDG-----GYVLSNGHKQLMCLARSILSKA 1372
|
170
....*....|
gi 490250284 186 HLLLLDEPAA 195
Cdd:TIGR01271 1373 KILLLDEPSA 1382
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-243 |
1.28e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSF----DGFRALTDLSLAIGVGELRCVIGPNGAGKT-TLMDVITGKTRPQ----SGKALYD-QSV--- 87
Cdd:PRK15134 2 TQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHgESLlha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 88 DLTTLDPVAIARqgIGRKFQKPTVfeALTVAENLalamkgDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAGL- 166
Cdd:PRK15134 82 SEQTLRGVRGNK--IAMIFQEPMV--SLNPLHTL------EKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 167 -----LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ--HSLMVVEHDMGFVETIADRVTVLH 239
Cdd:PRK15134 152 dyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLADRVAVMQ 231
|
....
gi 490250284 240 QGQV 243
Cdd:PRK15134 232 NGRC 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-251 |
1.28e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.17 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENINVSFDG--FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD----QSVDLTTL-DPVAI 97
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASLrNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 98 ARQGIgrkfqkpTVFEAlTVAENLALAMKGDKSvwaslRARIS------------SEQDDRLNEVLrllrldGEryrQAG 165
Cdd:PRK11176 422 VSQNV-------HLFND-TIANNIAYARTEQYS-----REQIEeaarmayamdfiNKMDNGLDTVI------GE---NGV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 166 LLSHGQKQFLEIGMLLVQEPHLLLLDEpAAGMTDAETEYTAEL-FRTLAGQHSLMVVEHDMGFVETiADRVTVLHQGQVL 244
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDE-ATSALDTESERAIQAaLDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
....*..
gi 490250284 245 AEGSLRE 251
Cdd:PRK11176 558 ERGTHAE 564
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
55-239 |
1.68e-05 |
|
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: 45.55 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 55 VIGPNGAGKTTLMDVITGKTRPQ-----------------SGKALYD----------------QSVDLttldpvaiarqg 101
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELQDyfkklangeikvahkpQYVDL------------ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 102 IGRKFqKPTVFEALTVAenlalamkgdksvwaslrarisseqDDR--LNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGM 179
Cdd:COG1245 172 IPKVF-KGTVRELLEKV-------------------------DERgkLDELAEKLGLENILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490250284 180 LLVQEPHLLLLDEPaagmtdaeTEY--------TAELFRTLAGQH-SLMVVEHDMGFVETIADRVTVLH 239
Cdd:COG1245 226 ALLRDADFYFFDEP--------SSYldiyqrlnVARLIRELAEEGkYVLVVEHDLAILDYLADYVHILY 286
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
162-257 |
2.56e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 162 RQAGLLSHGQKQFL----EIGMLLVQEphLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMgfvETI--ADR 234
Cdd:TIGR00630 484 RAAGTLSGGEAQRIrlatQIGSGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRLRDLgNTLIVVEHDE---DTIraADY 558
|
90 100
....*....|....*....|....*....
gi 490250284 235 VTVL------HQGQVLAEGSLREVQANEQ 257
Cdd:TIGR00630 559 VIDIgpgageHGGEVVASGTPEEILANPD 587
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
146-253 |
2.58e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 146 RLNEVLRLLRLDGERYRQAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAET--EYTAELFRTLAGQHSLMVVEH 223
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL-DPRTrnEVWDEVRSMVRDGATVLLTTQ 202
|
90 100 110
....*....|....*....|....*....|
gi 490250284 224 DMGFVETIADRVTVLHQGQVLAEGSLREVQ 253
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
32-70 |
1.28e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.28e-04
10 20 30
....*....|....*....|....*....|....*....
gi 490250284 32 VSFDGFRALTDLSLAIGvgELRCVIGPNGAGKTTLMDVI 70
Cdd:COG4637 5 IRIKNFKSLRDLELPLG--PLTVLIGANGSGKSNLLDAL 41
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-248 |
1.40e-04 |
|
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: 43.01 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 16 RFREQTDPVLQleninvsfdgfraltDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALydqsvdlttLDPV 95
Cdd:TIGR00957 1293 RYREDLDLVLR---------------HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII---------IDGL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 96 AIARQGI-GRKF------QKPTVFEAlTVAENL-ALAMKGDKSVW-----ASLRARISSEQDdrlnevlrllRLDGERYR 162
Cdd:TIGR00957 1349 NIAKIGLhDLRFkitiipQDPVLFSG-SLRMNLdPFSQYSDEEVWwalelAHLKTFVSALPD----------KLDHECAE 1417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 163 QAGLLSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMtDAETE-YTAELFRTLAGQHSLMVVEHDMgfvETIAD--RVTVLH 239
Cdd:TIGR00957 1418 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAV-DLETDnLIQSTIRTQFEDCTVLTIAHRL---NTIMDytRVIVLD 1493
|
....*....
gi 490250284 240 QGQVLAEGS 248
Cdd:TIGR00957 1494 KGEVAEFGA 1502
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
43-93 |
1.54e-04 |
|
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: 42.48 E-value: 1.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 490250284 43 LSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDLTTLD 93
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDgQPVTADNRE 402
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-257 |
1.76e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 22 DPVLQLENINVSFD-----------GFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYD-QSVDL 89
Cdd:PRK10261 311 EPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 90 TTLDPVAIARQGIGRKFQKPtvFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGERYRQAglLSH 169
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDP--YASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE--FSG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 170 GQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQH--SLMVVEHDMGFVETIADRVTVLHQGQVLAEG 247
Cdd:PRK10261 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
250
....*....|
gi 490250284 248 SLREVQANEQ 257
Cdd:PRK10261 547 PRRAVFENPQ 556
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
40-247 |
1.87e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLAIGVGELRCVIGPNGAGKTTL-MDVITGKTRPQsgkalYDQSVDlttldpvAIARQGIGRKfQKPTVfealTVA 118
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAEGQRR-----YVESLS-------AYARQFLGQM-DKPDV----DSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 119 ENLALAMKGD-KSVWASLRARISSEQDdrLNEVLRLL--------RLD-----GERY----RQAGLLSHGQKQFL----E 176
Cdd:cd03270 74 EGLSPAIAIDqKTTSRNPRSTVGTVTE--IYDYLRLLfarvgireRLGflvdvGLGYltlsRSAPTLSGGEAQRIrlatQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 177 IGMLLVQEphLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMgfvETI--ADRVTVL------HQGQVLAEG 247
Cdd:cd03270 152 IGSGLTGV--LYVLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDE---DTIraADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
162-247 |
2.20e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 162 RQAGLLSHGQKQFLEIGMLLVQEPH--LLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETiADRV--- 235
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLgNTVILIEHNLDVLSS-ADWIidf 161
|
90
....*....|....*
gi 490250284 236 ---TVLHQGQVLAEG 247
Cdd:cd03238 162 gpgSGKSGGKVVFSG 176
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-197 |
2.89e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.99 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 21 TDPVLQLENINVSFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGKALYDQSVDLTTLDPVAIARQ 100
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 101 GigrkfQKPTVFEALTVAENLALAmkgdksvwASLRARISSEQDDRLNEVLRLLRLDGERYRQaglLSHGQKQFLEIGML 180
Cdd:PRK13543 88 G-----HLPGLKADLSTLENLHFL--------CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ---LSAGQKKRLALARL 151
|
170
....*....|....*..
gi 490250284 181 LVQEPHLLLLDEPAAGM 197
Cdd:PRK13543 152 WLSPAPLWLLDEPYANL 168
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
39-80 |
3.10e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 3.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490250284 39 ALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK 80
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-202 |
4.39e-04 |
|
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: 40.32 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 34 FDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQ---SGKALYDqsvdlttldpvAIARQGIGRKFQKPT 110
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYN-----------GIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 111 VFEA--------LTVAENL--ALAMKGdksvwaslrarisseqddrlNEVLRllrldGeryrqaglLSHGQKQFLEIGML 180
Cdd:cd03233 86 IYVSeedvhfptLTVRETLdfALRCKG--------------------NEFVR-----G--------ISGGERKRVSIAEA 132
|
170 180
....*....|....*....|..
gi 490250284 181 LVQEPHLLLLDEPAAGMtDAET 202
Cdd:cd03233 133 LVSRASVLCWDNSTRGL-DSST 153
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
167-265 |
4.82e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 167 LSHGQKQFLEIGMLLV---QEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVETiADRVTVL---- 238
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLgHSVIYIDHDPALLKQ-ADYLIEMgpgs 1778
|
90 100 110
....*....|....*....|....*....|
gi 490250284 239 --HQGQVLAEGSLREVQANEQ-VIEVYLGR 265
Cdd:PRK00635 1779 gkTGGKILFSGPPKDISASKDsLLKTYMCN 1808
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
32-80 |
6.18e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 6.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490250284 32 VSFDGFRALTDLSLAIGVGeLRCVIGPNGAGKTTLMD----VITGKTRPQSGK 80
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDaiklALYGKTSRLKRK 52
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-202 |
6.48e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 40 LTDLSLA------IGVgelrcvIGPNGAGKTTLMDVITGKTRPQSGKalydqsvdlttldpvAIARQG--IGRKFQKPTV 111
Cdd:PRK11819 23 LKDISLSffpgakIGV------LGLNGAGKSTLLRIMAGVDKEFEGE---------------ARPAPGikVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 112 FEALTVAENLALAMkgdksvwASLRARIsseqdDRLNEVLRLLRLDGERY-----RQAGL-------------------- 166
Cdd:PRK11819 82 DPEKTVRENVEEGV-------AEVKAAL-----DRFNEIYAAYAEPDADFdalaaEQGELqeiidaadawdldsqleiam 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490250284 167 --------------LSHGQKQFLEIGMLLVQEPHLLLLDEPaagmT---DAET 202
Cdd:PRK11819 150 dalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEP----TnhlDAES 198
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
167-239 |
7.61e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 7.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490250284 167 LSHGQKQFLEIGMLLVQEPHLLLLDEPAAGMTDAETEYTAELFRTLA--GQHSLMVVEHDMGFVETIADRVTVLH 239
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
25-224 |
1.53e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 25 LQLENinvsFDGFRALTDLSLAIGvgeLRCVIGPNGAGKTTLMDVIT----GKTRpqSGKALYDQSVDLTTLDP------ 94
Cdd:COG0419 5 LRLEN----FRSYRDTETIDFDDG---LNLIVGPNGAGKSTILEAIRyalyGKAR--SRSKLRSDLINVGSEEAsvelef 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 95 -------VAIARQGIGRKFQKPT------VFEALTVAENLALAMKGDKSVWASLRARISSEQDDRLNEVLRLLRLDGerY 161
Cdd:COG0419 76 ehggkryRIERRQGEFAEFLEAKpserkeALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSG--L 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490250284 162 RQAGLLSHGQKQFLEIGMLLVqephlLLLDEpaaGMTDAETeyTAELFRTLagqHSLMVVEHD 224
Cdd:COG0419 154 DPIETLSGGERLRLALADLLS-----LILDF---GSLDEER--LERLLDAL---EELAIITHV 203
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
54-70 |
1.80e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 38.71 E-value: 1.80e-03
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-254 |
1.94e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 37 FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKT----RPQSGKALYDqsvdltTLDPVAIARQGIGRKF---QKP 109
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYD------GITPEEIKKHYRGDVVynaETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 110 TVFEALTVAENL--ALAMKG--------DKSVWASLRARIsseqddrlneVLRLLRLDGERYRQAGL-----LSHGQKQF 174
Cdd:TIGR00956 148 VHFPHLTVGETLdfAARCKTpqnrpdgvSREEYAKHIADV----------YMATYGLSHTRNTKVGNdfvrgVSGGERKR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490250284 175 LEIGMLLVQEPHLLLLDEPAAGMtDAETEYtaELFRTLAGQHSLMvveHDMGFVeTIA----------DRVTVLHQGQVL 244
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGL-DSATAL--EFIRALKTSANIL---DTTPLV-AIYqcsqdayelfDKVIVLYEGYQI 290
|
250
....*....|
gi 490250284 245 AEGSLREVQA 254
Cdd:TIGR00956 291 YFGPADKAKQ 300
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
37-80 |
2.25e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 2.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 490250284 37 FRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITGKTRPQSGK 80
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
167-238 |
2.36e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 2.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490250284 167 LSHGQKQFLEIGMLL---VQEPHLLLLDEPAAGMTDAETEYTAELFRTLAGQ-HSLMVVEHDMGFVEtIADRVTVL 238
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQgHTVVIIEHNMHVVK-VADYVLEL 884
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-72 |
3.86e-03 |
|
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: 37.13 E-value: 3.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490250284 25 LQLENINV-SFDGFRALTDLSLAIGVGELRCVIGPNGAGKTTLMDVITG 72
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
32-70 |
5.10e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 5.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490250284 32 VSFDGFRALTDLSLAIGVGELRCVI-GPNGAGKTTLMDVI 70
Cdd:COG3950 6 LTIENFRGFEDLEIDFDNPPRLTVLvGENGSGKTTLLEAI 45
|
|
| |
