|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-260 |
1.38e-144 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 405.69 E-value: 1.38e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKM 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIM 160
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLVQQFLKGL 240
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFLDGI 246
|
250 260
....*....|....*....|
gi 2096624516 241 SDGPVPFHYPAQTYADELLG 260
Cdd:PRK11831 247 ADGPVPFRYPAGDYHADLLG 266
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
3.77e-126 |
|
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: 357.75 E-value: 3.77e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKM 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMarraalaraiaLDPELIM 160
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMrkrvalaralaLDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLVQQFL 237
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-236 |
4.63e-121 |
|
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: 344.87 E-value: 4.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMS 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLVQQF 236
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-213 |
3.61e-53 |
|
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: 171.55 E-value: 3.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelyAARTKMS 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
9.67e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 164.50 E-value: 9.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelyAARTKM 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-----PEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG------------Marraal 148
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvalaralaP------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 149 araialDPELIMYDEPFAGQDPismgvlvKL-------IKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVI-GAG 220
Cdd:COG3842 153 ------EPRVLLLDEPLSALDA-------KLreemreeLRRLQRELGITFIYVTHDQEEALALADRIAVM-NDGRIeQVG 218
|
....
gi 2096624516 221 TPDE 224
Cdd:COG3842 219 TPEE 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-224 |
4.16e-48 |
|
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: 159.03 E-value: 4.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELYAARTKM 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQ-SGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG------------Marraa 147
Cdd:COG1122 78 GLVFQnPDDQLFAPTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGqkqrvaiagvlaM----- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 148 laraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:COG1122 152 -------EPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-237 |
5.91e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 162.24 E-value: 5.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsrKELYAART--- 78
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--------RDLFTNLPpre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 -KMSMLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG---------Marraal 148
Cdd:COG1118 75 rRVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGqrqrvalarA------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 149 araIALDPELIMYDEPFAGQDpismgvlVKLIKSLNEVL-------GLSSLIVTHDVTEVMSIADHVIIIaDQGVIGA-G 220
Cdd:COG1118 148 ---LAVEPEVLLLDEPFGALD-------AKVRKELRRWLrrlhdelGGTTVFVTHDQEEALELADRVVVM-NQGRIEQvG 216
|
250
....*....|....*...
gi 2096624516 221 TPDEMRNH-ESPLVQQFL 237
Cdd:COG1118 217 TPDEVYDRpATPFVARFL 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-237 |
1.50e-47 |
|
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: 157.89 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyaarTKMS 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLRE---HTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNH-ESPLVQQFL 237
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHpASPFVYSFL 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
1.03e-46 |
|
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: 153.88 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMsRKELYAARTKMS 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPlrehtklsealiklvvlmklqavglrgakdlmpseLSGGMARRAALARAIALDPELIMY 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
1.18e-46 |
|
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: 154.55 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQ--SGALFTDmSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:cd03225 78 GLVFQnpDDQFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-240 |
2.57e-46 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 155.88 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAAR-TKMSMLFQSGALFTDMSVF 96
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 97 DNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVL 176
Cdd:cd03294 121 ENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 177 VKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE-MRNHESPLVQQFLKGL 240
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEiLTNPANDYVREFFRGV 264
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-240 |
4.14e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.00 E-value: 4.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpSMSRKELYAARTKM 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG------------Marraal 148
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGqqqrvaiaralaM------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 149 araialDPELIMYDEPFAGQDPISMGVLVKLIKSL-NEvlGLSSLIVTHDvtevMS----IADHVIIIaDQGVIGA-GTP 222
Cdd:COG1126 154 ------EPKVMLFDEPTSALDPELVGEVLDVMRDLaKE--GMTMVVVTHE----MGfareVADRVVFM-DGGRIVEeGPP 220
|
250
....*....|....*....
gi 2096624516 223 DEMRNH-ESPLVQQFLKGL 240
Cdd:COG1126 221 EEFFENpQHERTRAFLSKV 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-227 |
4.17e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 4.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsRKELYAARTKMS 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAF-------PLREHTKLSEALIKLVvlmklqavGLRGAKDLMPSELSGGMARRAALARAIAL 154
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFfarlyglPRKEARERIDELLELF--------GLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIaDQG-VIGAGTPDEMRN 227
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAII-DKGrIVADGTPDELKA 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
1.81e-45 |
|
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: 152.35 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS--FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:cd03258 1 MIELKNVSkvFGDTGGKVTalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGT 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
9.25e-45 |
|
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: 157.37 E-value: 9.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS-----RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYA 75
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 ARTKMSMLFQ--SGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGL-RGAKDLMPSELSGG----------- 141
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGqrqrvaiaral 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 -MarraalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:COG1123 420 aL------------EPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....
gi 2096624516 221 TPDE 224
Cdd:COG1123 488 PTEE 491
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
2.24e-44 |
|
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: 149.18 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVS--FSRGDRT--IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAAR 77
Cdd:cd03255 1 IELKNLSktYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 -TKMSMLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVtEVMSIADHVIIIADqGVI 217
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRD-GKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
2.78e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.24 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS----RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsrKELYAA 76
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMarraalaraiaLDP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMrqrvaiaralaNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVII 210
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
6.60e-44 |
|
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: 148.00 E-value: 6.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYK----NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaar 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 tkMSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:cd03293 75 --RGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-235 |
7.68e-44 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 149.03 E-value: 7.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYA---AR 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARlgiAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TkmsmlFQSGALFTDMSVFDN--IAFPLREHTKLSEALIKLVVLMK------------LQAVGLRGAKDLMPSELSGG-- 141
Cdd:COG0411 84 T-----FQNPRLFPELTVLENvlVAAHARLGRGLLAALLRLPRARReereareraeelLERVGLADRADEPAGNLSYGqq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 ---------MarraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIa 212
Cdd:COG0411 159 rrleiaralA-----------TEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL- 226
|
250 260
....*....|....*....|....
gi 2096624516 213 DQG-VIGAGTPDEMRNHesPLVQQ 235
Cdd:COG0411 227 DFGrVIAEGTPAEVRAD--PRVIE 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-237 |
1.31e-43 |
|
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: 147.77 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrKELYAARTKMS 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 162 DEPFAGQDpismgvlVKL-------IKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNH-ESPLV 233
Cdd:cd03300 155 DEPLGALD-------LKLrkdmqleLKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEpANRFV 227
|
....
gi 2096624516 234 QQFL 237
Cdd:cd03300 228 ADFI 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
2.06e-43 |
|
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: 146.88 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKD--VSFSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:cd03257 1 LLEVKNlsVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQ--SGALFTDMSVFDNIAFPLREHTKLS-EALIKLVVLMKLQAVGL-RGAKDLMPSELSGGMARRAALARAI 152
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM-YAGKI 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
4.20e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 4.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS--FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyAA 76
Cdd:COG1136 4 LLELRNLTksYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL-AR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 --RTKMSMLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG-----------Ma 143
Cdd:COG1136 83 lrRRHIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGqqqrvaiaralV- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 144 rraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDvTEVMSIADHVIIIADqGVI 217
Cdd:COG1136 161 ----------NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRD-GRI 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
4.74e-43 |
|
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: 145.79 E-value: 4.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLK-----PDAGDILFEGGSIPSMsRKELYAA 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDL-DVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFtDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGL--RGAKDLMPSELSGGMARRAALARAIAL 154
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLssLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-252 |
4.83e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 4.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS--FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:COG1135 1 MIELENLSktFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVV--LMKLqaVGLRGAKDLMPSELSGG------------M 142
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKAEIRKRVaeLLEL--VGLSDKADAYPSQLSGGqkqrvgiaralaN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 143 arraalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQG-VIGAGT 221
Cdd:COG1135 158 ------------NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVL-ENGrIVEQGP 224
|
250 260 270
....*....|....*....|....*....|..
gi 2096624516 222 PDEM-RNHESPLVQQFLKGLSDGPVPFHYPAQ 252
Cdd:COG1135 225 VLDVfANPQSELTRRFLPTVLNDELPEELLAR 256
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-238 |
6.94e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.67 E-value: 6.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTiyKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSmsrkeLYAARTKM 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-----LPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIM 160
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQA-LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE-MRNHESPLVQQFLK 238
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAlLDGEPPPALAAYLG 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-225 |
9.47e-43 |
|
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: 145.96 E-value: 9.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARtKM 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--AR-RI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAF-------PLREHTKLSEALIKLVvlmkLQAVGLRGAKDLMPSELSGG--------MARR 145
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDREAVEEA----LERTGLEHLADRPVDELSGGerqrvliaRALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 146 aalaraiaLDPELIMYDEPFAGQDPIS-MGVLvKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:COG1120 154 --------QEPPLLLLDEPTSHLDLAHqLEVL-ELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
.
gi 2096624516 225 M 225
Cdd:COG1120 225 V 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-229 |
1.24e-42 |
|
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: 145.27 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARTKMSM 82
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMK---------LQAVGLRGAKDLMPSELSGGMARRAALARAIA 153
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEReareraeelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 154 LDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIaDQG-VIGAGTPDEMRNHE 229
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVL-DQGrVIAEGTPDEVRNNP 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
4.08e-42 |
|
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: 143.98 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFpLREHTKLSEALIKLVVLMKLQAVGL--RGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE-MRNHESPLVQQFL 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFV 236
|
.
gi 2096624516 238 K 238
Cdd:cd03295 237 G 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
7.10e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 7.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTK 79
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFDNIAFPLREhTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG------------Marraa 147
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeqqrvaiaralvN----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 148 laraialDPELIMYDEPFAGQDP-ISMGVLvKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:COG2884 155 -------RPELLLADEPTGNLDPeTSWEIM-ELLEEINRR-GTTVLIATHDLELVDRMPKRVLEL-EDGRL 215
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-239 |
3.74e-41 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 145.00 E-value: 3.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA-RTKMSMLFQSGALFTDMSVF 96
Cdd:TIGR01186 10 NDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQFALFPHMTIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 97 DNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVL 176
Cdd:TIGR01186 90 QNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 177 VKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE-MRNHESPLVQQFLKG 239
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEiLRNPANEYVEEFIGK 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-237 |
1.36e-40 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 143.30 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRkeLYAARTKMS 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SR--LHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLR---EHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIAdQGVI-GAGTPDEM-RNHESPLVQQF 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS-QGNIeQAGTPDQVwREPATRFVLEF 236
|
.
gi 2096624516 237 L 237
Cdd:PRK10851 237 M 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
2.43e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 142.52 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrKELYAARTKM 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG----------Marraalar 150
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvalgraL-------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 151 aiALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVIG-AGTPDEMRNH 228
Cdd:COG3839 149 --VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM-NDGRIQqVGTPEELYDR 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-224 |
2.91e-40 |
|
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: 139.24 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMS 81
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFP-LREHTKLSEALI------KLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIAL 154
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGrLGRRSTWRSLFGlfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
6.00e-40 |
|
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: 137.66 E-value: 6.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSmSRKELYAARTKMS 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFM-DDGRI 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
12-236 |
1.47e-38 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 137.86 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 12 GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRkeLYAARTKMSMLFQSGALFT 91
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI---TR--LPPQKRDYGIVFQSYALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 92 DMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPI 171
Cdd:TIGR03265 90 NLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 172 smgVLVKL---IKSLNEVLGLSSLIVTHDVTEVMSIADHvIIIADQGVI-GAGTPDEMRNH-ESPLVQQF 236
Cdd:TIGR03265 169 ---VREHLrteIRQLQRRLGVTTIMVTHDQEEALSMADR-IVVMNHGVIeQVGTPQEIYRHpATPFVADF 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-213 |
6.34e-38 |
|
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: 130.98 E-value: 6.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsRKELYAARTKMS 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIafplrehtklsealiklvvlmklqavglrgakdlmpsELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
9.12e-38 |
|
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: 138.50 E-value: 9.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKD--VSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDA---GDILFEGGSIPSMSRKELya 75
Cdd:COG1123 4 LLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 aRTKMSMLFQS-GALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIAL 154
Cdd:COG1123 82 -GRRIGMVFQDpMTQLNPVTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
1.13e-36 |
|
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: 128.91 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrKELYAARTKMS 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 162 DEPFAGQDpismgvlVKL-------IKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADqGVI 217
Cdd:cd03301 155 DEPLSNLD-------AKLrvqmraeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND-GQI 209
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-230 |
1.17e-36 |
|
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: 129.70 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMSML 83
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHE--RARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 84 FQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDE 163
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 164 PFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHES 230
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
2.09e-36 |
|
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: 128.81 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELYA-ARTKM 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMHKrARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIM 160
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEEL-LEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
7.41e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 7.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsrKELYAARTKM 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG--------KPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTD--MSVFDNIAFPLREHTKLSEAL---IKLVVLMKLQAVGLRGAKDLMPSELSGG-----------MAr 144
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPsraDREAVDEALERVGLEDLADRPIGELSGGqqqrvllaralAQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 145 raalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIaDQGVIGAGTPDE 224
Cdd:COG1121 157 ----------DPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEE 224
|
....*
gi 2096624516 225 MRNHE 229
Cdd:COG1121 225 VLTPE 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-220 |
4.28e-35 |
|
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: 124.95 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsrKELYAARTKMSM 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQSGALFTDM--SVFDNIAFPLREHTKLSEALIKLV---VLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:cd03235 73 VPQRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKADkakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIaDQGVIGAG 220
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-213 |
9.50e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 9.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKMSM 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQSGALFtDMSVFDNIAFP--LREHTKLSEALIKLvvlmkLQAVGLrgAKDLM---PSELSGG----------Marraa 147
Cdd:COG4619 79 VPQEPALW-GGTVRDNLPFPfqLRERKFDRERALEL-----LERLGL--PPDILdkpVERLSGGerqrlaliraL----- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 148 laraiALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:COG4619 146 -----LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
9.78e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 124.92 E-value: 9.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRG----DRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaa 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQS--GALFTDMSVFDNIAFPLREHtKLSEALIKLVVLmkLQAVGLRGA-KDLMPSELSGG----------Ma 143
Cdd:COG1124 78 RRRVQMVFQDpyASLHPRHTVDRILAEPLRIH-GLPDREERIAEL--LEQVGLPPSfLDRYPHQLSGGqrqrvaiaraL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 144 rraalaraiALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVIGA-GTP 222
Cdd:COG1124 154 ---------ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM-QNGRIVEeLTV 223
|
250
....*....|....*..
gi 2096624516 223 DEMRN-HESPLVQQFLK 238
Cdd:COG1124 224 ADLLAgPKHPYTRELLA 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-237 |
3.91e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.68 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS--FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:PRK11153 1 MIELKNISkvFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNH-ESPLVQQ 235
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHpKHPLTRE 239
|
..
gi 2096624516 236 FL 237
Cdd:PRK11153 240 FI 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-237 |
5.36e-34 |
|
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: 122.83 E-value: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaaRTKMSMLFQSGALFTDMSVFD 97
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLV 177
Cdd:cd03299 91 NIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 178 KLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESP-LVQQFL 237
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNeFVAEFL 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
6.23e-34 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 122.23 E-value: 6.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVS--FSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsRKELYAARTK 79
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFDNIAFPLREHTkLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELI 159
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSlnEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMR 226
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-220 |
2.45e-33 |
|
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: 119.46 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARtKMSM 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--AR-KIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQSgalftdmsvfdniafplrehtklsealiklvvlmkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYD 162
Cdd:cd03214 78 VPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 163 EPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-225 |
3.19e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 123.68 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyaarTKMS 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-237 |
3.49e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 122.51 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:COG1125 1 MIEFENVTKRyPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFDNIAF-PLREhtKLSEALIKLVV--LMKLqaVGLRGAK--DLMPSELSGG------------M 142
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATvPRLL--GWDKERIRARVdeLLEL--VGLDPEEyrDRYPHELSGGqqqrvgvaralaA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 143 arraalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTP 222
Cdd:COG1125 154 ------------DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTP 221
|
250
....*....|....*.
gi 2096624516 223 DEM-RNHESPLVQQFL 237
Cdd:COG1125 222 EEIlANPANDFVADFV 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
4.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRT-IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpSMSRKELYAARTK 79
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQS--GALFTDmSVFDNIAF-PLreHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK13639 80 VGIVFQNpdDQLFAP-TVEEDVAFgPL--NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-237 |
3.63e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 119.09 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIY-----KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkalDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGA--LFTDmSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGA-KDLMPSELSGGMARRAALARAIA 153
Cdd:TIGR04521 81 RKKVGLVFQFPEhqLFEE-TVYKDIAFGPK-NLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 154 LDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLV 233
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELE 238
|
....
gi 2096624516 234 QQFL 237
Cdd:TIGR04521 239 KIGL 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-220 |
5.63e-32 |
|
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: 117.01 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPkGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFeGGSIPSMSRKELY--AARTKMSMLFQSGALFTDMSVF 96
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRKKINlpPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 97 DNIAFPLREHTKlSEALI---KLVVLMKLQAVGLRGakdlmPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISM 173
Cdd:cd03297 94 ENLAFGLKRKRN-REDRIsvdELLDLLGLDHLLNRY-----PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2096624516 174 GVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
6.11e-32 |
|
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: 116.42 E-value: 6.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsRKELYAARTKM 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFplreHTKLSEALIKLVVLMK-LQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELI 159
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRF----WAALYGLRADREAIDEaLEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHD 197
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQ 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-241 |
1.66e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElYAARTKM 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIM 160
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIaDQGVIGA-GTPDEM-RNHESPLVQQFLK 238
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFI-DKGRIAEdGDPQVLiKNPPSQRLQEFLQ 237
|
...
gi 2096624516 239 GLS 241
Cdd:PRK09493 238 HVS 240
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-231 |
1.86e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.28 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelyAARTKMS 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-----AENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 162 DEPFAGQDpismgvlVKL-------IKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADqGVIGA-GTPDEMrnHESP 231
Cdd:PRK09452 169 DESLSALD-------YKLrkqmqneLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD-GRIEQdGTPREI--YEEP 236
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-237 |
2.20e-31 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 118.64 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIyKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSmsrkeLYAARTKM 80
Cdd:NF040840 1 MIRIENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN-----LPPEKRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIM 160
Cdd:NF040840 75 AYVYQNYMLFPHKTVFENIAFGLKLR-KVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM-RNHESPLVQQFL 237
Cdd:NF040840 154 LDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVfRRPKNEFVARFV 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-230 |
4.13e-31 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 117.59 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 32 IMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrKELYAARTKMSMLFQSGALFTDMSVFDNIAFPLREHtKLSE 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMR-KVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 112 ALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSS 191
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2096624516 192 LIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHES 230
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
7.07e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 115.16 E-value: 7.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILfeGGSIPsmsrkeLYAARTKMSML 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--AGTAP------LAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 84 FQSGALFTDMSVFDNIAFPLREHTKlSEALiklvvlMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDE 163
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQWR-DAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 164 PFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADqGVIG 218
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE-GKIG 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-199 |
1.31e-30 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 113.60 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 8 SFSRGDRT--IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTK-MSMLF 84
Cdd:TIGR02211 10 RYQEGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 85 QSGALFTDMSVFDNIAFP-LREHTKLSEAliKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDE 163
Cdd:TIGR02211 90 QFHHLLPDFTALENVAMPlLIGKKSVKEA--KERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 2096624516 164 PFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVT 199
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-220 |
1.35e-30 |
|
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: 113.36 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDrtiyKNMSFS--VPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelyAARTK 79
Cdd:cd03298 1 VRLDKIRFSYGE----QPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELI 159
Cdd:cd03298 72 VSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVA-LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
3.30e-30 |
|
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: 110.41 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKMSM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQsgalftdmsvfdniafplrehtklsealiklvvlmklqavglrgakdlmpseLSGGMARRAALARAIALDPELIMYD 162
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 163 EPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
3.73e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.97 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRkelyaaRTKMS 81
Cdd:cd03226 1 RIENISFSyKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQS--GALFTDmSVFDNIAFPLREhtkLSEALIKLVVLMKLqaVGLRGAKDLMPSELSGGMARRAALARAIALDPELI 159
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELLLGLKE---LDAGNEQAETVLKD--LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-220 |
4.35e-30 |
|
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: 111.99 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsRKELYAARTKMS 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFpLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVY-LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-197 |
7.87e-30 |
|
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: 111.35 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMSMLFQSGALFTDMSVFDN 98
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 IAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVK 178
Cdd:cd03292 99 VAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170
....*....|....*....
gi 2096624516 179 LIKSLNEVlGLSSLIVTHD 197
Cdd:cd03292 178 LLKKINKA-GTTVVVATHA 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-240 |
1.75e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.36 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAAR-TKMSMLFQSGALFTDMSVF 96
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 97 DNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVL 176
Cdd:PRK10070 125 DNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 177 VKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHES-PLVQQFLKGL 240
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAnDYVRTFFRGV 268
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
2.47e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRT-IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpSMSRKELYAARTK 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQS--GALFTdMSVFDNIAF-PLreHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK13636 84 VGMVFQDpdNQLFS-ASVYQDVSFgAV--NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-210 |
2.62e-29 |
|
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: 112.45 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKD--VSFSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKP---DAGDILFEGGSIPSMSRKEL 73
Cdd:COG0444 1 LLEVRNlkVYFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 74 YAARTK-MSMLFQS--GALftD--MSVFDNIAFPLREHTKLS-EALIKLVVLMkLQAVGLRGAKDLM---PSELSGGMar 144
Cdd:COG0444 81 RKIRGReIQMIFQDpmTSL--NpvMTVGDQIAEPLRIHGGLSkAEARERAIEL-LERVGLPDPERRLdryPHELSGGMrq 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 145 raalaraialDPELIMYDEPFAGQDP-ISMGVLvKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVII 210
Cdd:COG0444 158 rvmiaralalEPKLLIADEPTTALDVtIQAQIL-NLLKDLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-226 |
3.06e-29 |
|
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: 109.77 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaARTKMS 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIA-------FPLREHTKLSEALIKLVVLMKlqavglrgAKDLMPSELSGGMARRAALARAIAL 154
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYiharlygVPGAERRERIDELLDFVGLLE--------AADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMR 226
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-213 |
5.85e-29 |
|
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: 108.84 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrKELYAARTKMS 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVvlmkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLL-GIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINK 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
6.49e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.35 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELYA-ARTK 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THLPMHKrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGG----------MARraala 149
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVL-ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGerrrveiaraLAT----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 150 raialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:COG1137 154 -----NPKFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
9.55e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 9.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS--RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELYAART 78
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQS-GALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLI-VTHDVTEVMsIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKT-RKKTLIsITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-239 |
1.66e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.90 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEG----------GSIPSMSRKEL 73
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdGQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 74 YAARTKMSMLFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRG-AKDLMPSELSGGMARRAALARAI 152
Cdd:PRK10619 88 RLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIaDQGVI-GAGTPDEM-RNHES 230
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFL-HQGKIeEEGAPEQLfGNPQS 245
|
....*....
gi 2096624516 231 PLVQQFLKG 239
Cdd:PRK10619 246 PRLQQFLKG 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 |
2.48e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.43 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPsmsrkelYAARTKM 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREH-TKLSEALIKLVVLMKLQAVGLRGAKDLmpSELSGGMARRAALARAIALDPELI 159
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVYLARLKgLSKAEAKRRADEWLERLGLGDRANKKV--EELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSLNE----VLgLSslivTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRN 227
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAkgttVI-FS----SHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-198 |
3.76e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.80 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDA---GDILFEGGSIpsmsrKELYAAR 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRL-----TALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQSGALFTDMSVFDNIAFPLREHTKLSEAliKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLAFALPPTIGRAQR--RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2096624516 158 LIMYDEPFAGQDP---ISMGVLVkliksLNEV--LGLSSLIVTHDV 198
Cdd:COG4136 154 ALLLDEPFSKLDAalrAQFREFV-----FEQIrqRGIPALLVTHDE 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
1.61e-27 |
|
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: 104.00 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRT--IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFtDMSVFDNIafplrehtkLSE----------ALIKlvvlmklqavglrgakdlmpselsggmarraala 149
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI---------LSGgqrqriaiarALLR---------------------------------- 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 150 raialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMsIADHVIIIAD 213
Cdd:cd03228 114 -----DPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-229 |
1.75e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 106.23 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARTKM 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREH--TKLSEALIKLVVLMK------------LQAVGLRGAKDLMPSELSGGMARRA 146
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAQHQQlkTGLFSGLLKTPAFRRaesealdraatwLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 147 ALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGV-IGAGTPDEM 225
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV-NQGTpLANGTPEEI 241
|
....
gi 2096624516 226 RNHE 229
Cdd:PRK11300 242 RNNP 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-225 |
2.52e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.89 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRK-ELYAARTKMSMLFQSGALFTDMSVFDNI 99
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 100 AFPLR----EHTKLSEALIklvvlmkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGV 175
Cdd:TIGR02142 97 RYGMKrarpSERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2096624516 176 LVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-166 |
2.56e-27 |
|
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: 102.73 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 17 YKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKMSMLFQSGALFTDMSVF 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 97 DNIAFPLR-EHTKLSEALIKLVVLMKLqaVGLRGAKD----LMPSELSGGMARRAALARAIALDPELIMYDEPFA 166
Cdd:pfam00005 78 ENLRLGLLlKGLSKREKDARAEEALEK--LGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-196 |
7.09e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.73 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLR-------LIggqlkPDA---GDILFEGGSI--PSMS 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLI-----PGArveGEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 70 RKELyaaRTKMSMLFQSGALFTdMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRG-AKDLM---PSELSGG---- 141
Cdd:COG1117 87 VVEL---RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDeVKDRLkksALGLSGGqqqr 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 142 --------MarraalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLssLIVTH 196
Cdd:COG1117 163 lciaralaV------------EPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVTH 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-234 |
7.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.20 E-value: 7.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSF---SRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsiPSMSRKELYAAR 77
Cdd:PRK13650 4 IIEVKNLTFkykEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQS-GALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVmSIADHVIIIADQGVIGAGTPDEMRNHESPLVQ 234
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQ 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-229 |
1.67e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.43 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 14 RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMSMLFQSGALFTDM 93
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 94 SVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISM 173
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 174 GVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:PRK10895 174 IDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-228 |
2.18e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEG---GSIPSMSRkelyaar 77
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlSHVPPYQR------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 tKMSMLFQSGALFTDMSVFDNIAFPLREhTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:PRK11607 92 -PINMMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 158 LIMYDEPfagqdpisMGVLVKLIK--------SLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNH 228
Cdd:PRK11607 170 LLLLDEP--------MGALDKKLRdrmqlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
3.88e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.63 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS----RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI--PSMSRkely 74
Cdd:COG4525 3 MLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 aartkmSMLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIAL 154
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIA 212
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-229 |
7.38e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.96 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaARTKMS 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH----ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLnEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-227 |
7.57e-26 |
|
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: 100.97 E-value: 7.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARTKMSM 82
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQSGALFTDMSVFDNI---AFPLREHtKLSEALIKLVVL------MKLQAVGlrgakdlmpsELSGG-----------M 142
Cdd:cd03224 80 VPEGRRIFPELTVEENLllgAYARRRA-KRKARLERVYELfprlkeRRKQLAG----------TLSGGeqqmlaiaralM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 143 arraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTP 222
Cdd:cd03224 149 -----------SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
....*
gi 2096624516 223 DEMRN 227
Cdd:cd03224 217 AELLA 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-210 |
8.03e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 103.27 E-value: 8.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMSMLFQ--SGALFTDMSVFDN 98
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQdpYASLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 IAFPLREHTKLSEALIKLVVLMKLQAVGLR-GAKDLMPSELSGG-----------MArraalaraialDPELIMYDEPFA 166
Cdd:COG4608 118 IAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGqrqrigiaralAL-----------NPKLIVCDEPVS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2096624516 167 GQD-PISMGVLvKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVII 210
Cdd:COG4608 187 ALDvSIQAQVL-NLLEDLQDELGLTYLFISHDLSVVRHISDRVAV 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-213 |
1.20e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 100.32 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 13 DRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelyAARTKMSMLFQSGALFTD 92
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 93 MSVFDNIAFPLREHTKLSeALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPIS 172
Cdd:TIGR01277 85 LTVRQNIGLGLHPGLKLN-AEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2096624516 173 MGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQ 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-249 |
1.67e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGD--RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGD---ILFEGgsiPSMSRKELYAA 76
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG---ITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQS-GALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALD 155
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 156 PELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVmSIADHVIIIADQGVIGAGTPDEMRNHESpLVQQ 235
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE-MLKE 239
|
250
....*....|....
gi 2096624516 236 FlkGLSdgpVPFHY 249
Cdd:PRK13640 240 I--GLD---IPFVY 248
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-211 |
2.04e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 100.23 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsrKELYAARTKMSMLFQSGALFTDMSVFD 97
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG--------KQITEPGPDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIAFPLRE-HTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVL 176
Cdd:TIGR01184 74 NIALAVDRvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2096624516 177 VKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-229 |
2.40e-25 |
|
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: 104.45 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAFPLREHTK--LSEALiKLV----VLMKLQA-----VGLRGAKdlmpseLSGG-------- 141
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLGRPDASDeeLEAAL-EAAgldeFVAALPDgldtpLGEGGRG------LSGGqaqrlala 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 ---MarraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDvTEVMSIADHVIIIADQGVIG 218
Cdd:COG4988 486 ralL-----------RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVE 551
|
250
....*....|.
gi 2096624516 219 AGTPDEMRNHE 229
Cdd:COG4988 552 QGTHEELLAKN 562
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-226 |
3.67e-25 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 100.93 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaARTKMSMLFQSGALFTDMSVFD 97
Cdd:TIGR01188 10 DGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK----VRRSIGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NI-------AFPLREHTKLSEALIKLVvlmklqavGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDP 170
Cdd:TIGR01188 86 NLemmgrlyGLPKDEAEERAEELLELF--------ELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 171 ISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIaDQG-VIGAGTPDEMR 226
Cdd:TIGR01188 158 RTRRAIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAII-DHGrIIAEGTPEELK 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
4.71e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELYAARTK 79
Cdd:PRK13652 3 LIETRDLCYSySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQS--GALFTDmSVFDNIAF-PLreHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK13652 80 VGLVFQNpdDQIFSP-TVEQDIAFgPI--NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLVQQF 236
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVH 236
|
.
gi 2096624516 237 L 237
Cdd:PRK13652 237 L 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
5.79e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAG-----DILFEGGSIPSMSRKELYA 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 ARTKMSMLFQSGALFTDMSVFDNI--------AFPLREHTKLSEALiklvvlmkLQAVGLRGAKDLMPSELSGGMARRAA 147
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIiegpvivkGEPKEEATARAREL--------LAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 148 LARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIaDQGVIGAGTPDE--M 225
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFM-DQGRIVEQGPAKalF 232
|
250
....*....|..
gi 2096624516 226 RNHESPLVQQFL 237
Cdd:PRK11264 233 ADPQQPRTRQFL 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-198 |
6.20e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.12 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 16 IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAART-KMSMLFQSGALFTDMS 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 95 VFDNIAFPLR-EHTKLSEALIKlvVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISM 173
Cdd:PRK11629 104 ALENVAMPLLiGKKKPAEINSR--ALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|....*
gi 2096624516 174 GVLVKLIKSLNEVLGLSSLIVTHDV 198
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
6.69e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 6.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS-RGDRTI-YKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRT 78
Cdd:PRK13648 7 IIVFKNVSFQyQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGA-LFTDMSVFDNIAFPLREHTKLSEALIKlVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:PRK13648 84 HIGIVFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMHR-RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEMRNHESPLVQ 234
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
1.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRT-IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQS--GALFTdMSVFDNIAF-PLreHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:PRK13647 82 GLVFQDpdDQVFS-STVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPD--------EMRNHE 229
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSlltdedivEQAGLR 237
|
250
....*....|.
gi 2096624516 230 SPLVQQFLKGL 240
Cdd:PRK13647 238 LPLVAQIFEDL 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-237 |
1.48e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 97.75 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARTKM 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNI---AFPLREHTKLSEALIKLVVL------MKLQAVGLrgakdlmpseLSGG---------- 141
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLllgAYARRDRAEVRADLERVYELfprlkeRRRQRAGT----------LSGGeqqmlaigra 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 -MArraalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIaDQG-VIGA 219
Cdd:COG0410 151 lMS-----------RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVL-ERGrIVLE 217
|
250
....*....|....*...
gi 2096624516 220 GTPDEMRNHESpLVQQFL 237
Cdd:COG0410 218 GTAAELLADPE-VREAYL 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-231 |
2.60e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelyAARTKMSMLFQSGALFTDMSVFDNIA 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 101 FPLREHTKLSEALIKLVVLMkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLI 180
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAI-ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 181 KSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESP 231
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-235 |
5.38e-24 |
|
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: 100.68 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS--RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDmSVFDNIAF--PLREHTKLSEALiKLVVL--------MKLQA-VGLRGAKdlmpseLSGG------- 141
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLgdPDATDEEIIEAA-RLAGLhdfiealpMGYDTvVGEGGSN------LSGGqrqrlai 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 ----MarraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDvTEVMSIADHVIIIaDQG-V 216
Cdd:COG2274 623 aralL-----------RNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVL-DKGrI 687
|
250 260
....*....|....*....|..
gi 2096624516 217 IGAGTPDEMRNHESP---LVQQ 235
Cdd:COG2274 688 VEDGTHEELLARKGLyaeLVQQ 709
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-213 |
1.05e-23 |
|
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: 95.47 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVS--FSRGD--RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAAR 77
Cdd:TIGR02982 2 ISIRNLNhyYGHGSlrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQSGALFTDMSVFDNIAFPLREHTKLS-EALIKLVVLMkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQPNLSyQEARERARAM-LEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDvTEVMSIADHVIIIAD 213
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMED 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-225 |
1.07e-23 |
|
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: 97.86 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVkDVSFSRGDRTIykNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFeGGSIPSMSRKELY--AART 78
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-GGEVLQDSARGIFlpPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLvvlmkLQAVGLRGAKDL---MPSELSGG-----------Mar 144
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRK-RAPRAERRISF-----DEVVELLGIGHLldrRPATLSGGerqrvaigralL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 145 raalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQG-VIGAGTPD 223
Cdd:COG4148 150 ---------SSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLL-EQGrVVASGPLA 219
|
..
gi 2096624516 224 EM 225
Cdd:COG4148 220 EV 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
1.38e-23 |
|
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: 95.13 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS--FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsRKELYAA 76
Cdd:cd03266 1 MITADALTkrFRDVKKTVQavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNIAFPLREH----TKLSEALIKLVVLMKLQAVGLRGAKDlmpseLSGGMARRAALARAI 152
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYglkgDELTARLEELADRLGMEELLDRRVGG-----FSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
1.50e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 99.08 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAFPLREHT--KLSEALiKLV----VLMKL-----QAVGLRGAKdlmpseLSGG-------- 141
Cdd:COG1132 417 GVVPQDTFLFSG-TIRENIRYGRPDATdeEVEEAA-KAAqaheFIEALpdgydTVVGERGVN------LSGGqrqriaia 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 ---MarraalaraiaLDPELIMYDEPFAGQDPISMgvlVKLIKSLNEVL-GLSSLIVTHDVTEVMSiADHVIIIaDQG-V 216
Cdd:COG1132 489 ralL-----------KDPPILILDEATSALDTETE---ALIQEALERLMkGRTTIVIAHRLSTIRN-ADRILVL-DDGrI 552
|
....*...
gi 2096624516 217 IGAGTPDE 224
Cdd:COG1132 553 VEQGTHEE 560
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-215 |
2.45e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrKELYaaRTKM 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIY--RQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAFP--LREHTKLSEALIKLVVLMKLQAVGLRgaKDLmpSELSGGMARRAALARAIALDPEL 158
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPwqIRNQQPDPAIFLDDLERFALPDTILT--KNI--AELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVmSIADHVIIIADQG 215
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQPHA 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
2.95e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARtKM 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--AR-RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAF---PLREH-TKLSEALIKLVVlMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYgrsPWLSLwGRLSAEDNARVN-QAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 157 ELIMYDEPFAGQDpISMGV-LVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:PRK11231 158 PVVLLDEPTTYLD-INHQVeLMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-225 |
3.32e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 13 DRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIG-------GQLKPDaGDILFEGGSIPSMSRKELyaaRTKMSMLFQ 85
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVD-GKVLYFGKDIFQIDAIKL---RKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 86 SGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGL-RGAKDLM---PSELSGGMARRAALARAIALDPELIMY 161
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEVLGLssLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
4.77e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARtKM 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--AK-RL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAF---P-------LREHTKLSEALiklvvlmklQAVGLRGAKDLMPSELSGGMARRAALAR 150
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFgrfPyskgrltAEDREIIDEAI---------AYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 151 AIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
5.90e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 97.53 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSR--GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFtDMSVFDNIAF--PlrehtKLSEALIKLVvlmkLQAVGLRGAKDLMP-----------SELSGGMARRA 146
Cdd:COG4987 411 IAVVPQRPHLF-DTTLRENLRLarP-----DATDEELWAA----LERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 147 ALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEvMSIADHVIIIADQGVIGAGTPDE 224
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAG-LERMDRILVLEDGRIVEQGTHEE 555
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
6.19e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARTKm 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL--ARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAF---PLREHTKLSEALiklvVLMKLQAVGLRGAKDLMPSELSGG------MARRAALARA 151
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDAL----VAAALAQVDLAHLAGRDYPQLSGGeqqrvqLARVLAQLWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 152 IALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-217 |
7.65e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 11 RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMSMLFQS--GA 88
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsiSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 89 LFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGA-KDLMPSELSGGMARRAALARAIALDPELIMYDEPFAG 167
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2096624516 168 QDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM-DNGQI 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-213 |
8.92e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 92.64 E-value: 8.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGkITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaARTKMS 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-225 |
1.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.30 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 6 DVSFSRGDRTIYK-----NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRK--ELYAART 78
Cdd:PRK13645 11 NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQ--SGALFTDmSVFDNIAF-PLREHTKLSEALIKLVVLMKLQAVGLRGAKDlMPSELSGGMARRAALARAIALD 155
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGENKQEAYKKVPELLKLVQLPEDYVKR-SPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 156 PELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.32e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.90 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRkelyAARTKMS 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDN-IAFP--LREHTKLSEALIKLVvlmkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENlLVFGryFGMSTREIEAVIPSL----LEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLnEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-234 |
1.47e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDIlfEGGSIPsMSRKELYAARTK 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--TVGGMV-LSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQS-GALFTDMSVFDNIAFPLREHTKLSEALIKLVVlMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVD-QALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEMRNHESPLVQ 234
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
3.49e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKM 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SmlfQSGALFTDMSVFDNIAF---PLREHTKLSEALIKLVvlmkLQAVGLRGAKDLMPSELSGGMARR-------AALAR 150
Cdd:COG4559 81 P---QHSSLAFPFTVEEVVALgraPHGSSAAQDRQIVREA----LALVGLAHLAGRSYQTLSGGEQQRvqlarvlAQLWE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 151 AIALDPELIMYDEPFAGQDP----ISMGVLVKLIKSlnevlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:COG4559 154 PVDGGPRWLFLDEPTSALDLahqhAVLRLARQLARR-----GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-241 |
9.70e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI---PSMSRKELYAART 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGALFTDMSVFDNiafplrehtkLSEALIKLVVLMKLQAVG--------LRGAK--DLMPSELSGGMARRAAL 148
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEN----------LIEAPCKVLGLSKEQAREkamkllarLRLTDkaDRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMrnh 228
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF--- 228
|
250
....*....|...
gi 2096624516 229 ESPLVQQFLKGLS 241
Cdd:COG4161 229 TQPQTEAFAHYLS 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-199 |
9.91e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 9.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSR-GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTK 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFDNIAFPLREHTKLSEAlIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELI 159
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDD-IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2096624516 160 MYDEPFAG-QDPISMGVLvKLIKSLNEVlGLSSLIVTHDVT 199
Cdd:PRK10908 160 LADEPTGNlDDALSEGIL-RLFEEFNRV-GVTVLMATHDIG 198
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-225 |
1.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSR-KELYAARTKMSMLFQ--SGALFTDmSV 95
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 96 FDNIAFPlREHTKLSEALIKLVVLMKLQAVGL-RGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMG 174
Cdd:PRK13643 103 LKDVAFG-PQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 175 VLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13643 182 EMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-225 |
2.18e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.54 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 14 RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKP-----DAGDILFEGGSIpsMSRKELYAARTKMSMLFQSGA 88
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 89 LFTdMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGA-KDLM---PSELSGGMARRAALARAIALDPELIMYDEP 164
Cdd:PRK14271 112 PFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 165 FAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
3.59e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.08 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIY-----KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI-PSMSRKELYA 75
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerralYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 ARTKMSMLFQ--SGALFTDmSVFDNIAF-PLREHTKLSEALIKLVVLMKLqaVGLrgAKDLM---PSELSGGMARRAALA 149
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFgPMNFGVSEEDAKQKAREMIEL--VGL--PEELLarsPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-224 |
3.96e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKeLYAARTKMSMLFQ--SGALFTDmSV 95
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 96 FDNIAFPLReHTKLSEALIKLVVLMKLQAVGL--RGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISM 173
Cdd:PRK13637 102 EKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 174 GVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
6.01e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.44 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---RRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAFPLREHTKlsEALIKLV-------VLMKLQ-----AVGLRGAKdlmpseLSGGMARRAAL 148
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGRPDATD--EEVIEAAkaaqihdKIMRFPdgydtIVGERGLK------LSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDPISMgvlVKLIKSLNEVL-GLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEM 225
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTE---REIQAALRDVSkGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-212 |
7.16e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI--PSMSRkelyaart 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAER-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 kmSMLFQSGALFTDMSVFDNIAFPLrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK11248 73 --GVVFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIA 212
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLS 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-210 |
7.70e-21 |
|
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: 91.28 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTT----MLRLIggqlkPDAGDILFEGGSIPSMSRKELYAARTKMSMLFQS--GALFT 91
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpfGSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 92 DMSVFDNIAFPLREH-TKLSEALIKLVVLMKLQAVGL-RGAKDLMPSELSGG----------MARraalaraialDPELI 159
Cdd:COG4172 378 RMTVGQIIAEGLRVHgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGqrqriaiaraLIL----------EPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 160 MYDEPFAGQDpisMGV---LVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVII 210
Cdd:COG4172 448 VLDEPTSALD---VSVqaqILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMV 498
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
7.96e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 87.67 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:cd03254 3 IEFENVNFSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAF--PLREHTKLSEALiKLV----VLMKLQ-----AVGLRGakdlmpSELSGGMARRAALA 149
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLgrPNATDEEVIEAA-KEAgahdFIMKLPngydtVLGENG------GNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEM 225
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
1.20e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPDA---GDILFEGGSIPSMSRKELyaa 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVIEL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNIAFPLREHTKL-SEALIKLVVLMKLQAVGL----RGAKDLMPSELSGGMARRAALARA 151
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 152 IALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLssLIVTHDVTEVMSIADHVIIIADQGVIGAG-TPDEMRNHES 230
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGpTREVFTNPRH 238
|
....*....
gi 2096624516 231 PLVQQFLKG 239
Cdd:PRK14247 239 ELTEKYVTG 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-237 |
2.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI-PSMSRKELYAARTKMSMLFQ--SGALFTDmSV 95
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 96 FDNIAF-PLREHTKLSEALIKLVVLMKlqAVGLrgAKDLM---PSELSGGMARRAALARAIALDPELIMYDEPFAGQDPI 171
Cdd:PRK13641 104 LKDVEFgPKNFGFSEDEAKEKALKWLK--KVGL--SEDLIsksPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 172 SMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLVQQFL 237
Cdd:PRK13641 180 GRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYL 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-206 |
3.27e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIG--GQLKPDA---GDILFEGgsipsmsrKELYAA 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGFrveGKVTFHG--------KNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 -------RTKMSMLFQSGALFTDmSVFDNIAFPLR------EHTKLSEALIKLVVLM-----KLQAVGLrgakdlmpsEL 138
Cdd:PRK14243 83 dvdpvevRRRIGMVFQKPNPFPK-SIYDNIAYGARingykgDMDELVERSLRQAALWdevkdKLKQSGL---------SL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 139 SGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLssLIVTHDVTEVMSIAD 206
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-234 |
3.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.14 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIY-----KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSR-KELYA 75
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 ARTKMSMLFQ--SGALFTDmSVFDNIAF-PLREHTKLSEALIKLVVLMkLQAVGLRGAKDLMPSELSGGMARRAALARAI 152
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFgPKNFKMNLDEVKNYAHRLL-MDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHESPL 232
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
..
gi 2096624516 233 VQ 234
Cdd:PRK13646 241 AD 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-241 |
3.98e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI-----LFEGGSIPSmsRKELYAA 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDFSKTPS--DKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTKMSMLFQSGALFTDMSVFDNiafplrehtkLSEALIKLVVLMKLQAVG----------LRGAKDLMPSELSGGMARRA 146
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQN----------LIEAPCRVLGLSKDQALAraekllerlrLKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 147 ALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMr 226
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF- 228
|
250
....*....|....*
gi 2096624516 227 nhESPLVQQFLKGLS 241
Cdd:PRK11124 229 --TQPQTEAFKNYLS 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-206 |
4.76e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIG------GQLKPDaGDILFEGGSIPSmSRKELYA 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVE-GRVEFFNQNIYE-RRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 ARTKMSMLFQSGALFTdMSVFDNIAF--------PLREHTKLSEALIKLVVLM-----KLQAVGLrgakdlmpsELSGGM 142
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYgvkivgwrPKLEIDDIVESALKDADLWdeikhKIHKSAL---------DLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 143 ARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIAD 206
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-225 |
8.56e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.32 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS--FSRGDRTIYK---NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGS--IPSMSRKEL 73
Cdd:TIGR03269 279 IIKVRNVSkrYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 74 YAARTK--MSMLFQSGALFTDMSVFDNI--AFPLrehtKLSEALIKLVVLMKLQAVGLRGAK-----DLMPSELSGGMAR 144
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNLteAIGL----ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 145 RAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
.
gi 2096624516 225 M 225
Cdd:TIGR03269 515 I 515
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-251 |
1.20e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.01 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEG---GSIPSMSRkelyaart 78
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVPPAER-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGALFTDMSVFDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLK-LAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 159 IMYDEPFAGQDP---ISMGVlvkLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMrnhesplvqq 235
Cdd:PRK11000 155 FLLDEPLSNLDAalrVQMRI---EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL---------- 221
|
250
....*....|....*.
gi 2096624516 236 flkglsdgpvpFHYPA 251
Cdd:PRK11000 222 -----------YHYPA 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-170 |
1.27e-19 |
|
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: 83.95 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI----PSMSRKELYAArt 78
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrDEPHENILYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 kmsmlfQSGALFTDMSVFDNIAFPLREHtklseALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:TIGR01189 80 ------HLPGLKPELSALENLHFWAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170
....*....|..
gi 2096624516 159 IMYDEPFAGQDP 170
Cdd:TIGR01189 149 WILDEPTTALDK 160
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-228 |
1.27e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.30 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMSMLFQS--GALFTDMSVFDN 98
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 IAFPLRE-HTKLSEALIKLVVLMKLQAVGLRgaKDLM---PSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMG 174
Cdd:PRK15079 121 IAEPLRTyHPKLSRQEVKDRVKAMMLKVGLL--PNLInryPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 175 VLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNH 228
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-217 |
1.34e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 84.69 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFeGGSIPSMSRKELYAartKMSMLF-QSGALFTDMSVF 96
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFLR---RIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 97 DNIAFpLREHTKLSEA-----LIKLVVLMKLQAVGLRGAKDL-----MPSELSGGMarraalaraiALDPELIMYDEPFA 166
Cdd:cd03267 114 DSFYL-LAAIYDLPPArfkkrLDELSELLDLEELLDTPVRQLslgqrMRAEIAAAL----------LHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 167 GQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI-DKGRL 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-225 |
2.21e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 12 GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARtKMSMLFQSGALFT 91
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--AR-RIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 92 DMSVFDNIAFPLREHTKLSEALIKL---VVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQ 168
Cdd:PRK10253 95 DITVQELVARGRYPHQPLFTRWRKEdeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 169 DpISMGV-LVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK10253 175 D-ISHQIdLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-259 |
2.57e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 12 GDRTIYKNMSFSVPKGKITAIMGPSGIGKTT----MLRLIGGQlkpdaGDILFEGGSIPSMSRKELYAARTKMSMLFQ-- 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 86 SGALFTDMSVFDNIAFPLREHTK-LSEALIKLVVLMKLQAVGLRGA-KDLMPSELSGGMARRAALARAIALDPELIMYDE 163
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 164 PFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIAdHVIIIADQGVIgagtpdemrnhesplVQQflkglSDG 243
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALC-HQVIVLRQGEV---------------VEQ-----GDC 510
|
250
....*....|....*.
gi 2096624516 244 PVPFHYPAQTYADELL 259
Cdd:PRK15134 511 ERVFAAPQQEYTRQLL 526
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-141 |
4.06e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpSMSRKELYAartkm 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-RRQRDEYHQ----- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 81 SMLF---QSGaLFTDMSVFDNIAFPLREHTKLSEAliklVVLMKLQAVGLRGAKDLMPSELSGG 141
Cdd:PRK13538 75 DLLYlghQPG-IKTELTALENLRFYQRLHGPGDDE----ALWEALAQVGLAGFEDVPVRQLSAG 133
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-169 |
5.01e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.54 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI----PSMSRKELYAArt 78
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqrDSIARGLLYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 kmsmlfQSGALFTDMSVFDNIAFPLREHTKLSealiklvVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:cd03231 80 ------HAPGIKTTLSVLENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170
....*....|.
gi 2096624516 159 IMYDEPFAGQD 169
Cdd:cd03231 147 WILDEPTTALD 157
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
6.21e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPDA---GDILFEGGSI--PSMSRKELy 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNIysPDVDPIEV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 aaRTKMSMLFQSGALFTDMSVFDNIAFPLREH--TKLSEALIKLVVLMKLQAVGLRGAKDLM---PSELSGGMARRAALA 149
Cdd:PRK14267 84 --RREVGMVFQYPNPFPHLTIYDNVAIGVKLNglVKSKKELDERVEWALKKAALWDEVKDRLndyPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG-TPDEMRNH 228
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGpTRKVFENP 239
|
250
....*....|.
gi 2096624516 229 ESPLVQQFLKG 239
Cdd:PRK14267 240 EHELTEKYVTG 250
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-225 |
9.32e-19 |
|
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: 82.28 E-value: 9.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGD--RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDmSVFDNIAFPLREHTKlsEALIKLV-------VLMKL-----QAVGLRGAKdlmpseLSGGMARRAA 147
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRPGATR--EEVEEAAraanaheFIMELpegydTVIGERGVK------LSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 148 LARAIALDPELIMYDEPFAGQDPISMgvlvKLI-KSLNEVL-GLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEM 225
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESE----RLVqAALERLMkNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
1.01e-18 |
|
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: 82.20 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSF---SRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRT 78
Cdd:cd03249 1 IEFKNVSFrypSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---RS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGALFtDMSVFDNIAFPLREHTKLS-EALIKLV----VLMKL-----QAVGLRGakdlmpSELSGGMARRAAL 148
Cdd:cd03249 78 QIGLVSQEPVLF-DGTIAENIRYGKPDATDEEvEEAAKKAnihdFIMSLpdgydTLVGERG------SQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDPISMGV----LVKLIKslnevlGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDE 224
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLvqeaLDRAMK------GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
1.51e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS---RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsiPSMSRKELYAAR 77
Cdd:PRK13642 4 ILEVENLVFKyekESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQS-GALFTDMSVFDNIAFPLREHTKLSEALIKLVVlMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVD-EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-198 |
1.59e-18 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 81.71 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDR----TIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 R-TKMSMLFQSGALFTDMSVFDNIAFPL-----REHTKLSEALiklvvlmkLQAVGLRGAKDLMPSELSGGMARRAALAR 150
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLelagrRDARARARAL--------LERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2096624516 151 AIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDV 198
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-225 |
1.87e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.44 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGD------RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsIPSMSRKELY 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 AARTKMSMLFQS-GALFTDMSVFDNIAF-PlrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAI 152
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFgP--ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-225 |
2.35e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIG--GQLKPD---AGDILFEGGSIPSmSRKELYA 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYS-PRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 ARTKMSMLFQSGALFTdMSVFDNIAFPLR-----EHTKLSEALIKlvvlmklqavGLRGA------KDLMPSE---LSGG 141
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRlkgikDKQVLDEAVEK----------SLKGAsiwdevKDRLHDSalgLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 MARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLssLIVTHDVTEVMSIADHVIIIADQGVIGAGT 221
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
....
gi 2096624516 222 PDEM 225
Cdd:PRK14239 231 TKQM 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-225 |
2.77e-18 |
|
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: 81.28 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAG---DIL---FEGGSIPsmsrkELy 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVW-----EL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 aaRTKMSMLfqSGALF----TDMSV--------FDNIAFplreHTKLSEALIKLVVLMkLQAVGLRGAKDLMPSELSGG- 141
Cdd:COG1119 77 --RKRIGLV--SPALQlrfpRDETVldvvlsgfFDSIGL----YREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGe 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 ----------MarraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:COG1119 148 qrrvliaralV-----------KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
250
....*....|....
gi 2096624516 212 ADQGVIGAGTPDEM 225
Cdd:COG1119 217 KDGRVVAAGPKEEV 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
2.95e-18 |
|
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: 80.71 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTI--YKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDmSVFDNIAFPLREHT--KLSEA--LIKLVVLMKLQAVGLrgakDLMPSE----LSGGMARRAALARA 151
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGAPLADdeRILRAaeLAGVTDFVNKHPNGL----DLQIGErgrgLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 152 IALDPELIMYDEPFAGQDpisMGVLVKLIKSLNEVLGLSSLIV-THDvTEVMSIADHVIIIaDQGVI 217
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD---MNSEERLKERLRQLLGDKTLIIiTHR-PSLLDLVDRIIVM-DSGRI 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-225 |
2.96e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 81.42 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGS--------IPSMSRKE 72
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 73 LyaARTKMSMLFQSGA--LFTDMSVFDNI-----AFPLREHTKLSEALIKLvvlmkLQAVGL-RGAKDLMPSELSGGMAR 144
Cdd:TIGR02323 83 L--MRTEWGFVHQNPRdgLRMRVSAGANIgerlmAIGARHYGNIRATAQDW-----LEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 145 RAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
.
gi 2096624516 225 M 225
Cdd:TIGR02323 236 V 236
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-225 |
4.12e-18 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 80.49 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDA----GDILFEGGSIPSMSRKELyaartKMSMLFQS--GALFTD 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLtqtsGEILLDGRPLLPLSIRGR-----HIATIMQNprTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 93 MSVFDNIAFPLREHTKLSEALIKLVVlMKLQAVGLRGAKDLM---PSELSGGMARRAALARAIALDPELIMYDEPFAGQD 169
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLSKQARALIL-EALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 170 PISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
5.19e-18 |
|
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: 83.10 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRT-IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAFPLREHT--KLSEALiKLVVLMKLQAvGLRGAKDLM----PSELSGGMARRAALARAIAL 154
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDASdaEIREAL-ERAGLDEFVA-ALPQGLDTPigegGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDvTEVMSIADHVIII 211
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-241 |
6.93e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI-----------LFEGGSIPSMSRK--ELYAARTKMSMLFQ 85
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkkNNHELITNPYSKKikNFKELRRRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 86 --SGALFTDmSVFDNIAF-PLREHTKLSEAliKLVVLMKLQAVGLRGA-KDLMPSELSGGMARRAALARAIALDPELIMY 161
Cdd:PRK13631 124 fpEYQLFKD-TIEKDIMFgPVALGVKKSEA--KKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSlNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE--MRNH-------ESPL 232
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEifTDQHiinstsiQVPR 279
|
....*....
gi 2096624516 233 VQQFLKGLS 241
Cdd:PRK13631 280 VIQVINDLI 288
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-210 |
7.04e-18 |
|
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: 82.42 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKD--VSFSRGDRT--IYKNMSFSVPKGKITAIMGPSGIGKT----TMLRLIGGQLKPDAGDILFEGGSIPSMSRKELY 74
Cdd:COG4172 8 SVEDlsVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 AAR-TKMSMLFQ--SGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLM---PSELSGGMARRAAL 148
Cdd:COG4172 88 RIRgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDpismgVLV-----KLIKSLNEVLGLSSLIVTHDVTEVMSIADHVII 210
Cdd:COG4172 168 AMALANEPDLLIADEPTTALD-----VTVqaqilDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-225 |
9.88e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpSMSRKELYAARTKM 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQ---SGALFTDMSvfDNIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:PRK13638 80 ATVFQdpeQQIFYTDID--SDIAFSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-225 |
1.81e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRT-IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsIPSMSRKELYAARTK 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGAL-FTDMSVFDNIAF-PlrEHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPE 157
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFgP--ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEvMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENV 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-141 |
2.25e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrkELYAARTKM 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEAC 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLR----EHTKLSEAliklvvlmkLQAVGLRGAKDLMPSELSGG 141
Cdd:PRK13539 76 HYLGHRNAMKPALTVAENLEFWAAflggEELDIAAA---------LEAVGLAPLAHLPFGYLSAG 131
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-250 |
4.82e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.63 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSR-KELYAARTKMSMLFQ--SGALFtDMSV 95
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQfpESQLF-EETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 96 FDNIAF-PlrEHTKLSEALIKLVVLMKLQAVGLrgAKDLM---PSELSGGMARRAALARAIALDPELIMYDEPFAGQDPI 171
Cdd:PRK13649 104 LKDVAFgP--QNFGVSQEEAEALAREKLALVGI--SESLFeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 172 SMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNH----ES-----PLVQQFLKGLSD 242
Cdd:PRK13649 180 GRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdflEEkqlgvPKITKFAQRLAD 258
|
....*....
gi 2096624516 243 GPVPF-HYP 250
Cdd:PRK13649 259 RGISFsSLP 267
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-252 |
1.19e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARtKMSML 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF--AR-KVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 84 FQSGALFTDMSVFDNIA------------FPLREHTKLSEAlIKLVVLMKLqavglrgAKDLMPSeLSGGMARRAALARA 151
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEA-ISLVGLKPL-------AHRLVDS-LSGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 152 IALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHEsp 231
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE-- 239
|
250 260
....*....|....*....|.
gi 2096624516 232 lVQQFLKGLSDGPVPfhYPAQ 252
Cdd:PRK10575 240 -TLEQIYGIPMGILP--HPAG 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-223 |
1.34e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.89 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGS-----IPSMSRKELYA-AR 77
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAERRRlLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQSGA--LFTDMSVFDNIAFPL-----REHTKLSEALIKLvvlmkLQAVGLRGAK-DLMPSELSGGMARRAALA 149
Cdd:PRK11701 89 TEWGFVHQHPRdgLRMQVSAGGNIGERLmavgaRHYGDIRATAGDW-----LERVEIDAARiDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPD 223
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-58 |
1.70e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.62 E-value: 1.70e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-227 |
2.28e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.52 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSvpKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSmsrkELYAARTKMSMLFQSGALFTDMSVFDN 98
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 IAFPLREHTK-LSEALIKLVVLmkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLV 177
Cdd:TIGR01257 1024 ILFYAQLKGRsWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2096624516 178 KLIksLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRN 227
Cdd:TIGR01257 1102 DLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-216 |
2.46e-16 |
|
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: 74.56 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGD--RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:cd03246 2 EVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIafplrehtklsealiklvvlmklqavglrgakdlmpseLSGGMARRAALARAIALDPELIM 160
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNeVLGLSSLIVTHDvTEVMSIADHVIIIADQGV 216
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
3.02e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFeggsipsmsrkelyAARTKM 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------------GETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALF-TDMSVFDNIAfplREHTKLSEALIKLVvlmkLQAVGLRGAKDLMP-SELSGGMARRAALARAIALDPEL 158
Cdd:COG0488 381 GYFDQHQEELdPDKTVLDELR---DGAPGGTEQEVRGY----LGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 159 IMYDEPfagqDPISMGVLVKLIKSLNEVLglssLIVTHDVTEVMSIADHVIIIADQGVI 217
Cdd:COG0488 454 LLLDEPtnhlDIETLEALEEALDDFPGTV----LLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-218 |
4.58e-16 |
|
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: 73.23 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMS 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQsgalftdmsvfdniafplrehtkLSEALIKLVVLmklqavglrgAKDLMpselsggmarraalaraiaLDPELIMY 161
Cdd:cd03216 79 MVYQ-----------------------LSVGERQMVEI----------ARALA-------------------RNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 162 DEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIG 218
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-242 |
6.45e-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: 76.76 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPDAGDILFE------------------ 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 62 -----GGSIPS-------MSRKELYAARTKMSMLFQ-SGALFTDMSVFDNIAFPLRE-HTKLSEALIKLVVLMKLQAVGL 127
Cdd:TIGR03269 81 pcpvcGGTLEPeevdfwnLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEiGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 128 RGAKdlMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLsSLIVTHDVTEVMS-IAD 206
Cdd:TIGR03269 161 RITH--IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGI-SMVLTSHWPEVIEdLSD 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 2096624516 207 HVIIIADQGVIGAGTPDEmrnhespLVQQFLKGLSD 242
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDE-------VVAVFMEGVSE 266
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-211 |
7.32e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.42 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 12 GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSM--SRKELYAA-----RTKMSM-L 83
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYvpQRSEVPDSlpltvRDLVAMgR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 84 FQSgalftdmsvfdniAFPLREHTKLSEAliklVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDE 163
Cdd:NF040873 83 WAR-------------RGLWRRLTRDDRA----AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2096624516 164 PFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSiADHVIII 211
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-58 |
7.36e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.90 E-value: 7.36e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-224 |
9.71e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAArtkmsMLFQSGALFTDMSVFD 97
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA-----MVFQNYALYPHMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIAFPLReHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDpismgvlV 177
Cdd:PRK11650 96 NMAYGLK-IRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-------A 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 178 KL-------IKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVI-GAGTPDE 224
Cdd:PRK11650 168 KLrvqmrleIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM-NGGVAeQIGTPVE 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-224 |
1.95e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyaARTKM 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAF---PLR----EHTKLSEAliklVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIA 153
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMgrtPHRsrfdTWTETDRA----AVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 154 LDPELIMYDEPFAGQDpISMGV-LVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:PRK09536 156 QATPVLLLDEPTASLD-INHQVrTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-120 |
3.44e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFSRGDRTIYKNMSFSVPKG-KItAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGsipsmsrkelyaarTKMSM 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------------LRIGY 65
|
90 100 110
....*....|....*....|....*....|....*...
gi 2096624516 83 LFQSGALFTDMSVFDNIAFPLREHTKLSEALIKLVVLM 120
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRALEAELEELEAKL 103
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-220 |
3.79e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 71.19 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRG--DRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFeGGSIPSMSRKELyaaRTK 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-DGVPVSDLEKAL---SSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFtDMSVFDNIafplrehtklsealiklvvlmklqavGLRgakdlmpseLSGGMARRAALARAIALDPELI 159
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNL--------------------------GRR---------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEvMSIADHVIIIADQGVIGAG 220
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTG-IEHMDKILFLENGKIIMQG 178
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-210 |
8.38e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMSMLFQS--GALFTDMSVFDN 98
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 IAFPLREHTKLSEALIKLVVLMKLQAVGLRGAK-DLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQD-PISMGVL 176
Cdd:PRK11308 115 LEEPLLINTSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVL 194
|
170 180 190
....*....|....*....|....*....|....
gi 2096624516 177 vKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVII 210
Cdd:PRK11308 195 -NLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-196 |
1.36e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 70.25 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPDAGDILFEGGSIPSMSRKElyAARTKM 80
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEE--RARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDniaFpLREhtkLSEAliklvvlmklqavglrgakdlmpseLSGGMARRAALARAIALDPELIM 160
Cdd:cd03217 80 FLAFQYPPEIPGVKNAD---F-LRY---VNEG-------------------------FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTH 196
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH 162
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
1.47e-14 |
|
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: 72.78 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSR-GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFtDMSVFDNIAFPLREHT--KLSEAliklvvlmkLQAVGL----RGAKDLMPSE-------LSGGMARRAA 147
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRLARPDATdeELWAA---------LERVGLadwlRALPDGLDTVlgeggarLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 148 LARAIALDPELIMYDEPFAGQDPismGVLVKLIKSLNEVL-GLSSLIVTHD 197
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDA---ETADELLEDLLAALsGRTVVLITHH 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-228 |
3.96e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTkm 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 smlfqsgaLFTDMSVFdniaFPLREHTKLSEALiklVVLMKLQAVGLRGAKdlmPSELSGGMARRAALARAIALDPELIM 160
Cdd:PRK09544 82 --------LPLTVNRF----LRLRPGTKKEDIL---PALKRVQAGHLIDAP---MQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 161 YDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVIGAGTPDEMRNH 228
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLH 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-217 |
4.73e-14 |
|
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: 69.42 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS---RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRT 78
Cdd:cd03248 12 VKFQNVTFAyptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL---HS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGALFTDmSVFDNIAFPLR--EHTKLSEALIKL---VVLMKLQA-----VGLRGakdlmpSELSGGMARRAAL 148
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYGLQscSFECVKEAAQKAhahSFISELASgydteVGEKG------SQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSiADHVIIIaDQGVI 217
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVL-DGGRI 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
5.53e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsRKELYAARTKM 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLreHTKLSEALI-KLVVLMKLQAVglrgaKDLMPSELSGGMARRAALARAIALDPELI 159
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDI--HFSPGAVGItELCRLFSLEHL-----IDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 2096624516 160 MYDEPFAGQDPISMGVLVKLIKSlNEVLGLSSLIVTH 196
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-58 |
6.74e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.09 E-value: 6.74e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-253 |
7.12e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 7 VSFSRGD--RTIYKNMSFSVPKGKITAIMGPSGIGKT----TMLRLIggqlkPD------AGDILFEGGSIPSMSRKELY 74
Cdd:PRK15134 13 VAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 AAR-TKMSMLFQSGalFTDMSVFDNIAFPLRE----HTKLSEALIKLVVLMKLQAVGLRGAKDLM---PSELSGGMARRA 146
Cdd:PRK15134 88 GVRgNKIAMIFQEP--MVSLNPLHTLEKQLYEvlslHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 147 ALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMR 226
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250 260
....*....|....*....|....*....
gi 2096624516 227 NH-ESPLVQQFLKGLSDG-PVPFHYPAQT 253
Cdd:PRK15134 246 SApTHPYTQKLLNSEPSGdPVPLPEPASP 274
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-213 |
7.13e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPDAGDILFEGGSIPSMS---RkelyaAR 77
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSpdeR-----AR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQSGALFTDMSVFD--NIAFPLREHTKLSEALIKLVVLMKLQAVGLrgAKDLMPSEL----SGG---------M 142
Cdd:COG0396 77 AGIFLAFQYPVEIPGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGL--DEDFLDRYVnegfSGGekkrneilqM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 143 ARRaalaraialDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTH-----DVTEvmsiADHVIIIAD 213
Cdd:COG0396 155 LLL---------EPKLAILDETDSGLDIDALRIVAEGVNKLRS-PDRGILIITHyqrilDYIK----PDFVHVLVD 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-225 |
1.03e-13 |
|
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: 68.67 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS-RGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:cd03252 1 ITFEHVRFRyKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFtDMSVFDNIAF-----PLR---EHTKLSEA--LIKLVVLMKLQAVGLRGAKdlmpseLSGGMARRAALA 149
Cdd:cd03252 78 VGVVLQENVLF-NRSIRDNIALadpgmSMErviEAAKLAGAhdFISELPEGYDTIVGEQGAG------LSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEM 225
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-226 |
1.72e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.75 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS---RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRT 78
Cdd:TIGR00958 479 IEFQDVSFSypnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL---HR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSGALFTDmSVFDNIAFPLREHTKLsealiklvvlMKLQAVGLRGAKDL---MP-----------SELSGGMAR 144
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGLTDTPDE----------EIMAAAKAANAHDFimeFPngydtevgekgSQLSGGQKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 145 RAALARAIALDPELIMYDEPFAGQDPISMgvlvKLIKSLNEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDE 224
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQ 699
|
..
gi 2096624516 225 MR 226
Cdd:TIGR00958 700 LM 701
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-211 |
1.84e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 9 FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTT----MLRLIGGQlkpdAGDILFEGGSIPSMSRKELYAARTKMSM 82
Cdd:PRK10261 330 LNRVTREVHavEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQ----GGEIIFNGQRIDTLSPGKLQALRRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQS--GALFTDMSVFDNIAFPLREHTKLS-EALIKLVVLMkLQAVGLRGAKDL-MPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK10261 406 IFQDpyASLDPRQTVGDSIMEPLRVHGLLPgKAAAARVAWL-LERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-211 |
3.56e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKD--VSFSR--GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPD---AGDILFEGGSIPSMSRKEL 73
Cdd:PRK09473 12 LLDVKDlrVTFSTpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 74 YAART-KMSMLFQS--GALFTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLM---PSELSGGMARRAA 147
Cdd:PRK09473 92 NKLRAeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 148 LARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-196 |
3.99e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.41 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 6 DVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSmsrkelyAARTK-MSMLF 84
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-------GDRSRfMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 85 QSGALFTDMSVFDNIAFPLREHTKLSEALIKlvvlMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEP 164
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGRRAKQMPG----SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190
....*....|....*....|....*....|..
gi 2096624516 165 FAGQDPISMGVLVKLIKSLNEVLGlSSLIVTH 196
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHLRGGG-AALVTTH 195
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-220 |
4.49e-13 |
|
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: 66.04 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 5 KDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKP--DAGDILFEGgsipSMSRKELYAARTKMSM 82
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLING----RPLDKRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 lfQSGALFTDMSVFDNIAFplrehtklsealiklvvlmklqAVGLRGakdlmpseLSGGMARRAALARAIALDPELIMYD 162
Cdd:cd03213 89 --QDDILHPTLTVRETLMF----------------------AAKLRG--------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 163 EPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDV-TEVMSIADHVIIIADQGVIGAG 220
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-183 |
5.84e-13 |
|
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: 66.14 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 11 RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDA---GDILFEGgsipsmsrKELYAARTK--MSMLFQ 85
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG--------QPRKPDQFQkcVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 86 SGALFTDMSVFDNIAF--PLREHTKLSEALI-KLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYD 162
Cdd:cd03234 89 DDILLPGLTVRETLTYtaILRLPRKSSDAIRkKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180
....*....|....*....|.
gi 2096624516 163 EPFAGQDPISMGVLVKLIKSL 183
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQL 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
5.97e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkELYAARTKM 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFPLREH----TKLSEALIKLVVLMKL--QAVGLRGAKDLMPSELSGGMarraalaraiaL 154
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPKRqasmQKMKQLLAALGCQLDLdsSAGSLEVADRQIVEILRGLM-----------R 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 155 DPELIMYDEPFAGQDPISMGVLVKLIKSLnEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-213 |
1.50e-12 |
|
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: 64.38 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIyknmSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKM 80
Cdd:cd03215 4 VLEVRGLSVKGAVRDV----SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--AIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SML----FQSGaLFTDMSVFDNIAfplrehtklsealiklvvlmklqavglrgakdlMPSELSGG----------Marra 146
Cdd:cd03215 78 AYVpedrKREG-LVLDLSVAENIA---------------------------------LSSLLSGGnqqkvvlarwL---- 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 147 alaraiALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:cd03215 120 ------ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE 179
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-225 |
1.67e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMSMLFQSGALFTDMSVFD 97
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD--AQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIAFPL----------REHTKLSEALiklvvlmkLQAVGL-----RGAKDLMPSE---------LSggmarraalaraia 153
Cdd:COG1129 99 NIFLGReprrgglidwRAMRRRAREL--------LARLGLdidpdTPVGDLSVAQqqlveiaraLS-------------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 154 LDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM 225
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
2.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVS--FSRGDRTIYK---NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI--------------LFEG 62
Cdd:PRK13651 3 IKVKNIVkiFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 63 GSI-----PSMSR--KELYAARTKMSMLFQsgalFTDMSVFD-----NIAF-PLREHTKLSEALIKLVVLMKLqaVGL-R 128
Cdd:PRK13651 83 VLEklviqKTRFKkiKKIKEIRRRVGVVFQ----FAEYQLFEqtiekDIIFgPVSMGVSKEEAKKRAAKYIEL--VGLdE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 129 GAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHV 208
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRT 235
|
250 260 270
....*....|....*....|....*....|
gi 2096624516 209 IIIADQGVIGAGTPDEMRNHESPLVQQFLK 238
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSDNKFLIENNME 265
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-224 |
3.59e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILF-EGGSIPSMSRkelyaartkm 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsENANIGYYAQ---------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 smlfQSGALF-TDMSVFDNIAFPLREhtKLSEALIKlVVLMKLqavgLRGAKDLMPS--ELSGGMARRAALARAIALDPE 157
Cdd:PRK15064 390 ----DHAYDFeNDLTLFDWMSQWRQE--GDDEQAVR-GTLGRL----LFSQDDIKKSvkVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 158 LIMYDEPFAGQDPISmgvlvklIKSLNEVLGL--SSLI-VTHDVTEVMSIADHVIIIADQGVIG-AGTPDE 224
Cdd:PRK15064 459 VLVMDEPTNHMDMES-------IESLNMALEKyeGTLIfVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-240 |
4.56e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDV--SFSRGDRTI--YKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA 76
Cdd:PRK10535 4 LLELKDIrrSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 RTK-MSMLFQSGALFTDMSVFDNIAFP-----LREHTKLSEAliklvvLMKLQAVGLRGAKDLMPSELSGGMARRAALAR 150
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPavyagLERKQRLLRA------QELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 151 AIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDvTEVMSIADHVIIIADQGVI----------GAG 220
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHD-PQVAAQAERVIEIRDGEIVrnppaqekvnVAG 235
|
250 260
....*....|....*....|
gi 2096624516 221 TPDEMrNHESPLVQQFLKGL 240
Cdd:PRK10535 236 GTEPV-VNTASGWRQFVSGF 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-226 |
4.87e-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: 63.97 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 26 KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELY-AARTKMS---MLFQSGALFTDMSVFDN-IA 100
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKPQYiKADYEGTvrdLLSSITKDFYTHPYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 101 FPLrehtklsealiKLVVLMKLQAvglrgakdlmpSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLI 180
Cdd:cd03237 101 KPL-----------QIEQILDREV-----------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2096624516 181 KSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQ-GVIG-AGTPDEMR 226
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEpSVNGvANPPQSLR 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-58 |
5.40e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 5.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 3 EVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-227 |
1.20e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.11 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 20 MSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDA---GDILFEGGSIPSMSR--KELYAARTKMSMLFQSGALFTDMS 94
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRlaRDIRKSRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 95 VFDNI------AFPL-REHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAG 167
Cdd:PRK09984 103 VLENVligalgSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 168 QDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRN 227
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-221 |
1.24e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSrkelYAART-KMSMLFQ--SGALFTDMS 94
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSqRIRMIFQdpSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 95 VFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLR-GAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISM 173
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2096624516 174 GVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGT 221
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-259 |
2.55e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKT----TMLRLI---GGQLKpdAGDILFEGGSIPSMSRKELYAARTK------MSMLF 84
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQ--CDKMLLRRRSRQVIELSEQSAAQMRhvrgadMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 85 QS--GALFTDMSVFDNIAFPLREHTKLS--EALIKLVVLmkLQAVGLRGAKDLM---PSELSGGMARRAALARAIALDPE 157
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQGASreEAMVEAKRM--LDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMrnhesplvqqfl 237
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI------------ 256
|
250 260
....*....|....*....|..
gi 2096624516 238 kglsdgpvpFHYPAQTYADELL 259
Cdd:PRK10261 257 ---------FHAPQHPYTRALL 269
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-65 |
4.99e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 4.99e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQlkPD----AGDILFEGGSI 65
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESI 73
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-225 |
7.02e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:PRK13657 335 VEFDDVSFSyDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFtDMSVFDNIAF--------PLREHTKLSEAL-IKLVVLMKLQA-VGLRGakdlmpSELSGGMARRAALAR 150
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIRVgrpdatdeEMRAAAERAQAHdFIERKPDGYDTvVGERG------RQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 151 AIALDPELIMYDEPFAGQDPISMgvlVKLIKSLNEVL-GLSSLIVTHDVTEVMSiADhVIIIADQG-VIGAGTPDEM 225
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETE---AKVKAALDELMkGRTTFIIAHRLSTVRN-AD-RILVFDNGrVVESGSFDEL 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-258 |
1.15e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 11 RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPD---AGDILFEGGSIpsmSRKELyaarTKMSMLFQSG 87
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEM----RAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 88 ALFT-DMSVFDNIAFP--LREHTKLSEALIKLVVLMKLQAVGLR-------GAKDLMPSeLSGGMARRAALARAIALDPE 157
Cdd:TIGR00955 108 DLFIpTLTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVT-EVMSIADHVIIIADQGVIGAGTPDEmrnhespLVQQF 236
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQ-------AVPFF 258
|
250 260
....*....|....*....|...
gi 2096624516 237 LKGlsDGPVPFHY-PAQTYADEL 258
Cdd:TIGR00955 259 SDL--GHPCPENYnPADFYVQVL 279
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
1.33e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS-------------------FSRGDRTIY--KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDIL 59
Cdd:COG4586 1 IIEVENLSktyrvyekepglkgalkglFRREYREVEavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 60 FeGGSIPSMSRKELyaARtKMSMLF-QSGALFTDMSVFDNIAFpLREHTKLSEALIK-----LVVLMKL-----QAV--- 125
Cdd:COG4586 81 V-LGYVPFKRRKEF--AR-RIGVVFgQRSQLWWDLPAIDSFRL-LKAIYRIPDAEYKkrldeLVELLDLgelldTPVrql 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 126 --GLRgakdlMPSELSGGMarraalaraiALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMS 203
Cdd:COG4586 156 slGQR-----MRCELAAAL----------LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEA 220
|
250 260
....*....|....*....|....*.
gi 2096624516 204 IADHVIIIaDQG-VIGAGTPDEMRNH 228
Cdd:COG4586 221 LCDRVIVI-DHGrIIYDGSLEELKER 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-198 |
2.59e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 15 TIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTK-MSMLFQSGALFTDM 93
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 94 SVFDNIAFP--LREHtklSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPI 171
Cdd:PRK10584 104 NALENVELPalLRGE---SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*..
gi 2096624516 172 SMGVLVKLIKSLNEVLGLSSLIVTHDV 198
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-217 |
3.84e-10 |
|
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: 58.31 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 9 FSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPsmsrkelyaartkmsMLFQSGA 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---------------LLGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 89 LFTDMSVFDNIAFPLREHtKLSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQ 168
Cdd:cd03220 95 FNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 169 DPISMgvlVKLIKSLNEVL--GLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:cd03220 174 DAAFQ---EKCQRRLRELLkqGKTVILVSHDPSSIKRLCDRALVL-EKGKI 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-224 |
4.04e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 4 VKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTKMSM 82
Cdd:PRK15056 9 VNDVTVTwRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQSGALFTD----MSVFDNIAFpLREHTKLSEAliklVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:PRK15056 89 VDWSFPVLVEdvvmMGRYGHMGW-LRRAKKRDRQ----IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIadQGVIGAGTPDE 224
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV--KGTVLASGPTE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-103 |
4.31e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSF---SRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSipSMSRKELYAART 78
Cdd:PTZ00265 383 IQFKNVRFhydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRS 460
|
90 100
....*....|....*....|....*
gi 2096624516 79 KMSMLFQSGALFTDmSVFDNIAFPL 103
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSL 484
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-235 |
6.39e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.07 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRT--IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDmSVFDN--IAFPLREHTKLSEALIKlVVLMKL--QAVGLrgakDLMPSE----LSGGMARRAALARA 151
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNllLAAPNASDEALIEVLQQ-VGLEKLleDDKGL----NAWLGEggrqLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 152 IALDPELIMYDEPFAGQDPIS----MGVLVKLIKslnevlGLSSLIVTHDVTEVMSIaDHVIIIADQGVIGAGtpdemrN 227
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQ------NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG------T 556
|
....*...
gi 2096624516 228 HESPLVQQ 235
Cdd:PRK11160 557 HQELLAQQ 564
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
7.30e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelYAARTKM 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIaFPLREHTK-------LSEALIKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIA 153
Cdd:PRK09700 83 GIIYQELSVIDELTVLENL-YIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 154 LDPELIMYDEPFAGQDPISMGVLVKLIKSL-NEvlGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEMRNHE 229
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrKE--GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDD 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-219 |
9.37e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.35 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 23 SVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFeGGSIPSMSRKELYAA--RTKMSMLFQSGALFTDMSVFDNIA 100
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGICLPpeKRRIGYVFQDARLFPHYKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 101 FPLREhtKLSEALIKLVVLMKLQAVGLRgakdlMPSELSGGMARRAALARAIALDPELIMYDEPFAGQD-PIS---MGVL 176
Cdd:PRK11144 99 YGMAK--SMVAQFDKIVALLGIEPLLDR-----YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKrelLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2096624516 177 VKLIKSLNevlgLSSLIVTHDVTEVMSIADHVIIIaDQGVIGA 219
Cdd:PRK11144 172 ERLAREIN----IPILYVSHSLDEILRLADRVVVL-EQGKVKA 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-225 |
1.05e-09 |
|
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: 58.22 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSF--SRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKEL-----Y 74
Cdd:COG4618 331 LSVENLTVvpPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhigY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 75 aartkmsmLFQSGALFtDMSVFDNIAfplrehtKLSEALIKLVVlmklQAVGLRGAKDL---MP-----------SELSG 140
Cdd:COG4618 411 --------LPQDVELF-DGTIAENIA-------RFGDADPEKVV----AAAKLAGVHEMilrLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 141 G----------MarraalaraiALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDvTEVMSIADHVII 210
Cdd:COG4618 471 GqrqriglaraL----------YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHR-PSLLAAVDKLLV 538
|
250
....*....|....*
gi 2096624516 211 IADQGVIGAGTPDEM 225
Cdd:COG4618 539 LRDGRVQAFGPRDEV 553
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-210 |
1.09e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSfsRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSmsRKELYAARTKMSM 82
Cdd:PRK09700 267 EVRNVT--SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 LFQS---GALFTDMSVFDNIA----------------FPLREHTKLSEALIKLVVLmKLQAVglrgakDLMPSELSGGMA 143
Cdd:PRK09700 343 ITESrrdNGFFPNFSIAQNMAisrslkdggykgamglFHEVDEQRTAENQRELLAL-KCHSV------NQNITELSGGNQ 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 144 RRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVII 210
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAV 481
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-62 |
1.85e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.63 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVS----------------FSRGDRTIY------KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:COG1134 4 MIEVENVSksyrlyhepsrslkelLLRRRRTRReefwalKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
....
gi 2096624516 59 LFEG 62
Cdd:COG1134 84 EVNG 87
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-67 |
1.86e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.86e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 7 VSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLK--PDAGDILFEGGSIPS 67
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR 98
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-100 |
2.24e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS-RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:PRK10790 341 IDIDNVSFAyRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGV 417
|
90 100
....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIA 100
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVT 436
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-225 |
2.61e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDA--------GDILFEGGSIPSMSRKE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 73 LYAARTKMSMLFQSGALFtdmSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPSE---LSGG-------- 141
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAF---SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDvttLSGGelarvqfa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 142 -MARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAG 220
Cdd:PRK13547 158 rVLAQLWPPHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
....*
gi 2096624516 221 TPDEM 225
Cdd:PRK13547 238 APADV 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-217 |
2.73e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 13 DRTIYKNMSFSVPKGKITAIMGPSGIGKT----TMLRLIGGQLKPDAGDILFEGGSI-PSMSRKELYAarTKMSmlfqsg 87
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVaPCALRGRKIA--TIMQ------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 88 alfTDMSVFDniafPLRE-HTKLSEALIKL-------VVLMKLQAVGLRGAK---DLMPSELSGGMARRAALARAIALDP 156
Cdd:PRK10418 87 ---NPRSAFN----PLHTmHTHARETCLALgkpaddaTLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 157 ELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIaDQGVI 217
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVM-SHGRI 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-240 |
3.93e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.29 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKT----TMLRLIGGQLKPDAGDILFEGGSIPSMSRKE---LYAArtKMSMLFQSG--AL 89
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKErrnLVGA--EVAMIFQDPmtSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 90 FTDMSVFDNIAFPLREHTKLSEALIKLVVLMKLQAVGL---RGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFA 166
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 167 GQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDEM-RNHESPLVQQFLKGL 240
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIfRAPRHPYTQALLRAL 257
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-213 |
1.10e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAArtKMSMLFQSGALFTDMSVFDN 98
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA--GVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 I---AFPLReHTKLSEALIKLVVLMKLQAVGLrgakDLMPS----ELSGGMARRAALARAIALDPELIMYDEPFAGQDPI 171
Cdd:PRK11288 100 LylgQLPHK-GGIVNRRLLNYEAREQLEHLGV----DIDPDtplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2096624516 172 SMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:PRK11288 175 EIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKD 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-206 |
1.12e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaARTKM 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAFP--LREHTKLSEALIKLVVLM-KLQAVGLRGAkdlmpSELSGGMARRAALARAIALDPE 157
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGgfFAERDQFQERIKWVYELFpRLHERRIQRA-----GTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2096624516 158 LIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIAD 206
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLAD 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-224 |
1.23e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMSMLFQSGALFTDMSVFD 97
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD--AIALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIAfpL-REHTK-----LSEALIKLVVLMklQAVGLRGAKDLMPSELSGGMarraalaraialDPELIMYDEPFAgqdpi 171
Cdd:COG3845 100 NIV--LgLEPTKggrldRKAARARIRELS--ERYGLDVDPDAKVEDLSVGEqqrveilkalyrGARILILDEPTA----- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 172 smgVLV-----KLIKSLNEV--LGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:COG3845 171 ---VLTpqeadELFEILRRLaaEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-218 |
1.27e-08 |
|
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: 55.22 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGqLKPDA---GDILFEGGSIPSMSRKElyAAR 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRD--TER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 78 TKMSMLFQSGALFTDMSVFDNIaFPLREHT----KLSEALIKLVVLMKLQAVGLRGAKDLMP-SELSGGMARRAALARAI 152
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENI-FLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIG 218
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-213 |
1.78e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSfsrgDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMSM 82
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 83 L----FQSGaLFTDMSVFDNIAFP-LREHTK---LSEALIKLVVLMKLQAVGLRGAKDLMP-SELSGG----------Ma 143
Cdd:COG1129 332 VpedrKGEG-LVLDLSIRENITLAsLDRLSRgglLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGnqqkvvlakwL- 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 144 rraalaraiALDPELIMYDEPFAGQDpismgvlV-------KLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:COG1129 410 ---------ATDPKVLILDEPTRGID-------VgakaeiyRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-100 |
1.96e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMsrkELYAARTKMS 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLA 392
|
90
....*....|....*....
gi 2096624516 82 MLFQSGALFTDmSVFDNIA 100
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNIA 410
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-224 |
5.05e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLkPDAGDILFEGGSIPSMSRKELYAARTKMSMlfQSGALFTdMSVFDNIA 100
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQ--QQTPPFA-MPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 101 fpLREHTKLSEALIKLVVLMKLQAVGLrgaKDLMP---SELSGG-----MARRAALARAIALDPE--LIMYDEPFAGQDP 170
Cdd:PRK03695 92 --LHQPDKTRTEAVASALNEVAEALGL---DDKLGrsvNQLSGGewqrvRLAAVVLQVWPDINPAgqLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 171 ISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIGAGTPDE 224
Cdd:PRK03695 167 AQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-213 |
8.41e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMSMLFQSGALFTDMSVFDN 98
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 99 I---AFPLR----EHTKLSEALIKLVVLMKLqavglrgakDLMPSE----LSGGMARRAALARAIALDPELIMYDEPFAG 167
Cdd:PRK10982 94 MwlgRYPTKgmfvDQDKMYRDTKAIFDELDI---------DIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2096624516 168 QDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRD 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-226 |
9.32e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 26 KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEggsiPSMSRKELYAARTkmsmlfqsgalfTDMSVFDNiafpLRE 105
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKPQYIKPD------------YDGTVEDL----LRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 106 HT-KLSEALIKLVVLMKLQavglrgAKDLMPS---ELSGGMARRAALARAIALDPELIMYDEPFAGQDpISMGVLV-KLI 180
Cdd:PRK13409 424 ITdDLGSSYYKSEIIKPLQ------LERLLDKnvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRLAVaKAI 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2096624516 181 KSLNEVLGLSSLIVTHDVTEVMSIADHVII-IADQGVIG-AGTPDEMR 226
Cdd:PRK13409 497 RRIAEEREATALVVDHDIYMIDYISDRLMVfEGEPGKHGhASGPMDMR 544
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-211 |
9.76e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.22 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPD----AGDILFEGGSIPSMSRKElyaaRTK-----MSMLFQ--SG 87
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRE----RRKiigreIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 88 ALFTDMSVFDNIAFPL-----------REHTKLSEAlIKLvvlmkLQAVGLRGAKDLM---PSELSGGMARRAALARAIA 153
Cdd:COG4170 101 CLDPSAKIGDQLIEAIpswtfkgkwwqRFKWRKKRA-IEL-----LHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 154 LDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-211 |
1.10e-07 |
|
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: 52.13 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLR-LIGGQLKPDAGDILFEGGsiPSMSRKELYAARTKMSMLFQS---GALFTDMS 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGK--PVDIRNPAQAIRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 95 VFDNIAFP-LREHTKLS---EALIKLVVLMKLQAVGLRGAKDLMP-SELSGGMARRAALARAIALDPELIMYDEPFAGQD 169
Cdd:TIGR02633 356 VGKNITLSvLKSFCFKMridAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2096624516 170 PISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-63 |
1.28e-07 |
|
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: 50.55 E-value: 1.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 2 VEVKDVSFSRGDR-----TIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGG 63
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-60 |
4.14e-07 |
|
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: 48.69 E-value: 4.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2096624516 2 VEVKDVSFSRGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGqL---------KPDAGDILF 60
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LwpwgsgrigMPEGEDLLF 68
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-57 |
6.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 6.20e-07
10 20 30
....*....|....*....|....*....|....*
gi 2096624516 24 VPK-GKITAIMGPSGIGKTTMLRLIGGQLKPDAGD 57
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGD 129
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-238 |
7.29e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSF---SRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPD---------------------- 54
Cdd:PTZ00265 1166 IEIMDVNFryiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 55 ------------------------------AGDILFEGGSIPSMSRKELyaaRTKMSMLFQSGALFtDMSVFDNIAFPlR 104
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDL---RNLFSIVSQEPMLF-NMSIYENIKFG-K 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 105 EHTKLSEA--LIKLVVLMK-LQAVGLRGAKDLMP--SELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVLVKL 179
Cdd:PTZ00265 1321 EDATREDVkrACKFAAIDEfIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 180 IKSLNEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGA-----GTPDEMRNHESPLVQQFLK 238
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDRTGSfvqahGTHEELLSVQDGVYKKYVK 1463
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-197 |
7.51e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSR-GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILfeggsipsmsrkelYAARTK 79
Cdd:PLN03073 508 IISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------------RSAKVR 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDMSVFdniafPLREHTKLSEALIKLVVLMKLQAVGLRGAKDLMPS-ELSGGMARRAALARAIALDPEL 158
Cdd:PLN03073 574 MAVFSQHHVDGLDLSSN-----PLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190
....*....|....*....|....*....|....*....
gi 2096624516 159 IMYDEPfagQDPISMGVLVKLIKSLNEVLGlSSLIVTHD 197
Cdd:PLN03073 649 LLLDEP---SNHLDLDAVEALIQGLVLFQG-GVLMVSHD 683
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-58 |
8.21e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 8.21e-07
10 20 30
....*....|....*....|....*....|....*.
gi 2096624516 24 VPK-GKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDY 130
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-225 |
1.03e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSF--SRGDRTIyKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAA---- 76
Cdd:COG3845 259 EVENLSVrdDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvay 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 77 ----RTKMsmlfqsgALFTDMSVFDNIAFPLREHTKLSEALIklvvlMKLQAVGLRgAKDLM-------PSE------LS 139
Cdd:COG3845 338 ipedRLGR-------GLVPDMSVAENLILGRYRRPPFSRGGF-----LDRKAIRAF-AEELIeefdvrtPGPdtparsLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 140 GG----------MArraalaraiaLDPELIMYDEPFAGQDPISM----GVLVKLIKSlnevlGLSSLIVTHDVTEVMSIA 205
Cdd:COG3845 405 GGnqqkvilareLS----------RDPKLLIAAQPTRGLDVGAIefihQRLLELRDA-----GAAVLLISEDLDEILALS 469
|
250 260
....*....|....*....|
gi 2096624516 206 DHVIIIADQGVIGAGTPDEM 225
Cdd:COG3845 470 DRIAVMYEGRIVGEVPAAEA 489
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-60 |
1.73e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 48.65 E-value: 1.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGD-RTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG---------QLkPDAGDILF 60
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgriAR-PAGARVLF 430
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-58 |
2.23e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 2.23e-06
10 20 30
....*....|....*....|....*....|...
gi 2096624516 26 KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV 397
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-226 |
2.80e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.20 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAARTkms 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 mlfqsgA---------LFTDMSVFDNIAFplreHTKL-------SEALI-KLvvlmkLQAVGLRGAKDLMPSELSGGMAR 144
Cdd:NF033858 79 ------AympqglgknLYPTLSVFENLDF----FGRLfgqdaaeRRRRIdEL-----LRATGLAPFADRPAGKLSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 145 RAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVThdvTEVMSIA---DHVIIIaDQG-VIGAG 220
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVA---TAYMEEAerfDWLVAM-DAGrVLATG 219
|
....*.
gi 2096624516 221 TPDEMR 226
Cdd:NF033858 220 TPAELL 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
3.61e-06 |
|
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: 46.66 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFS-----RGDRTI--YKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILF--EGGSIP--SMS 69
Cdd:COG4778 4 LLEVENLSKTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 70 RKELYAARtKMSMLFQS---------GALftdmsvfDNIAFPLREH-TKLSEALIKlvvlmklqavglrgAKDLM----- 134
Cdd:COG4778 84 PREILALR-RRTIGYVSqflrviprvSAL-------DVVAEPLLERgVDREEARAR--------------ARELLarlnl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 135 PSEL--------SGG----------MArraalaraiaLDPELIMYDEPFAGQDPISMGVLVKLIKSLNE----VLGlssl 192
Cdd:COG4778 142 PERLwdlppatfSGGeqqrvniargFI----------ADPPLLLLDEPTASLDAANRAVVVELIEEAKArgtaIIG---- 207
|
250 260
....*....|....*....|..
gi 2096624516 193 iVTHDvTEVMS-IADHVIIIAD 213
Cdd:COG4778 208 -IFHD-EEVREaVADRVVDVTP 227
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-239 |
3.90e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.98 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 24 VPK-GKITAIMGPSGIGKTTMLRLIGGQLKPDAG---------DIL--FEGGSIPSMSRKeLYAARTKMSMLFQsgalFT 91
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFRGSELQNYFTK-LLEGDVKVIVKPQ----YV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 92 DM--SVFDNIAFPLREHTKLSEALIKLVvlmklQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQD 169
Cdd:cd03236 97 DLipKAVKGKVGELLKKKDERGKLDELV-----DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 170 PISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHV-IIIADQGVIGAGT-PDEMRNHesplVQQFLKG 239
Cdd:cd03236 172 IKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIhCLYGEPGAYGVVTlPKSVREG----INEFLDG 238
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-62 |
4.54e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 4.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 3 EVKDVSFSRGDRTIY---KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEG 62
Cdd:PRK13545 23 KLKDLFFRSKDGEYHyalNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-101 |
5.03e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYkNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMsrkelyaARTKM 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------AKPYC 72
|
90 100
....*....|....*....|.
gi 2096624516 81 SMLFQSGALFTDMSVFDNIAF 101
Cdd:PRK13541 73 TYIGHNLGLKLEMTVFENLKF 93
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-211 |
5.42e-06 |
|
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: 47.32 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 24 VPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrkelyaaRTKMSMLFQSGALFTDMSVFDNIaFPL 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----------LTNISDVHQNMGYCPQFDAIDDL-LTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 104 REHTKLSEAL-------IKLVVLMKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISMGVL 176
Cdd:TIGR01257 2030 REHLYLYARLrgvpaeeIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190
....*....|....*....|....*....|....*
gi 2096624516 177 VKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:TIGR01257 2110 WNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-65 |
5.97e-06 |
|
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: 45.64 E-value: 5.97e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2096624516 24 VPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSI 65
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-242 |
6.11e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 20 MSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPD----AGDILFEGGSIPSMSRKElyaaRTK-----MSMLFQSGALF 90
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRE----RRKlvghnVSMIFQEPQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 91 TDMSvfDNIAFPL---------------REHTKLSEAlIKLvvlmkLQAVGLRGAKDLM---PSELSGGMARRAALARAI 152
Cdd:PRK15093 102 LDPS--ERVGRQLmqnipgwtykgrwwqRFGWRKRRA-IEL-----LHRVGIKDHKDAMrsfPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIADHV-IIIADQGVIGAGTPDEMRNHESP 231
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKInVLYCGQTVETAPSKELVTTPHHP 253
|
250
....*....|.
gi 2096624516 232 LVQQFLKGLSD 242
Cdd:PRK15093 254 YTQALIRAIPD 264
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-89 |
1.05e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 26 KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGD-ILFEGGSIPSMSRKELYAARTKMSMLFQSGAL 89
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKASGSGEL 65
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-72 |
1.47e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 1.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG--QLKPDAGDILFEGGSIPSMSRKE 72
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPED 74
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-235 |
1.58e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.78 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSR--GDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTK 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL---RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 MSMLFQSGALFTDmSVFDNIAFPLREHTKLS--EALIKLVVLM----KLQAvGLrgakDLMPSE----LSGGMARRAALA 149
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQYSREqiEEAARMAYAMdfinKMDN-GL----DTVIGEngvlLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEvlGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGtpdemrNHE 229
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG------THA 563
|
....*.
gi 2096624516 230 SPLVQQ 235
Cdd:PRK11176 564 ELLAQN 569
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-183 |
1.62e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 6 DVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPD--AGDILFEGGSIPSMSRKelyaartKMSML 83
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILK-------RTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 84 FQSGALFTDMSVFDNIAFP--LR--------EHTKLSEALIKLVVLMKLQ--AVG---LRGakdlmpseLSGGMARRAAL 148
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCslLRlpksltkqEKILVAESVISELGLTKCEntIIGnsfIRG--------ISGGERKRVSI 217
|
170 180 190
....*....|....*....|....*....|....*
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDPISMGVLVKLIKSL 183
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-237 |
1.71e-05 |
|
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: 46.06 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 16 IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgsipsmsrKELYAARTKMSMlfqsgalftDMSV 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------RISFSPQTSWIM---------PGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 96 FDNIAFPLREHTKLSEALIKLVVLMklQAVGLRGAKDLMP-----SELSGGMARRAALARAIALDPELIMYDEPFAGQD- 169
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQLE--EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDv 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 170 ----PISMGVLVKLIKSLNEVLGLSSLivthdvtEVMSIADHVIIIADQGVIGAGTPDEMRNHESPLVQQFL 237
Cdd:TIGR01271 582 vtekEIFESCLCKLMSNKTRILVTSKL-------EHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLL 646
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-62 |
1.97e-05 |
|
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: 44.85 E-value: 1.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2096624516 16 IYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEG 62
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-67 |
2.12e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096624516 6 DVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTML-----RLIGGQLkpDAGDILFEGGSIPS 67
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRPLDS 832
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-237 |
3.10e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS---RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmsrkelyAART 78
Cdd:PLN03130 615 ISIKNGYFSwdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTV---------AYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 79 KMSMLFQSgalftdmSVFDNIAFPLREHTKLSEALIKLVVLMK---------LQAVGLRGAKdlmpseLSGGMARRAALA 149
Cdd:PLN03130 686 QVSWIFNA-------TVRDNILFGSPFDPERYERAIDVTALQHdldllpggdLTEIGERGVN------ISGGQKQRVSMA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 150 RAIALDPELIMYDEPFAGQDP-ISMGVLVKLIKslNEVLGLSSLIVTHDVtEVMSIADHVIIIADQGVIGAGTPDEMRNH 228
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIK--DELRGKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
....*....
gi 2096624516 229 eSPLVQQFL 237
Cdd:PLN03130 830 -GPLFQKLM 837
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-218 |
4.68e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELYAArtKMSMLFQSGALFTDMSVFD 97
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA--GIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIaFPLREHT---------KLSEALIKLvvlmkLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQ 168
Cdd:PRK10762 99 NI-FLGREFVnrfgridwkKMYAEADKL-----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2096624516 169 DPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIADQGVIG 218
Cdd:PRK10762 173 TDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-225 |
5.19e-05 |
|
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: 44.55 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFS--RGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGgSIPSMSRKelyaartk 79
Cdd:TIGR00957 637 ITVHNATFTwaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQ-------- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 80 msmlfqsgALFTDMSVFDNIAFplreHTKLSEALIKLVvlmkLQAVGLRGAKDLMPS-----------ELSGGMARRAAL 148
Cdd:TIGR00957 708 --------AWIQNDSLRENILF----GKALNEKYYQQV----LEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDP-ISMGVLVKLIKSLNEVLGLSSLIVTHDVTEVMSIaDHVIIIADQGVIGAGTPDEM 225
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-218 |
6.47e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 17 YKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKelyaARTKMSMLF-----QSGALFT 91
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA----QRLARGLVYlpedrQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 92 DMSVFDNIAfPLREHTK---LSEALIKLVVLMKLQAVGLRGAKDLMPSE-LSGGMARRAALARAIALDPELIMYDEPFAG 167
Cdd:PRK15439 355 DAPLAWNVC-ALTHNRRgfwIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 168 QDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIAdQGVIG 218
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMH-QGEIS 482
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-97 |
8.39e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSrgdrtiYKNMSFSV-P------KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELY 74
Cdd:PRK10522 323 LELRNVTFA------YQDNGFSVgPinltikRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPE 393
|
90 100
....*....|....*....|...
gi 2096624516 75 AARTKMSmlfqsgALFTDMSVFD 97
Cdd:PRK10522 394 DYRKLFS------AVFTDFHLFD 410
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
159-246 |
8.44e-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: 43.46 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 159 IMY--DEPFAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDvTEVMSIADHVIiiaDQG---------VIGAGTPDEMRN 227
Cdd:TIGR00630 510 VLYvlDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHD-EDTIRAADYVI---DIGpgagehggeVVASGTPEEILA 584
|
90
....*....|....*....
gi 2096624516 228 HESPLVQQFLKGLSDGPVP 246
Cdd:TIGR00630 585 NPDSLTGQYLSGRKKIEVP 603
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-49 |
1.01e-04 |
|
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: 42.23 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2096624516 6 DVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG 49
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG 55
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-222 |
1.02e-04 |
|
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: 42.48 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGD--RTIYKNMSFSVPKGKITAIMGPSGIGKTTM----LRLIggqlKPDAGDILFEGGSIPSMSRKELya 75
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 aRTKMSMLFQSGALFTDmSVFDNIAfPLREHT--KLSEALIKlvVLMKLQAVGLRGAKDLMPSE----LSGGMARRAALA 149
Cdd:cd03244 77 -RSRISIIPQDPVLFSG-TIRSNLD-PFGEYSdeELWQALER--VGLKEFVESLPGGLDTVVEEggenLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIKSlnEVLGLSSLIVTHDVTEVMSiADHVIIIaDQG-VIGAGTP 222
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVL-DKGrVVEFDSP 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-213 |
1.14e-04 |
|
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: 42.32 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRG-DRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDIlFEGGSIPSMSRKELYAARTKM 80
Cdd:cd03290 1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-HWSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQS-GALFTDMSVFDNIAFplreHTKLSEALIKLVVlmklQAVGLRGAKDLMPS-----------ELSGGMARRAAL 148
Cdd:cd03290 80 SVAYAAqKPWLLNATVEENITF----GSPFNKQRYKAVT----DACSLQPDIDLLPFgdqteigergiNLSGGQRQRICV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096624516 149 ARAIALDPELIMYDEPFAGQDP------ISMGVLvKLIKSLNEVLglssLIVTHDVtEVMSIADHVIIIAD 213
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIhlsdhlMQEGIL-KFLQDDKRTL----VLVTHKL-QYLPHADWIIAMKD 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-218 |
2.03e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGqLKPDA---GDILFEGGSIPSMSRKElyAARTKMSMLFQSGALFTDMSV 95
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRD--TERAGIAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 96 FDNIaFPLREHTKLSealiklvvLMKLQAVGLRGAK-------DLMP----SELSGGMARRAALARAIALDPELIMYDEP 164
Cdd:PRK13549 100 LENI-FLGNEITPGG--------IMDYDAMYLRAQKllaqlklDINPatpvGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 165 FAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIIIADQGVIG 218
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-181 |
2.11e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.76 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVS--FSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTM----LRLIGGQlkpdaGDILFEGGSIPSMSRKELya 75
Cdd:cd03289 3 MTVKDLTakYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTE-----GDIQIDGVSWNSVPLQKW-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 76 aRTKMSMLFQSGALFTdmSVFDNIAFPLREHTklSEALIKLVvlmklQAVGLRGAKDLMPSE-----------LSGGMAR 144
Cdd:cd03289 76 -RKAFGVIPQKVFIFS--GTFRKNLDPYGKWS--DEEIWKVA-----EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQ 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 2096624516 145 RAALARAIALDPELIMYDEPFAGQDPISMGVLVKLIK 181
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-49 |
3.16e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 3.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2096624516 2 VEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGG 49
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-181 |
3.49e-04 |
|
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: 41.82 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDaGDILFEGGSIPSMSrkeLYAARTKM 80
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT---LQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTdmsvfDNIAFPLREHTKLSEALIKLVVlmklQAVGLRGAKDLMPSE-----------LSGGMARRAALA 149
Cdd:TIGR01271 1295 GVIPQKVFIFS-----GTFRKNLDPYEQWSDEEIWKVA----EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLA 1365
|
170 180 190
....*....|....*....|....*....|..
gi 2096624516 150 RAIALDPELIMYDEPFAGQDPISMGVLVKLIK 181
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-58 |
6.11e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 6.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 7 VSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-226 |
6.85e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQlkpdagdilFEggsipsMSRKELYAARTKMSMLFQsgALFTDMSVFD 97
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQ---------FE------ISEGRVWAERSIAYVPQQ--AWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIAFPLREHTklsEALIKLVVLMKLQA------VGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPi 171
Cdd:PTZ00243 740 NILFFDEEDA---ARLADAVRVSQLEAdlaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA- 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 172 SMGVLVKLIKSLNEVLGLSSLIVTHDVtEVMSIADHVIIIADQGVIGAG-TPDEMR 226
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGsSADFMR 870
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-213 |
7.35e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 19 NMSFSVPKGKITAIMGPSGIGKTTMLRLIGGqLKPDA---GDILFEG-----GSIPSMSRK-------ELyaartkmsml 83
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFDGevcrfKDIRDSEALgiviihqEL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 84 fqsgALFTDMSVFDNIaFPLREHTKL-----SEALIKLVVLMKlqAVGLRGAKDLMPSELSGGMARRAALARAIALDPEL 158
Cdd:NF040905 88 ----ALIPYLSIAENI-FLGNERAKRgvidwNETNRRARELLA--KVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2096624516 159 IMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHVIIIAD 213
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRD 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-219 |
9.07e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 3 EVKDVSFSRGDrtiykNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKE-LYAARTKMS 81
Cdd:PRK10762 259 KVDNLSGPGVN-----DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 82 MLFQSGALFTDMSVFDNIAFPLREHtkLSEALIKLVVLMKLQAVG----LRGAKdlMPS------ELSGGMARRAALARA 151
Cdd:PRK10762 334 EDRKRDGLVLGMSVKENMSLTALRY--FSRAGGSLKHADEQQAVSdfirLFNIK--TPSmeqaigLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096624516 152 IALDPELIMYDEPFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHvIIIADQGVIGA 219
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDR-ILVMHEGRISG 475
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-62 |
1.77e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096624516 1 MVEVKDVSFSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEG 62
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-217 |
3.21e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.35 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 21 SFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKElyAARTKMsMLF----QSGALFTDMSVF 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRAGI-MLCpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 97 DNIAFPLREH-------------TKLSEALIKLVvlmklqAVGLRGAKDLMpSELSGGMARRAALARAIALDPELIMYDE 163
Cdd:PRK11288 350 DNINISARRHhlragclinnrweAENADRFIRSL------NIKTPSREQLI-MNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2096624516 164 PFAGQDPISMGVLVKLIKSLNEVlGLSSLIVTHDVTEVMSIADHvIIIADQGVI 217
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADR-IVVMREGRI 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-211 |
3.67e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.37 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 14 RTIYKNMSFSVPKGKITAIMGPSGIGKT-TMLRLIGGQLKPDAGDILFEGGsiPSMSRKELYAARTKMSMLFQS---GAL 89
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGK--PVKIRNPQQAIAQGIAMVPEDrkrDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 90 FTDMSVFDNIAFP-LREHTKLS---EALIKLVVLMKLQAVGLRGAKDLMP-SELSGGMARRAALARAIALDPELIMYDEP 164
Cdd:PRK13549 353 VPVMGVGKNITLAaLDRFTGGSridDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2096624516 165 FAGQDPISMGVLVKLIKSLNEvLGLSSLIVTHDVTEVMSIADHVIII 211
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
178-239 |
4.24e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 4.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096624516 178 KLIKSLNEV--LGLSSLIVTHDvTEVMSIADHVIiiaDQG---------VIGAGTPDEMRNHESPLVQQFLKG 239
Cdd:COG0178 525 RLIETLKRLrdLGNTVIVVEHD-EDTIRAADYII---DIGpgagehggeVVAQGTPEEILKNPDSLTGQYLSG 593
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
4.76e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 37.90 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVS-FSRGDRTIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLkPDAGDILFEGGSIPSMSRKELyaaRTKM 80
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESW---RKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 81 SMLFQSGALFTDmSVFDNIAF--PLREHTKLSEALIKLVVL--MKLQAVGLrgakDLMPSE----LSGGMARRAALARAI 152
Cdd:PRK11174 426 SWVGQNPQLPHG-TLRDNVLLgnPDASDEQLQQALENAWVSefLPLLPQGL----DTPIGDqaagLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 153 ALDPELIMYDEPFAGQDPISMGvlvKLIKSLNEV-LGLSSLIVTHDVTEVMSIaDHVIIIADQGVIGAGTPDEMRNHESP 231
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQ---LVMQALNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-97 |
5.31e-03 |
|
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: 37.01 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 2 VEVKDVSFSRGDR--TIYKNMSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIpsmSRKELYAARTK 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSS 83
|
90 100
....*....|....*....|...
gi 2096624516 80 MSMLFQ-----SGALFTDMSVFD 97
Cdd:cd03369 84 LTIIPQdptlfSGTIRSNLDPFD 106
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-58 |
5.92e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 5.92e-03
10 20 30
....*....|....*....|....*....|...
gi 2096624516 26 KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-49 |
6.13e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 6.13e-03
10 20
....*....|....*....|....*
gi 2096624516 26 KGKITAIMGPSGIGKTTML-RLIGG 49
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLnALLPE 108
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-249 |
7.79e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 37.65 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 20 MSFSVPKGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDILFEGGSIPSMSRKELyaaRTKMSMLFQSGALFTDMSVFdNI 99
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPVLFSGTVRF-NI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 100 AfPLREHTK------LSEALIKLVVlmKLQAVGLRGAKDLMPSELSGGMARRAALARAIALDPELIMYDEPFAGQDPISM 173
Cdd:PLN03232 1331 D-PFSEHNDadlweaLERAHIKDVI--DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096624516 174 GVLVKLIKSlnEVLGLSSLIVTHDVTEVMSiADHVIIIADQGVIGAGTPDEMRNHESPLVQQFLKglSDGPVPFHY 249
Cdd:PLN03232 1408 SLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH--STGPANAQY 1478
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
178-246 |
8.07e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 178 KLIKSLNEV--LGLSSLIVTHDvTEVMSIADHVIiiaDQG---------VIGAGTPDEMRNHESPLVQQFLKGLSDGPVP 246
Cdd:PRK00349 529 RLIETLKHLrdLGNTLIVVEHD-EDTIRAADYIV---DIGpgagvhggeVVASGTPEEIMKNPNSLTGQYLSGKKKIEVP 604
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-209 |
8.90e-03 |
|
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: 36.15 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 18 KNMSFSVPKGKITAIMGPSGIGKTTmlrliggqlkpdagdILFEGgsipsmsrkeLYAARTKMsmlfqsgaLFTDMSVFD 97
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEG----------LYASGKAR--------LISFLPKFS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096624516 98 NIafplrehtklsealiKLVVLMKLQAVGLRGAKDLMP----SELSGGMARRAALARAIALDPE--LIMYDEPFAGQDPI 171
Cdd:cd03238 59 RN---------------KLIFIDQLQFLIDVGLGYLTLgqklSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 2096624516 172 SMGVLVKLIKSLNEvLGLSSLIVTHDVTeVMSIADHVI 209
Cdd:cd03238 124 DINQLLEVIKGLID-LGNTVILIEHNLD-VLSSADWII 159
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-58 |
9.25e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 36.72 E-value: 9.25e-03
10 20 30
....*....|....*....|....*....|...
gi 2096624516 26 KGKITAIMGPSGIGKTTMLRLIGGQLKPDAGDI 58
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLLNALAPDLELKTGEI 195
|
|
| |
