|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-305 |
9.00e-49 |
|
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: 172.71 E-value: 9.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 8 NGLFTGGIYFVeiislvgGLFLVKNNFLNLNVMVGVwNAGIGSILDPFMSLPVVTSFLAQQKVAIDRVNKrlaAVKTEQT 87
Cdd:COG2274 389 QQLATVALLWL-------GAYLVIDGQLTLGQLIAF-NILSGRFLAPVAQLIGLLQRFQDAKIALERLDD---ILDLPPE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 88 HEDNVKSTTQEPLQ-KLIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNe 166
Cdd:COG2274 458 REEGRSKLSLPRLKgDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL-ID- 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 167 kGQQRTQF-----QGALAYVPQRNQLFNTTVWRNLTLDKPY-DRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSE 239
Cdd:COG2274 536 -GIDLRQIdpaslRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGeGGSNLSG 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 240 GQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
71-305 |
2.22e-47 |
|
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: 166.86 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 71 AIDRVNKRLAAVKtEQTHEDNVKSTTQEPLQkLIFHNVDFTYPsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLL 150
Cdd:COG4988 307 AAEKIFALLDAPE-PAAPAGTAPLPAAGPPS-IELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 151 LNLLDPGKGSISaVNekGQ-----QRTQFQGALAYVPQRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALP 224
Cdd:COG4988 384 LGFLPPYSGSIL-IN--GVdlsdlDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 225 DGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDT 303
Cdd:COG4988 461 DGLDTPLGeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
..
gi 1714390902 304 VI 305
Cdd:COG4988 541 IL 542
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-305 |
8.89e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 165.72 E-value: 8.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 8 NGLFTGGIYFVEIISLVG----GLFLVKNNFLNLNVMVGVWNAgIGSILDPFMSLPVVTSFLAQQKVAIDRVNKRLAavk 83
Cdd:COG1132 244 SALFFPLMELLGNLGLALvllvGGLLVLSGSLTVGDLVAFILY-LLRLFGPLRQLANVLNQLQRALASAERIFELLD--- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 84 TEQTHEDNVKSTTQEPLQKLI-FHNVDFTYPSQtEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS 162
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIeFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 163 --AVNEKGQQRTQFQGALAYVPQRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFS 238
Cdd:COG1132 399 idGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGeRGVNLS 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 239 EGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRIL 545
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
53-305 |
6.43e-45 |
|
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: 160.32 E-value: 6.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 53 DPFMSLPVVTSFLAQQKVAIDRVNKRLAAVKTEQTHEDNVKSTTQEPLQkliFHNVDFTYPSQTEPVFEKLNLSILKSQI 132
Cdd:COG4987 287 EALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLE---LEDVSFRYPGAGRPVLDGLSLTLPPGER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 133 TFVVGHNGAGKTTLIKLLLNLLDPGKGSISA--VNEKGQQRTQFQGALAYVPQRNQLFNTTVWRNLTLDKPY-DRQDVHQ 209
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPQSGSITLggVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 210 ALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV 288
Cdd:COG4987 444 ALERVGLGDWLAALPDGLDTWLGeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV 523
|
250
....*....|....*..
gi 1714390902 289 LIITHTFDLIQDSDTVI 305
Cdd:COG4987 524 LLITHRLAGLERMDRIL 540
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
103-305 |
1.45e-37 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 131.35 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISA--VNEKGQQRTQFQGALAY 180
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNTTVWRNLtldkpydrqdvhqalqavnmdriidalpdgwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1714390902 261 DEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
99-307 |
1.78e-37 |
|
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: 139.73 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 99 PLQKLIFHNVDFTYPSqTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVNekGQQRTQF---- 174
Cdd:TIGR02857 318 PASSLEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-AVN--GVPLADAdads 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 175 -QGALAYVPQRNQLFNTTVWRNLTLDKPY-DRQDVHQALQAVNMDRIIDALPDGWHTEVGKV-TNFSEGQMRRLSIARAL 251
Cdd:TIGR02857 394 wRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGgAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 252 LAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVIKV 307
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
102-305 |
5.14e-34 |
|
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: 123.87 E-value: 5.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYPSQtEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--SAVNEKGQQRTQFQGALA 179
Cdd:cd03254 2 EIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIliDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVWRNLTLDKPY-DRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQF 257
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGeNGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1714390902 258 LIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKIL 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
105-305 |
9.81e-34 |
|
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: 122.58 E-value: 9.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALAYVP 182
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 Q--RNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLA 253
Cdd:cd03225 82 QnpDDQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPF----------TLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTVI 305
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLElADRVI 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
103-305 |
4.46e-33 |
|
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: 121.67 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEK---GQQRTQFQGALA 179
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL-VDGKditKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQ--RNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLS 246
Cdd:COG1122 79 LVFQnpDDQLFAPTVEedvafgpENLGLPREEIRERVEEALELVGLehlaDRPPHEL--------------SGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 247 IARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTVI 305
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAElADRVI 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
105-305 |
3.30e-32 |
|
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: 119.26 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--SAVNEKGQQRTQFQGALAYVP 182
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIliDGHDVRDYTLASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGeRGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1714390902 261 DEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIV 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
105-309 |
1.01e-31 |
|
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: 118.03 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTE-PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALAYV 181
Cdd:cd03249 3 FKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 182 PQRNQLFNTTVWRNLTLDKPYDRQ-DVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLI 259
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDeEVEEAAKKANIHDFIMSLPDGYDTLVGeRGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVIKVGK 309
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQN 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
103-305 |
2.02e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNekGQQRTQFQGALAYVP 182
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVR-LF--GKPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQL---FNTTV--------WRNLTLDKPY---DRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRR 244
Cdd:COG1121 82 QRAEVdwdFPITVrdvvlmgrYGRRGLFRRPsraDREAVDEALERVGLedlaDRPIGEL--------------SGGQQQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 245 LSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTVI 305
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVL 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
105-293 |
3.16e-30 |
|
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: 113.40 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGALAYVPQR 184
Cdd:cd03235 2 VEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV---FGKPLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 ---NQLFNTTV--------WRNLTLDKPY---DRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLS 246
Cdd:cd03235 77 rsiDRDFPISVrdvvlmglYGHKGLFRRLskaDKAKVDEALERVGLselaDRQIGEL--------------SGGQQQRVL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1714390902 247 IARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITH 293
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTH 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
117-293 |
2.94e-28 |
|
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: 107.95 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 117 EPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE-KGQQRTQFQGALAYVPQRNQLFNT-TVWR 194
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpIRDAREDYRRRLAYLGHADGLKPElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 195 NLTL-----DKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDA 269
Cdd:COG4133 95 NLRFwaalyGLRADREAIDEALEAVGLAGLADL----------PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*
gi 1714390902 270 RNQSELMHTVRELSQKIG-VLIITH 293
Cdd:COG4133 165 AGVALLAELIAAHLARGGaVLLTTH 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
103-305 |
1.22e-27 |
|
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: 106.40 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPS---QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnekgqqrtQFQGALA 179
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----------SVPGSIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFL 258
Cdd:cd03250 70 YVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGeKGINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 259 IMDEPFSDLDArnqselmHTVRELSQK-IG--------VLIITHTFDLIQDSDTVI 305
Cdd:cd03250 150 LLDDPLSAVDA-------HVGRHIFENcILglllnnktRILVTHQLQLLPHADQIV 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
103-305 |
1.57e-27 |
|
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: 106.93 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGS--ISAVNEKGQQRTQFQGALAY 180
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSilIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFL 258
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPdATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGeRGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 259 IMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKII 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-293 |
1.74e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 111.68 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 4 AAANNGLFTGgiyfveIISLVGGLFLVknnflnLNVMVGVwNAGIGSILDP-------FMSLPVVTSFLAQQKVAIDRVN 76
Cdd:TIGR02868 233 AAAATALGAA------LTLLAAGLAVL------GALWAGG-PAVADGRLAPvtlavlvLLPLAAFEAFAALPAAAQQLTR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 77 KRLAAVKTEQTHEDNVKSTTQE-------PLQK--LIFHNVDFTYPSQtEPVFEKLNLSILKSQITFVVGHNGAGKTTLI 147
Cdd:TIGR02868 300 VRAAAERIVEVLDAAGPVAEGSapaagavGLGKptLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 148 KLLLNLLDPGKGSISAVNEKGQQRTQ--FQGALAYVPQRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALP 224
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDGVPVSSLDQdeVRRRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALP 458
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 225 DGWHTEVGK-VTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITH 293
Cdd:TIGR02868 459 DGLDTVLGEgGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
106-305 |
2.29e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 103.11 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 106 HNVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEKGQQRTQFQGALAYVPQ-- 183
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-LNGKPIKAKERRKSIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 RNQLFNTTVWRNLTL---DKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:cd03226 81 DYQLFTDSVREELLLglkELDAGNEQAETVLKDLDLYALKERHP----------LSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 261 DEPFSDLDARNQSELMHTVRELS-QKIGVLIITHTFDLIQD-SDTVI 305
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVL 197
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
56-293 |
5.60e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.60 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 56 MSLPVVTSF--LAQQKVAIDRVNKrlaavKTEQTHEdnVKSTTQEPLQK----LIFHNVDFTYPSQTEPVFEKLNLSILK 129
Cdd:PRK11160 293 ALMPVAGAFqhLGQVIASARRINE-----ITEQKPE--VTFPTTSTAAAdqvsLTLNNVSFTYPDQPQPVLKGLSLQIKA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 130 SQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-------SAVNEkgqqrTQFQGALAYVPQRNQLFNTTVWRNLTLDKP- 201
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiADYSE-----AALRQAISVVSQRVHLFSATLRDNLLLAAPn 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 202 -YDRQdVHQALQAVNMDRIIDALP--DGWHTEVGKvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHT 278
Cdd:PRK11160 441 aSDEA-LIEVLQQVGLEKLLEDDKglNAWLGEGGR--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEL 517
|
250
....*....|....*
gi 1714390902 279 VRELSQKIGVLIITH 293
Cdd:PRK11160 518 LAEHAQNKTVLMITH 532
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
103-297 |
1.74e-25 |
|
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: 102.04 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEK---GQQRTQFQGALA 179
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL-LDGRdlaSLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQL-FNTTV--------------WRNLTldkPYDRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEG 240
Cdd:COG1120 79 YVPQEPPApFGLTVrelvalgryphlglFGRPS---AEDREAVEEALERTGLehlaDRPVDEL--------------SGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 241 QMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELS--QKIGVLIITHtfDL 297
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLH--DL 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
105-305 |
2.11e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 101.13 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQ--RTQFQGALAYVP 182
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVWRNLTLDKPY-DRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGeRGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1714390902 261 DEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRII 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
102-305 |
2.26e-25 |
|
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: 101.03 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALA 179
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEV---GKvtNFSEGQMRRLSIARALLAHKQ 256
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVeegGE--NLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 257 FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRIL 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
103-305 |
4.62e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 100.70 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE-KGQQRTQFQGALAYV 181
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 182 PQRNQLF-NTTVWRNLT-------LDKPYDRQDVHQALQAVNMDRIIDalpdgwhtevGKVTNFSEGQMRRLSIARALLA 253
Cdd:COG4555 80 PDERGLYdRLTVRENIRyfaelygLFDEELKKRIEELIELLGLEEFLD----------RRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQD-SDTVI 305
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVV 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
123-304 |
2.32e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.00 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLdPGKGSISaVNekGQQ-----RTQFQGALAYVPQRNQLFNTTVWRNLT 197
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLK-IN--GIElreldPESWRKHLSWVGQNPQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 LDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSEL 275
Cdd:PRK11174 445 LGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180
....*....|....*....|....*....
gi 1714390902 276 MHTVRELSQKIGVLIITHTFDLIQDSDTV 304
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
102-293 |
4.09e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.62 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYPSQTE--PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGALA 179
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV---DGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFN-TTVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARAL 251
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVALglelrgvPKAERRERARELLELVGLAGFEDAYPH----------QLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1714390902 252 LAHKQFLIMDEPFSDLDA--RN--QSELMHTVRElsQKIGVLIITH 293
Cdd:COG1116 154 ANDPEVLLMDEPFGALDAltRErlQDELLRLWQE--TGKTVLFVTH 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
77-297 |
1.58e-23 |
|
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: 100.36 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 77 KRLAAVKTEQTHEDNVKSTTQ--EPLqkLIFHNVDFTYPSQTEPVF---EKLNLSILKSQITFVVGHNGAGKTTLIKLLL 151
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAaaEPL--LEVRNLSKRYPVRGKGGVravDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 152 NLLDPGKGSI-----SAVNEKGQQRTQFQGALAYVPQ--RNQLFNT-TVWRNLT--------LDKPYDRQDVHQALQAVN 215
Cdd:COG1123 313 GLLRPTSGSIlfdgkDLTKLSRRSLRELRRRVQMVFQdpYSSLNPRmTVGDIIAeplrlhglLSRAERRERVAELLERVG 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 216 MDR-IIDALPdgwHTevgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIIT 292
Cdd:COG1123 393 LPPdLADRYP---HE-------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGltYLFIS 462
|
....*
gi 1714390902 293 HtfDL 297
Cdd:COG1123 463 H--DL 465
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
105-305 |
1.88e-23 |
|
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: 96.00 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTE-PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVNEKGQQRTQ---FQGALAY 180
Cdd:cd03248 14 FQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPISQYEhkyLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNTTVWRNLTL---DKPYDRqdVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQ 256
Cdd:cd03248 93 VGQEPVLFARSLQDNIAYglqSCSFEC--VKEAAQKAHAHSFISELASGYDTEVGeKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 257 FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQIL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
123-265 |
2.99e-23 |
|
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: 93.10 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISA--VNEKGQQRTQFQGALAYVPQRNQLFN-TTVWRNL--- 196
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLrlg 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 197 ----TLDKPYDRQDVHQALQAVNmdriidaLPDGWHTEVGKVTN-FSEGQMRRLSIARALLAHKQFLIMDEPFS 265
Cdd:pfam00005 84 lllkGLSKREKDARAEEALEKLG-------LGDLADRPVGERPGtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
98-309 |
3.04e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.80 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 98 EPLQKLI-FHNVDFTYPSQTE-PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQ----- 170
Cdd:TIGR00958 473 LNLEGLIeFQDVSFSYPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhy 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 171 -RTQfqgaLAYVPQRNQLFNTTVWRNLT--LDKpYDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLS 246
Cdd:TIGR00958 553 lHRQ----VALVGQEPVLFSGSVRENIAygLTD-TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGeKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 247 IARALLAHKQFLIMDEPFSDLDARNQselmHTVRELSQKIG--VLIITHTFDLIQDSDTVIKVGK 309
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECE----QLLQESRSRASrtVLLIAHRLSTVERADQILVLKK 688
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
123-293 |
3.52e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.52 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEK--GQQRTQFQGALAYVPQRNQLFNT-TVWRNLT-- 197
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR-VLGEdvARDPAEVRRRIGYVPQEPALYPDlTVRENLRff 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 -----LDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQ 272
Cdd:COG1131 98 arlygLPRKEARERIDELLELFGLTDAADR----------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR 167
|
170 180
....*....|....*....|..
gi 1714390902 273 SELMHTVRELSQK-IGVLIITH 293
Cdd:COG1131 168 RELWELLRELAAEgKTVLLSTH 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
105-305 |
3.52e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 99.51 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQtEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNekGQ---QRTQ--FQGALA 179
Cdd:COG5265 360 FENVSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL-ID--GQdirDVTQasLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVG----KVtnfSEGQMRRLSIARALLAH 254
Cdd:COG5265 436 IVPQDTVLFNDTIAYNIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGerglKL---SGGEKQRVAIARTLLKN 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
103-305 |
3.56e-23 |
|
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: 95.63 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI------SAVNEKGQQRTQfqg 176
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdLALADPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 177 aLAYVPQRNQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVGKV-TNFSEGQMRRLSIARALLAH 254
Cdd:cd03252 78 -VGVVLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQgAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRII 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
103-305 |
4.05e-23 |
|
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: 99.21 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLdPGKGSIS-AVNEKGQQRTQFQGAL--- 178
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISgEVLLDGRDLLELSEALrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 179 --AYVPQ--RNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwHTevgkvtnFSEGQMRRLSI 247
Cdd:COG1123 84 riGMVFQdpMTQLNPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYP---HQ-------LSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 248 ARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQD-SDTVI 305
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGttVLLITHDLGVVAEiADRVV 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
103-296 |
6.32e-23 |
|
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: 94.11 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEK--GQQRTQFQGALAY 180
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-INGYsiRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNT-TVWRNLTL--------DKPYDrQDVHQALQAVNmdriidaLPDGWHTevgKVTNFSEGQMRRLSIARAL 251
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkglpKSEIK-EEVELLLRVLG-------LTDKANK---RARTLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1714390902 252 LAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFD 296
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMD 193
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
110-305 |
6.75e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.63 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 110 FTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQ-----GALAYVPQR 184
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF---HDIPLTKLQldswrSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQLFNTTVWRNLTLDKP-YDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:PRK10789 398 PFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGeRGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1714390902 263 PFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEIL 520
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
107-305 |
8.42e-23 |
|
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: 93.71 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEPVF--EKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-----SAVNEKGQQRTQFQGA-L 178
Cdd:cd03255 5 NLSKTYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtDISKLSEKELAAFRRRhI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 179 AYVPQRNQLFNT-TVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARA 250
Cdd:cd03255 85 GFVFQSFNLLPDlTALENVELplllagvPKKERRERAEELLERVGLGDRLNHYPS----------ELSGGQQQRVAIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 251 LLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQDSDTVI 305
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGttIVVVTHDPELAEYADRII 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
110-305 |
1.02e-22 |
|
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: 93.93 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 110 FTYPSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--SAVNEKGQ----QRTQFQGALAYVPQ 183
Cdd:cd03290 8 FSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPsfeaTRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 RNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGeRGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1714390902 263 PFSDLDARNQSELMHT-VRELSQ--KIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03290 167 PFSALDIHLSDHLMQEgILKFLQddKRTLVLVTHKLQYLPHADWII 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
103-307 |
1.76e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALAY 180
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNTTVWRNLTL--DKPYDRQDVHQALQ-AVNMDrIIDALPDGWHTEVGKV-TNFSEGQMRRLSIARALLAHKQ 256
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYarTEQYSREQIEEAARmAYAMD-FINKMDNGLDTVIGENgVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 257 FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVIKV 307
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
106-305 |
2.44e-22 |
|
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: 91.73 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 106 HNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALAYVPQ 183
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 rnqlfnttvwrnltldkpydrqdvhqALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLSIARALLAHKQFLI 259
Cdd:cd03214 81 --------------------------ALELLGLahlaDRPFNEL--------------SGGERQRVLLARALAQEPPILL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQK--IGVLIITHTFDL-IQDSDTVI 305
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLaARYADRVI 169
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
103-293 |
1.15e-21 |
|
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: 90.99 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEP--VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNekGQQRTQFQGALAY 180
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL-VD--GEPVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFN-TTVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALL 252
Cdd:cd03293 78 VFQQDALLPwLTVLDNVALglelqgvPKAEARERAEELLELVGLSGFENAYPH----------QLSGGMRQRVALARALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1714390902 253 AHKQFLIMDEPFSDLDA--RN--QSELMHTVRElsQKIGVLIITH 293
Cdd:cd03293 148 VDPDVLLLDEPFSALDAltREqlQEELLDIWRE--TGKTVLLVTH 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
71-304 |
1.89e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 94.43 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 71 AIDRVNKRLAAVKTEQThednvKSTTQEPLQKLIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLL 150
Cdd:COG4618 304 AYRRLNELLAAVPAEPE-----RMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 151 LNLLDPGKGS-------ISAVNekgqqRTQFQGALAYVPQRNQLFNTTVWRNLT-LDKPyDRQDVHQALQAVNMDRIIDA 222
Cdd:COG4618 379 VGVWPPTAGSvrldgadLSQWD-----REELGRHIGYLPQDVELFDGTIAENIArFGDA-DPEKVVAAAKLAGVHEMILR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 223 LPDGWHTEVGKV-TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQD 300
Cdd:COG4618 453 LPDGYDTRIGEGgARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAA 532
|
....
gi 1714390902 301 SDTV 304
Cdd:COG4618 533 VDKL 536
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
118-293 |
2.35e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.34 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS-AVNEKGQQRTQFQGALAYVPQRNQLFNT-TVWRN 195
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwNGTPLAEQRDEPHENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LTL---DKPYDRQDVHQALQAVNMDRIIDALpdgwhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQ 272
Cdd:TIGR01189 94 LHFwaaIHGGAQRTIEDALAAVGLTGFEDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|..
gi 1714390902 273 SELMHTVRELSQKIG-VLIITH 293
Cdd:TIGR01189 164 ALLAGLLRAHLARGGiVLLTTH 185
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
107-305 |
4.01e-21 |
|
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: 88.22 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEK--GQQRTQFQGALAYVPQR 184
Cdd:cd03230 5 NLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-VLGKdiKKEPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQLFNT-TVWRNLTLdkpydrqdvhqalqavnmdriidalpdgwhtevgkvtnfSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:cd03230 82 PSLYENlTVRENLKL---------------------------------------SGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 264 FSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTVI 305
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVA 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
54-305 |
5.00e-21 |
|
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: 93.47 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 54 PFMSLPVVTSFLAQQKVAIDRVNKRLAavkTEQTHEDNVKSTTQEP--LQKLIFHNVDFTYPSQTEPVFEKLNLSILKSQ 131
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLS---HEELEPDSIERRTIKPgeGNSITVHNATFTWARDLPPTLNGITFSIPEGA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 132 ITFVVGHNGAGKTTLIklllnlldpgkGSISAVNEKGQQRTQFQGALAYVPQRNQLFNTTVWRNLTLDKPYDRQDVHQAL 211
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLL-----------SALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVL 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 212 QAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDArnqselmHTVRELSQKI---- 286
Cdd:TIGR00957 735 EACALLPDLEILPSGDRTEIGeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-------HVGKHIFEHVigpe 807
|
250 260
....*....|....*....|....*
gi 1714390902 287 GVL------IITHTFDLIQDSDTVI 305
Cdd:TIGR00957 808 GVLknktriLVTHGISYLPQVDVII 832
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
105-309 |
5.26e-21 |
|
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: 87.30 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISavnekgqqrtqfqgalayvpqr 184
Cdd:cd00267 2 IENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 nqlfnttvwrnltldkpYDRQDVHQALqavnmdriidalPDGWHTEVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPF 264
Cdd:cd00267 58 -----------------IDGKDIAKLP------------LEELRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 265 SDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTVIKVGK 309
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKD 155
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
103-297 |
1.07e-20 |
|
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: 87.96 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAYVP 182
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLF-NTTVWRNL-------TLDKPYDRQDVHQALQAVNMDRIIDALPDGwhtevgkvtnFSEGQMRRLSIARALLAH 254
Cdd:cd03259 79 QDYALFpHLTVAENIafglklrGVPKAEIRARVRELLELVGLEGLLNRYPHE----------LSGGQQQRVALARALARE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQ 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
107-309 |
1.13e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVNEKGQQRTQFQGALAYVP 182
Cdd:PRK13647 9 DLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgWHtevgkvtnFSEGQMRRLSIARALLAHK 255
Cdd:PRK13647 88 PDDQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPP--YH--------LSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLI---QDSDTVIKVGK 309
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAaewADQVIVLKEGR 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
90-305 |
1.88e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.96 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 90 DNVKSTTQEPLQKLI-FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISA----V 164
Cdd:PLN03232 1221 ENNRPVSGWPSRGSIkFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdV 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 165 NEKGQqrTQFQGALAYVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVGKV-TNFSEGQMR 243
Cdd:PLN03232 1301 AKFGL--TDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGgENFSVGQRQ 1378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKIL 1440
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
41-305 |
3.33e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 90.93 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 41 VGVWNAGI---GSILDPFMSLPVVTSFLAQQKVAIDRVNKRLAAVKteQTHEDNVKsttqePLQ--KLIFHNVDFTYPSQ 115
Cdd:PRK10790 281 VGVLYAFIsylGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPR--QQYGNDDR-----PLQsgRIDIDNVSFAYRDD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 116 tEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVN---EKGQQRTQFQGaLAYVPQRNQLFNTTV 192
Cdd:PRK10790 354 -NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRQG-VAMVQQDPVVLADTF 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 193 WRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVGKVTN-FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARN 271
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNnLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
250 260 270
....*....|....*....|....*....|....
gi 1714390902 272 QSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTIL 545
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
103-305 |
6.66e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.25 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPS--QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGS-------ISAVNEKgqQRTQ 173
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvlidgqdISSLSER--ELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 174 FQG-ALAYVPQRNQLFNT-TVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRR 244
Cdd:COG1136 83 LRRrHIGFVFQFFNLLPElTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS----------QLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 245 LSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQDSDTVI 305
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGttIVMVTHDPELAARADRVI 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
105-305 |
7.64e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.55 E-value: 7.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEkLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALAYVP 182
Cdd:PRK13657 337 FDDVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVWRNLTLDKPyDRQD--VHQALQAVNMDRIIDALPDGWHTEVGKVTN-FSEGQMRRLSIARALLAHKQFLI 259
Cdd:PRK13657 416 QDAGLFNRSIEDNIRVGRP-DATDeeMRAAAERAQAHDFIERKPDGYDTVVGERGRqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
110-290 |
8.28e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.10 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 110 FTYPSQTE-PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVnekgqqrtqfQGALAYVPQRNQLF 188
Cdd:PLN03130 622 FSWDSKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI----------RGTVAYVPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 189 NTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDL 267
Cdd:PLN03130 692 NATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180
....*....|....*....|....*
gi 1714390902 268 DARNQSELMHTV--RELSQKIGVLI 290
Cdd:PLN03130 772 DAHVGRQVFDKCikDELRGKTRVLV 796
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
103-305 |
1.75e-18 |
|
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: 81.21 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVNEKGQQRTQfqgAL 178
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgVPVSDLEKALSS---LI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 179 AYVPQRNQLFNTTVWRNLTldkpydrqdvhqalqavnmdriidalpdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFL 258
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNLG-------------------------------------RRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 259 IMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKIL 167
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
117-309 |
2.92e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 117 EPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvNEKGQQRTQFQGALAYVPQRNQLFNT-TVWRN 195
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL-DGGDIDDPDVAEACHYLGHRNAMKPAlTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LTLDKPY---DRQDVHQALQAVNMDRIIDaLPDGwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQ 272
Cdd:PRK13539 94 LEFWAAFlggEELDIAAALEAVGLAPLAH-LPFG---------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1714390902 273 SELMHTVRE-LSQKIGVLIITHTfDLIQDSDTVIKVGK 309
Cdd:PRK13539 164 ALFAELIRAhLAQGGIVIAATHI-PLGLPGARELDLGP 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
103-305 |
3.24e-18 |
|
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: 80.31 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISA----VNEKGQQRTQFQGAL 178
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 179 AYVPQRNQLFNT-TVWRNLTLdkpydrqdvhqalqavnmdriidALpdgwhtevgkvtnfSEGQMRRLSIARALLAHKQF 257
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIAL-----------------------GL--------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 258 LIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQD-SDTVI 305
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGitVVLVTHDLDEAARlADRVV 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
118-307 |
6.49e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEK-GQQRTQFQGALAYVPQRN----QLfntTV 192
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPiRRQRDEYHQDLLYLGHQPgiktEL---TA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 193 WRNLT----LDKPYDRQDVHQALQAVNMDRIIDALpdgwhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLD 268
Cdd:PRK13538 92 LENLRfyqrLHGPGDDEALWEALAQVGLAGFEDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 269 ARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVIKV 307
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
115-308 |
1.03e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 83.67 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 115 QTEP--VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvnEKgqqrtqfqgALAYVPQRNQLFNTTV 192
Cdd:PTZ00243 669 ELEPkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA--ER---------SIAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 193 WRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARN 271
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 272 QSELMHTV--RELSQKIGVLiITHTFDLIQDSDTVIKVG 308
Cdd:PTZ00243 818 GERVVEECflGALAGKTRVL-ATHQVHVVPRADYVVALG 855
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
105-305 |
1.26e-17 |
|
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: 79.86 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVF--EKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-----SAVNEKGQQRTQFQGA 177
Cdd:cd03257 4 VKNLSVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkDLLKLSRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 LAYVPQ------------RNQLfNTTVWRNLTLDKPYDRQD-VHQALQAVNMD-RIIDALPdgwHTevgkvtnFSEGQMR 243
Cdd:cd03257 84 IQMVFQdpmsslnprmtiGEQI-AEPLRIHGKLSKKEARKEaVLLLLVGVGLPeEVLNRYP---HE-------LSGGQRQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQD-SDTVI 305
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGltLLFITHDLGVVAKiADRVA 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
105-299 |
1.55e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE-----KGQQRTQFQGALA 179
Cdd:COG2884 4 FENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlKRREIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQL-FNTTVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARAL 251
Cdd:COG2884 83 VVFQDFRLlPDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH----------ELSGGEQQRVAIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1714390902 252 LAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKiG--VLIITHTFDLIQ 299
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GttVLIATHDLELVD 201
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
105-308 |
1.87e-17 |
|
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: 80.04 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSqTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--SAVNEKGQQRTQFQGALAYVP 182
Cdd:cd03295 3 FENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfiDGEDIREQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLF-NTTVWRNLTL-------DKPYDRQDVHQALQAVNMD--RIIDALPDgwhtevgkvtNFSEGQMRRLSIARALL 252
Cdd:cd03295 82 QQIGLFpHMTVEENIALvpkllkwPKEKIRERADELLALVGLDpaEFADRYPH----------ELSGGQQQRVGVARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 253 AHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHtfdliqDSDTVIKVG 308
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGktIVFVTH------DIDEAFRLA 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
105-305 |
2.39e-17 |
|
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: 78.99 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--AVNEKGQQRTQFQGALAYVP 182
Cdd:cd03369 9 VENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidGIDISTIPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVWRNLtldKPYDRQDVHQALQAVNMdriidalpdgwhTEVGkvTNFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:cd03369 89 QDPTLFSGTIRSNL---DPFDEYSDEEIYGALRV------------SEGG--LNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1714390902 263 PFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKIL 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
61-305 |
2.50e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.16 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 61 VTSF--LAQQKVAIDRVNKRLAAVKTEQTHEDNVKSTTQEPLQKLIFHNVDFTYPSQtEPVFEKLNLSILKSQITFVVGH 138
Cdd:COG4178 319 VDNYqsLAEWRATVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGP 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 139 NGAGKTTliklllnlldpGKGSIsavnekgqQRTQFQGALaYVPQRNQLFNTTVWRNLT---LDKPYDRQDVHQALQAVN 215
Cdd:COG4178 398 SGSGKSTllraiaglwpyGSGRI--------ARPAGARVL-FLPQRPYLPLGTLREALLypaTAEAFSDAELREALEAVG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 216 MDRIIDAL--PDGWHTEvgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITH 293
Cdd:COG4178 469 LGHLAERLdeEADWDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
250
....*....|..
gi 1714390902 294 TFDLIQDSDTVI 305
Cdd:COG4178 543 RSTLAAFHDRVL 554
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
54-309 |
3.56e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.33 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 54 PFMSLPVVTSFLAQQKVAIDRVNKRLAAvkteqthEDNVKSTtQEPLQ----KLIFHNVDFTYPSQTE-PVFEKLNLSIL 128
Cdd:PLN03232 570 PLNMLPNLLSQVVNANVSLQRIEELLLS-------EERILAQ-NPPLQpgapAISIKNGYFSWDSKTSkPTLSDINLEIP 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 129 KSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVnekgqqrtqfQGALAYVPQRNQLFNTTVWRNLTLDKPYDRQDVH 208
Cdd:PLN03232 642 VGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI----------RGSVAYVPQVSWIFNATVRENILFGSDFESERYW 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 209 QALQAVNMDRIIDALPDGWHTEVG-KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTV--RELSQK 285
Cdd:PLN03232 712 RAIDVTALQHDLDLLPGRDLTEIGeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCmkDELKGK 791
|
250 260
....*....|....*....|....
gi 1714390902 286 IGVLiITHTFDLIQDSDTVIKVGK 309
Cdd:PLN03232 792 TRVL-VTNQLHFLPLMDRIILVSE 814
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
122-293 |
4.38e-17 |
|
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: 78.11 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 122 KLNLSI-LKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS-----------AVNEKGQQRtqfqgALAYVPQRNQLF- 188
Cdd:cd03297 14 TLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkKINLPPQQR-----KIGLVFQQYALFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 189 NTTVWRNLT-----LDKPYDRQDVHQALQAVNMDRIIDALPDGwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:cd03297 89 HLNVRENLAfglkrKRNREDRISVDELLDLLGLDHLLNRYPAQ----------LSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 264 FSDLDARNQSELMHTVRELSQ--KIGVLIITH 293
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTH 190
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
107-305 |
6.27e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.90 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKG--QQRTQ----FQG 176
Cdd:PRK13635 10 HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmVLSEETvwDVRRQvgmvFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 177 alayvPQrNQLFNTTV-------WRNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIAR 249
Cdd:PRK13635 90 -----PD-NQFVGATVqddvafgLENIGVPREEMVERVDQALRQVGMEDFLNREP----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 250 ALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK--IGVLIITHTFDLIQDSDTVI 305
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVI 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
107-305 |
8.01e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 76.49 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVNEKGqqRTQFQGALAYVP 182
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgADISQWD--PNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVwrnltldkpydrqdvhqalqavnMDRIidalpdgwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:cd03246 83 QDDELFSGSI-----------------------AENI-----------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 263 PFSDLDARNQSELMHTVRELS-QKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRIL 166
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
119-293 |
1.97e-16 |
|
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: 76.84 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTT-----LIKLLLNLLDPGKGSI----SAVNEKGQQRTQFQGALAYVPQRNQLFN 189
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTllrllNRLNDLIPGAPDEGEVlldgKDIYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 TTVWRNLTL--------DKPYDRQDVHQALQAVnmdriidALPDgwhtEVG---KVTNFSEGQMRRLSIARALLAHKQFL 258
Cdd:cd03260 95 GSIYDNVAYglrlhgikLKEELDERVEEALRKA-------ALWD----EVKdrlHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1714390902 259 IMDEPFSDLDARNQSELMHTVRELSQKIGVLIITH 293
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
103-297 |
2.62e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 76.63 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNE------KGQQRTQFQG 176
Cdd:COG3638 3 LELRNLSKRYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIL-VDGqdvtalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 177 ALAYVPQRNQLFN---------------TTVWRNLTldKPYDRQDVHQALQAvnMDRiidalpdgwhteVG-------KV 234
Cdd:COG3638 81 RIGMIFQQFNLVPrlsvltnvlagrlgrTSTWRSLL--GLFPPEDRERALEA--LER------------VGladkayqRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 235 TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQ--KIGVLIITHTFDL 297
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
103-293 |
3.68e-16 |
|
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: 75.69 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSIlKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVN--EKGQQRTQFQGALAY 180
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTI-RIDgqDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLF-NTTVWRNLT-------LDKPYDRQDVHQALQAVNmdriidaLPDGWHTEVGKvtnFSEGQMRRLSIARALL 252
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDyiawlkgIPSKEVKARVDEVLELVN-------LGDRAKKKIGS---LSGGMRRRVGIAQALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1714390902 253 AHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITH 293
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
123-296 |
3.74e-16 |
|
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: 76.22 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQF---QGALAYVPQRNQLF-NTTVWRNL-- 196
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL---NGKDITNLppeKRDISYVPQNYALFpHMTVYKNIay 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 -----TLDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARN 271
Cdd:cd03299 95 glkkrKVDKKEIERKVLEIAEMLGIDHLLNR----------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180
....*....|....*....|....*..
gi 1714390902 272 QSELMHTVRELSQKIG--VLIITHTFD 296
Cdd:cd03299 165 KEKLREELKKIRKEFGvtVLHVTHDFE 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
101-298 |
4.39e-16 |
|
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: 74.89 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 101 QKLIFHNVDFTYPSQTEPVFEKL----NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPG--KGSIsAVNEKGQQRTQF 174
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKQLlknvSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEV-LINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 175 QGALAYVPQRNQLFNTtvwrnLTldkpydrqdVHQALQ-AVNMDRIidalpdgwhtevgkvtnfSEGQMRRLSIARALLA 253
Cdd:cd03213 81 RKIIGYVPQDDILHPT-----LT---------VRETLMfAAKLRGL------------------SGGERKRVSIALELVS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITH--------TFDLI 298
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHqpsseifeLFDKL 182
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
103-293 |
5.00e-16 |
|
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: 76.34 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEpvFEK-----LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-----SAVNEKGQQRT 172
Cdd:TIGR04521 1 IKLKNVSYIYQPGTP--FEKkalddVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVtidgrDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 173 QFQGALAYVPQ--RNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRiidalpdgwhtEVGKVTNF--SEGQ 241
Cdd:TIGR04521 79 DLRKKVGLVFQfpEHQLFEETVYkdiafgpKNLGLSEEEAEERVKEALELVGLDE-----------EYLERSPFelSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 242 MRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL--SQKIGVLIITH 293
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTH 201
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
105-305 |
5.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQ-----FQGALA 179
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAktvwdIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQR--NQLFNTTV-------WRNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARA 250
Cdd:PRK13640 88 IVFQNpdNQFVGATVgddvafgLENRAVPRPEMIKIVRDVLADVGMLDYIDSEP----------ANLSGGQKQRVAIAGI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 251 LLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLI--ITHTFDLIQDSDTVI 305
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVisITHDIDEANMADQVL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
105-305 |
6.05e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 78.63 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGS--ISAVNEKGQQRTQFQGALAYVP 182
Cdd:PLN03130 1240 FEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRilIDGCDISKFGLMDLRKVLGIIP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVGKV-TNFSEGQMRRLSIARALLAHKQFLIMD 261
Cdd:PLN03130 1320 QAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAgENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 262 EPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRIL 1443
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
123-296 |
6.07e-16 |
|
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: 75.22 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGA---LAYVPQRNQLF-NTTVWRNLTL 198
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI---NGVDVTAAPPAdrpVSMLFQENNLFaHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 199 D-------KPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARN 271
Cdd:cd03298 94 GlspglklTAEDRQAIEVALARVGLAGLEKRLPG----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180
....*....|....*....|....*..
gi 1714390902 272 QSELMHTVREL--SQKIGVLIITHTFD 296
Cdd:cd03298 164 RAEMLDLVLDLhaETKMTVLMVTHQPE 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
103-293 |
7.09e-16 |
|
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: 75.51 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGsisavNEK---GQQRTQ------ 173
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG-----NDVrlfGERRGGedvwel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 174 ------FQGALAYVPQRNQ---------LFNTT-VWRNLTldkPYDRQDVHQALQAVNMDRIIDALpdgWHTevgkvtnF 237
Cdd:COG1119 77 rkriglVSPALQLRFPRDEtvldvvlsgFFDSIgLYREPT---DEQRERARELLELLGLAHLADRP---FGT-------L 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK--IGVLIITH 293
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTH 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
110-300 |
8.07e-16 |
|
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: 75.31 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 110 FTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-------SAVNEKGQQrtQFQGALAYVP 182
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdlTLLSGKELR--KARRRIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNT-TVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAH 254
Cdd:cd03258 89 QHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYP----------AQLSGGQKQRVGIARALANN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQD 300
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGltIVLITHEMEVVKR 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
106-299 |
8.78e-16 |
|
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: 75.22 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 106 HNVDFTYPSQTE--PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEK---GQQRTQFQGALAY 180
Cdd:COG1124 5 RNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT-FDGRpvtRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQ--------RNqlfntTVWRNLT-----LDKPYDRQDVHQALQAVNM-----DRIIDALpdgwhtevgkvtnfSEGQM 242
Cdd:COG1124 84 VFQdpyaslhpRH-----TVDRILAeplriHGLPDREERIAELLEQVGLppsflDRYPHQL--------------SGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 243 RRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQ--KIGVLIITHTFDLIQ 299
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVA 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
105-291 |
1.13e-15 |
|
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: 74.91 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKG-----QQRTQ-- 173
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtDINKLKgkalrQLRRQig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 174 --FQGaLAYVPQRNQLFN--------TTVWRNL-TLDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQM 242
Cdd:cd03256 82 miFQQ-FNLIERLSVLENvlsgrlgrRSTWRSLfGLFPKEEKQRALAALERVGLLDKAYQ----------RADQLSGGQQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 243 RRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII 291
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVI 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
117-307 |
1.20e-15 |
|
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: 74.07 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 117 EPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEK-GQQRTQFQGALAYVPQRNQLFNT-TVWR 194
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPlDFQRDSIARGLLYLGHAPGIKTTlSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 195 NLTLDKPY-DRQDVHQALQAVNMDRIIDALpdgwhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQS 273
Cdd:cd03231 93 NLRFWHADhSDEQVEEALARVGLNGFEDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....
gi 1714390902 274 ELMHTVRELSQKIGVLIITHTFDLiQDSDTVIKV 307
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDL-GLSEAGARE 195
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
107-309 |
1.22e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE------KGQQRTQFQGALAY 180
Cdd:PRK13636 10 ELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrKGLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNTTVWR-------NLTLDKPYDRQDVHQALQAVNMDRIIDAlPDGWhtevgkvtnFSEGQMRRLSIARALLA 253
Cdd:PRK13636 89 QDPDNQLFSASVYQdvsfgavNLKLPEDEVRKRVDNALKRTGIEHLKDK-PTHC---------LSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQ---DSDTVIKVGK 309
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGltIIIATHDIDIVPlycDNVFVMKEGR 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
70-309 |
1.77e-15 |
|
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: 76.91 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 70 VAIDRVnKRLAAVKTEQTH--EDNVKSTTQEPLQKLIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLI 147
Cdd:TIGR00957 1251 VAVERL-KEYSETEKEAPWqiQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLT 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 148 KLLLNLLDPGKGSI--SAVN--EKGQQRTQFQgaLAYVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDAL 223
Cdd:TIGR00957 1330 LGLFRINESAEGEIiiDGLNiaKIGLHDLRFK--ITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSAL 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 224 PDGWHTEVGKV-TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSD 302
Cdd:TIGR00957 1408 PDKLDHECAEGgENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT 1487
|
....*..
gi 1714390902 303 TVIKVGK 309
Cdd:TIGR00957 1488 RVIVLDK 1494
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
103-293 |
1.80e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.51 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPS--QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKGQQR-TQFQ 175
Cdd:COG4525 4 LTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvPVTGPGADRgVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 176 G-ALayVPQRNQLFNTTVWRNLT-LDKPYDRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLSIAR 249
Cdd:COG4525 84 KdAL--LPWLNVLDNVAFGLRLRgVPKAERRARAEELLALVGLadfaRRRIWQL--------------SGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 250 ALLAHKQFLIMDEPFSDLDA--RNQ-SELMHTVRELSQKiGVLIITH 293
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDAltREQmQELLLDVWQRTGK-GVFLITH 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
103-293 |
1.96e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEpvfeKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISavnekgqqrtqFQGA--LAY 180
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL-----------WNGQdlTAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VP---------QRNQLFN-TTVWRN--------LTLDKPyDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQM 242
Cdd:COG3840 67 PPaerpvsmlfQENNLFPhLTVAQNiglglrpgLKLTAE-QRAQVEQALERVGLAGLLDRLPG----------QLSGGQR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 243 RRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL--SQKIGVLIITH 293
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcrERGLTVLMVTH 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
109-304 |
2.47e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 109 DFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVN--EKGQQRTQFQGALAYVP 182
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgKPLDysKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNTTV-------WRNLTLDKPYDRQDVHQALQAVnmdriidalpDGWHTEVGKVTNFSEGQMRRLSIARALLAHK 255
Cdd:PRK13638 86 PEQQIFYTDIdsdiafsLRNLGVPEAEITRRVDEALTLV----------DAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQD-SDTV 304
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEiSDAV 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
105-309 |
3.30e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.02 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVNEKGQQRTQFQGALAY 180
Cdd:PRK13648 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNFEKLRKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 VPQRNQLFNTTVWRNLTLD-----KPYDR--QDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLA 253
Cdd:PRK13648 90 QNPDNQFVGSIVKYDVAFGlenhaVPYDEmhRRVSEALKQVDMLERADYEPN----------ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQ--DSDTVIKVGK 309
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEamEADHVIVMNK 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
115-309 |
4.17e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 115 QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLiklllnlldpgkgsISAVneKGQQRTQFQGALAYVPQRNqlfnttVWR 194
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTL--------------LRLL--AGALKGTPVAGCVDVPDNQ------FGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 195 NLTL-DKPYDRQDVHQALQAVNMDRIIDALpdgwhTEVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQS 273
Cdd:COG2401 99 EASLiDAIGRKGDFKDAVELLNAVGLSDAV-----LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1714390902 274 ELMHTVRELSQK--IGVLIITHTFDLIQD--SDTVIKVGK 309
Cdd:COG2401 174 RVARNLQKLARRagITLVVATHHYDVIDDlqPDLLIFVGY 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
102-305 |
5.35e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYPSQTE-PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLD-----------PGKGSISA------ 163
Cdd:PTZ00265 1165 KIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknEHTNDMTNeqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 164 ----------VNE--------KGQQRTQFQGA---------------------LAYVPQRNQLFNTTVWRNLTLDKP-YD 203
Cdd:PTZ00265 1245 deeqnvgmknVNEfsltkeggSGEDSTVFKNSgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKEdAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 204 RQDVHQALQAVNMDRIIDALPDGWHTEVGKV-TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL 282
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260
....*....|....*....|....*
gi 1714390902 283 SQKIGVLIIT--HTFDLIQDSDTVI 305
Cdd:PTZ00265 1405 KDKADKTIITiaHRIASIKRSDKIV 1429
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
115-309 |
5.86e-15 |
|
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: 72.25 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 115 QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEKGQQRTQFQ----GALAYVPQrnqLF-N 189
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-FDGKSYQKNIEAlrriGALIEAPG---FYpN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 TTVWRNL-TLDKPYD--RQDVHQALQAVNMDriidalpdgwHTEVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSD 266
Cdd:cd03268 87 LTARENLrLLARLLGirKKRIDEVLDVVGLK----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 267 LDARNQSELMHTVRELSQK-IGVLIITHTF---DLIQDSDTVIKVGK 309
Cdd:cd03268 157 LDPDGIKELRELILSLRDQgITVLISSHLLseiQKVADRIGIINKGK 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
107-298 |
6.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.19 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGALAYVPQR-- 184
Cdd:PRK13639 6 DLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI---KGEPIKYDKKSLLEVRKTvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 -------NQLFNTTVWR-------NLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwHtevgkvtNFSEGQMRRLSIARA 250
Cdd:PRK13639 82 ivfqnpdDQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPP---H-------HLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 251 LLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLI 298
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLV 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
105-300 |
1.37e-14 |
|
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: 71.28 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVNE-KGQQRTQFQGALA 179
Cdd:cd03292 3 FINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngQDVSDlRGRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLF-NTTVWRNLTL------DKPYD-RQDVHQALQAVNMDRIIDALPDGwhtevgkvtnFSEGQMRRLSIARAL 251
Cdd:cd03292 82 VVFQDFRLLpDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE----------LSGGEQQRVAIARAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 252 LAHKQFLIMDEPFSDLDARNQSELMhTVRELSQKIG--VLIITHTFDLIQD 300
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIM-NLLKKINKAGttVVVATHAKELVDT 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
107-293 |
1.87e-14 |
|
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: 71.38 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-------SAVNEKGQQ--RTQFqga 177
Cdd:cd03261 5 GLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgediSGLSEAELYrlRRRM--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 lAYVPQRNQLFNT-TVWRN--------LTLDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIA 248
Cdd:cd03261 80 -GMLFQSGALFDSlTVFENvafplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPA----------ELSGGMKKRVALA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 249 RALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITH 293
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGltSIMVTH 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
123-305 |
2.69e-14 |
|
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: 70.93 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGA---LAYVPQRNQLF-NTTVWRNL-- 196
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIPRLFpELTVLENVmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 --------TLDKPYDRQDVHQALQAVnmDRIIDA--LPDGWHTEVGkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSD 266
Cdd:cd03219 99 aaqartgsGLLLARARREEREARERA--EELLERvgLADLADRPAG---ELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1714390902 267 LDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTVI 305
Cdd:cd03219 174 LNPEETEELAELIRELRERgITVLLVEHDMDVVMSlADRVT 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
115-293 |
3.78e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.88 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 115 QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKGQQR-TQFQGAlAYVPQRNQLFN 189
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkPVEGPGAERgVVFQNE-GLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 TTVWRNLT-LDKPYDRQDVHQALQAVNMD----RIIdalpdgWHtevgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPF 264
Cdd:PRK11248 91 VAFGLQLAgVEKMQRLEIAHQMLKKVGLEgaekRYI------WQ--------LSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 265 SDLDA--RNQ-SELMHTVRELSQKiGVLIITH 293
Cdd:PRK11248 157 GALDAftREQmQTLLLKLWQETGK-QVLLITH 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
105-305 |
5.89e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.40 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRT--QFQGALAYVP 182
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlkEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QR--NQLFNTTVWRNLTL---DKPYDRQD----VHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLA 253
Cdd:PRK13632 90 QNpdNQFIGATVEDDIAFgleNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ----------NLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSE---LMHTVRELSQKIgVLIITHTFDLIQDSDTVI 305
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREikkIMVDLRKTRKKT-LISITHDMDEAILADKVI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
105-300 |
7.68e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEpvFEK-----LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE--------KGQQR 171
Cdd:PRK13641 5 FENVDYIYSPGTP--MEKkgldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 172 TQFQGALAYVPQRNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNM-DRIIDALPdgwhtevgkvTNFSEGQMR 243
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLkdvefgpKNFGFSEDEAKEKALKWLKKVGLsEDLISKSP----------FELSGGQMR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELsQKIG--VLIITHTFDLIQD 300
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGhtVILVTHNMDDVAE 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
118-293 |
8.03e-14 |
|
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: 69.49 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQF------QGALAYVPQRNQLF-NT 190
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL---DGQDITKLpmhkraRLGIGYLPQEASIFrKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 191 TVWRNL-------TLDKPYDRQDVHQALQAVNMDRIIDALPDGwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:cd03218 91 TVEENIlavleirGLSKKEREEKLEELLEEFHITHLRKSKASS----------LSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1714390902 264 FSDLDARNQSELMHTVRELSQK-IGVLIITH 293
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRgIGVLITDH 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
107-305 |
1.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.73 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTE----PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-----SAVNEKGQQRTQFQGA 177
Cdd:PRK13633 9 NVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdglDTSDEENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 LAYVPQRNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwHTevgkvtnFSEGQMRRLSIARA 250
Cdd:PRK13633 89 MVFQNPDNQIVATIVEedvafgpENLGIPPEEIRERVDESLKKVGMYEYRRHAP---HL-------LSGGQKQRVAIAGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 251 LLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK--IGVLIITHTFDLIQDSDTVI 305
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRII 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
121-296 |
1.79e-13 |
|
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: 68.65 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 121 EKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGALAYVPQRNQLFN-TTVWRNL--- 196
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL---EGKQITEPGPDRMVVFQNYSLLPwLTVRENIala 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 ------TLDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDAR 270
Cdd:TIGR01184 79 vdrvlpDLSKSERRAIVEEHIALVGLTEAADKRPG----------QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*...
gi 1714390902 271 NQSELMHTVRELSQKIGV--LIITHTFD 296
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVtvLMVTHDVD 176
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
119-309 |
2.70e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.36 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAYVPQRNQLF-NTTVWRN-- 195
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFpHMSLGENvg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 -----LTLDKPYDRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLSIARALLAHKQFLIMDEPFSD 266
Cdd:PRK11432 101 yglkmLGVPKEERKQRVKEALELVDLagfeDRYVDQI--------------SGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 267 LDARNQSELMHTVRELSQKIGV--LIITH----TFDLiqdSDTVIKVGK 309
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNItsLYVTHdqseAFAV---SDTVIVMNK 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
118-291 |
2.96e-13 |
|
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: 67.84 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISavnekgqqrtqFQGA--------------LAYVPQ 183
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR-----------FDGRditglppheraragIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 RNQLF-NTTVWRNLTL-DKPYDRQDVHQALqavnmDRIID---ALPDGWHTEVGkvtNFSEGQMRRLSIARALLAHKQFL 258
Cdd:cd03224 83 GRRIFpELTVEENLLLgAYARRRAKRKARL-----ERVYElfpRLKERRKQLAG---TLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190
....*....|....*....|....*....|....
gi 1714390902 259 IMDEPFSDLDARNQSELMHTVRELSQK-IGVLII 291
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLV 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
123-298 |
3.34e-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: 67.68 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLlDPGKGSIS---AVNEKGQQRTQFQGALAYVPQRNQLFNT-TVWRNLTL 198
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTSgqiLFNGQPRKPDQFQKCVAYVRQDDILLPGlTVRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 199 DkpydrqdVHQALQAVNMDRIIDA------LPDGWHTEVG--KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDAR 270
Cdd:cd03234 105 T-------AILRLPRKSSDAIRKKrvedvlLRDLALTRIGgnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1714390902 271 NQSELMHTVRELSQKIGVLIIT---------HTFDLI 298
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTihqprsdlfRLFDRI 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
102-301 |
1.00e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQG----- 176
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL---GDKPISMLSSrqlar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 177 ALAYVPQ-----------------RNQLFNttVWRNLTLDkpyDRQDVHQALQAVNmdriIDALPDgwhtevGKVTNFSE 239
Cdd:PRK11231 77 RLALLPQhhltpegitvrelvaygRSPWLS--LWGRLSAE---DNARVNQAMEQTR----INHLAD------RRLTDLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1714390902 240 GQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKiGVLIITHTFDLIQDS 301
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQAS 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
109-293 |
1.61e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 109 DFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGkgsISAVNE---KGQQRTQF---QGALAYVP 182
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEvllNGRRLTALpaeQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLF-NTTVWRNL------TLDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHK 255
Cdd:COG4136 83 QDDLLFpHLSVGENLafalppTIGRAQRRARVEQALEEAGLAGFADRDPA----------TLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1714390902 256 QFLIMDEPFSDLDA--RNQselmhtVREL------SQKIGVLIITH 293
Cdd:COG4136 153 RALLLDEPFSKLDAalRAQ------FREFvfeqirQRGIPALLVTH 192
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
118-293 |
1.62e-12 |
|
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: 65.82 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAYVPQRNQLF-NTTVWRNL 196
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 TL-----------DKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLIMDEPFS 265
Cdd:cd03296 96 AFglrvkprserpPEAEIRAKVHELLKLVQLDWLADRYP----------AQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 266 DLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELHVttVFVTH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
119-298 |
2.11e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnekgqqRTQFQGALAYVPQRNQLFNT---TVWRN 195
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQKLYLDTTlplTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LTLDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSEL 275
Cdd:PRK09544 90 LRLRPGTKKEDILPALKRVQAGHLIDA----------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|....*
gi 1714390902 276 MHTVRELSQKI--GVLIITHTFDLI 298
Cdd:PRK09544 160 YDLIDQLRRELdcAVLMVSHDLHLV 184
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
124-309 |
2.67e-12 |
|
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: 63.60 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISavnekgqqrtqFQGalayvpqrnqlfnttvwrnltldKPYD 203
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------VDG-----------------------KEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 204 RQDVHQALQAvnmdriidalpdGwhteVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL- 282
Cdd:cd03216 66 FASPRDARRA------------G----IAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLr 129
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 283 SQKIGVLIITHTFDLIQD-SD--TVIKVGK 309
Cdd:cd03216 130 AQGVAVIFISHRLDEVFEiADrvTVLRDGR 159
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
118-298 |
3.11e-12 |
|
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: 64.99 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQF------QGALAYVPQRNQLFNT- 190
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI---DGQDITHLpmheraRLGIGYLPQEASIFRKl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 191 TVWRNL--------TLDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:TIGR04406 92 TVEENImavleirkDLDRAEREERLEALLEEFQISHLRDN----------KAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1714390902 263 PFSDLDARNQSELMHTVRELSQK-IGVLIITH----TFDLI 298
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERgIGVLITDHnvreTLDIC 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
124-296 |
3.31e-12 |
|
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: 66.28 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVNEK---GQQRTQF----QGALAYVPQRNQLFNT-TVWRN 195
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI-RLGGEvlqDSARGIFlpphRRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LTldkpYDRQDVHQALQAVNMDRIIDALpdgwhtEVG-----KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDAR 270
Cdd:COG4148 98 LL----YGRKRAPRAERRISFDEVVELL------GIGhlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180
....*....|....*....|....*...
gi 1714390902 271 NQSELMHTVRELSQKIG--VLIITHTFD 296
Cdd:COG4148 168 RKAEILPYLERLRDELDipILYVSHSLD 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
48-304 |
3.98e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 48 IGSILDPFM---SLPVVTSFLAqqkvAIDRVNKRLAAVKTEQTHEDNVKSTTQEPLQKLIFHNVDFTYPSQTE-PVFEKL 123
Cdd:PTZ00265 329 LGVLISMFMltiILPNITEYMK----SLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDvEIYKDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI---SAVNEKGQQRTQFQGALAYVPQRNQLFNTTVWRN----- 195
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiinDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNikysl 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 --------------------------------------------------LTLDKPY---DRQDVHQALQAVNMDRIIDA 222
Cdd:PTZ00265 485 yslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnelIEMRKNYqtiKDSEVVDVSKKVLIHDFVSA 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 223 LPDGWHTEVGK-VTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL--SQKIGVLIITHTFDLIQ 299
Cdd:PTZ00265 565 LPDKYETLVGSnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIR 644
|
....*
gi 1714390902 300 DSDTV 304
Cdd:PTZ00265 645 YANTI 649
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
105-300 |
7.61e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTY----PSQTEPVFEkLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--------SAVNEKGQQRT 172
Cdd:PRK13643 4 FEKVNYTYqpnsPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsSTSKQKEIKPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 173 QFQGALAYVPQRNQLFNTTVWR-------NLTLDKPYDRQDVHQALQAVNMDRiidalpDGWHTEVGKVtnfSEGQMRRL 245
Cdd:PRK13643 83 RKKVGVVFQFPESQLFEETVLKdvafgpqNFGIPKEKAEKIAAEKLEMVGLAD------EFWEKSPFEL---SGGQMRRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 246 SIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD 300
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVAD 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
103-305 |
9.84e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.27 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTePvFEKL-----NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISA-----VNEKGQQRT 172
Cdd:PRK13634 3 ITFQKVEHRYQYKT-P-FERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgerviTAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 173 Q---------FQgalayVPQrNQLFNTTVWR-------NLTLDKPYDRQDVHQALQAVNMDR-IIDALPdgwhtevgkvT 235
Cdd:PRK13634 81 KplrkkvgivFQ-----FPE-HQLFEETVEKdicfgpmNFGVSEEDAKQKAREMIELVGLPEeLLARSP----------F 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 236 NFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII--THTF-DLIQDSDTVI 305
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVlvTHSMeDAARYADQIV 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
107-275 |
1.01e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.11 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFT-YPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnekgqqrtQFQGALAYVPQRN 185
Cdd:cd03291 39 NLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFSSQFS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 186 QLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVGK-VTNFSEGQMRRLSIARALLAHKQFLIMDEPF 264
Cdd:cd03291 108 WIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEgGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|.
gi 1714390902 265 SDLDARNQSEL 275
Cdd:cd03291 188 GYLDVFTEKEI 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
125-293 |
1.80e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 125 LSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQfQGALAYVPQRNQL---FNTTV--------- 192
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-KNLVAYVPQSEEVdwsFPVLVedvvmmgry 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 193 ----WrnLTLDKPYDRQDVHQALQAVNMdriidalPDGWHTEVGKVtnfSEGQMRRLSIARALLAHKQFLIMDEPFSDLD 268
Cdd:PRK15056 107 ghmgW--LRRAKKRDRQIVTAALARVDM-------VEFRHRQIGEL---SGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180
....*....|....*....|....*.
gi 1714390902 269 ARNQSELMHTVREL-SQKIGVLIITH 293
Cdd:PRK15056 175 VKTEARIISLLRELrDEGKTMLVSTH 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
103-293 |
2.50e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.58 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTT--------LiklllnllDPGKGSIsAVNEKG------ 168
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTllrmiagfE--------TPDSGRI-LLDGRDvtglpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 169 QQRtqfqgALAYVPQRNQLF-NTTVWRNLT-------LDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEG 240
Cdd:COG3842 75 EKR-----NVGMVFQDYALFpHLTVAENVAfglrmrgVPKAEIRARVAELLELVGLEGLADRYPH----------QLSGG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 241 QMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGItfIYVTH 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
106-305 |
2.87e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 106 HNVDFTY-PSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRT--QFQGALAYVP 182
Cdd:PRK13650 8 KNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QR--NQLFNTTV-------WRNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLA 253
Cdd:PRK13650 88 QNpdNQFVGATVeddvafgLENKGIPHEEMKERVNEALELVGMQDFKEREP----------ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFDLIQDSDTVI 305
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmtVISITHDLDEVALSDRVL 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
123-296 |
3.25e-11 |
|
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: 62.00 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDP--GKGSI---SAVNEKGQQRTQfqgaLAYVPQrnqlfNTTVWRNLT 197
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtsGRATVaghDVVREPREVRRR----IGIVFQ-----DLSVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 ldkPYDRQDVHQALQAVNMDRI---IDALPDG---WHTEVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARN 271
Cdd:cd03265 90 ---GWENLYIHARLYGVPGAERrerIDELLDFvglLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180
....*....|....*....|....*..
gi 1714390902 272 QSELMHTVRELSQKIG--VLIITHTFD 296
Cdd:cd03265 167 RAHVWEYIEKLKEEFGmtILLTTHYME 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
107-282 |
4.28e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQR--TQFQGALAYVPQR 184
Cdd:PRK09536 8 DLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaRAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQL-FNTTVWRNLTLDK-----------PYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALL 252
Cdd:PRK09536 86 TSLsFEFDVRQVVEMGRtphrsrfdtwtETDRAAVERAMERTGVAQFADR----------PVTSLSGGERQRVLLARALA 155
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 253 AHKQFLIMDEPFSDLDARNQSELMHTVREL 282
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRL 185
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
123-305 |
5.04e-11 |
|
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: 61.98 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS------------AVNEKGQQRTqFQG-------------A 177
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphRIARLGIART-FQNprlfpeltvlenvL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 LAYVPQRNQLFNTTVWRNLTLDKPYD--RQDVHQALQAVNMDRIIDALpdgwhtevgkVTNFSEGQMRRLSIARALLAHK 255
Cdd:COG0411 102 VAAHARLGRGLLAALLRLPRARREEReaRERAEELLERVGLADRADEP----------AGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVRELS--QKIGVLIITHTFDLIQD-SDTVI 305
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGlADRIV 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
105-293 |
5.67e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.13 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGA-LAYVPQ 183
Cdd:PRK13537 10 FRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 RNQLF-NTTVWRNLTLDKPY-------DRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHK 255
Cdd:PRK13537 88 FDNLDpDFTVRENLLVFGRYfglsaaaARALVPPLLEFAKLENKADA----------KVGELSGGMKRRLTLARALVNDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITH 293
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
103-268 |
6.28e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSqtEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnEKGqQRTQfqgaLAYVP 182
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLG-ETVK----IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLFNT--TVWRNLTLDKPYDR-QDVHQALQAVNMDriidalPDGWHTEVGKvtnFSEGQMRRLSIARALLAHKQFLI 259
Cdd:COG0488 385 QHQEELDPdkTVLDELRDGAPGGTeQEVRGYLGRFLFS------GDDAFKPVGV---LSGGEKARLALAKLLLSPPNVLL 455
|
....*....
gi 1714390902 260 MDEPFSDLD 268
Cdd:COG0488 456 LDEPTNHLD 464
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
103-305 |
8.13e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTEPVFEKLN---LSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKG-------SISAVNEKGQQRT 172
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 173 QFQGALAYVPQ--RNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDgwhtEVGKVTNF--SEGQMRRLSIA 248
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPE----DYVKRSPFelSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 249 RALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHTFD-LIQDSDTVI 305
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDqVLRIADEVI 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
106-299 |
8.27e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 106 HNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE-----KGQQRTQFQGALAY 180
Cdd:PRK10419 16 GGLSGKHQHQT--VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklNRAQRKAFRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 181 V---------PQRnqlfnTTVW------RNLT-LDKPYDRQDVHQALQAVNMD-RIIDALPdgwhtevgkvTNFSEGQMR 243
Cdd:PRK10419 94 VfqdsisavnPRK-----TVREiireplRHLLsLDKAERLARASEMLRAVDLDdSVLDKRP----------PQLSGGQLQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITHTFDLIQ 299
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVE 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
103-293 |
8.97e-11 |
|
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: 60.35 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGA---LA 179
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI---GGRDVTDLPPKdrdIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLF-NTTVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARAL 251
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFglklrkvPKDEIDERVREVAELLQIEHLLDRKP----------KQLSGGQRQRVALGRAI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 252 LAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII--TH 293
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIyvTH 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
105-293 |
1.42e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.39 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGA-LAYVPQ 183
Cdd:PRK13536 44 LAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARArIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 RNQL-FNTTVWRNLTLDKPYDRqdvhqaLQAVNMDRIIDALPDGWHTEV---GKVTNFSEGQMRRLSIARALLAHKQFLI 259
Cdd:PRK13536 122 FDNLdLEFTVRENLLVFGRYFG------MSTREIEAVIPSLLEFARLESkadARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190
....*....|....*....|....*....|....*
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRE-LSQKIGVLIITH 293
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSlLARGKTILLTTH 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
105-304 |
1.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 60.53 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTE---PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS---------AVNEKGQQRT 172
Cdd:PRK13649 5 LQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 173 QFQGALAYVPQrNQLFNTTVWRNLTLDkPYD-----RQDVHQALQAVNMDRIIDALPDGWHTEVgkvtnfSEGQMRRLSI 247
Cdd:PRK13649 85 KKVGLVFQFPE-SQLFEETVLKDVAFG-PQNfgvsqEEAEALAREKLALVGISESLFEKNPFEL------SGGQMRRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 248 ARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD-SDTV 304
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFV 215
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
102-305 |
2.01e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 59.92 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLD--PGKGSISAVNEKGQQRTQFQGALA 179
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDifDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWH---TEVGKvtNFSEGQMRRLSIARALLAHKQ 256
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvTEGGE--NFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 257 FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVL 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
112-305 |
2.28e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 112 YPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGS-------ISAVNEKgQQRTQfqgaLAYVPQR 184
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTllfegedISTLKPE-IYRQQ----VSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQLFNTTVWRNLTLdkPYD-RQdvhqalQAVNMDRIID-----ALPDgwHTEVGKVTNFSEGQMRRLSIARALLAHKQFL 258
Cdd:PRK10247 90 PTLFGDTVYDNLIF--PWQiRN------QQPDPAIFLDdlerfALPD--TILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 259 IMDEPFSDLD---ARNQSELMHT-VRElsQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PRK10247 160 LLDEITSALDesnKHNVNEIIHRyVRE--QNIAVLWVTHDKDEINHADKVI 208
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-262 |
2.35e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.97 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 23 LVGGLFLVKNNFLNLN--VMVGVwnagIGSILdpFMSLPVVT-----SFLAQQKVAIDRVNK---RLAAVktEQTHEDNV 92
Cdd:COG4615 246 LIGLILFLLPALGWADpaVLSGF----VLVLL--FLRGPLSQlvgalPTLSRANVALRKIEElelALAAA--EPAAADAA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 93 KSTTQEPLQKLIFHNVDFTYPS-QTEPVFE--KLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVN 165
Cdd:COG4615 318 APPAPADFQTLELRGVTYRYPGeDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILldgqPVT 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 166 EKGQQrtqfqgalAYvpqRnQLFnTTVW-------RNLTLDKPYDRQDVHQALQAVNMD---RIIDalpdgwhtevGKV- 234
Cdd:COG4615 398 ADNRE--------AY---R-QLF-SAVFsdfhlfdRLLGLDGEADPARARELLERLELDhkvSVED----------GRFs 454
|
250 260
....*....|....*....|....*....
gi 1714390902 235 -TNFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:COG4615 455 tTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
115-297 |
3.69e-10 |
|
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: 58.88 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 115 QTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS-AVNEKGQQRTQFQGALAYV-PQRNQLfnttv 192
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvAGLVPWKRRKKFLRRIGVVfGQKTQL----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 193 WRNLTLDKPY----DRQDVHQALQAVNMDRIIDALpdgwhtEVGK-----VTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:cd03267 107 WWDLPVIDSFyllaAIYDLPPARFKKRLDELSELL------DLEElldtpVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190
....*....|....*....|....*....|....
gi 1714390902 264 FSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
118-275 |
4.33e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnekgqqrtQFQGALAYVPQRNQLFNTTVWRNLT 197
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 LDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEVGK--VTnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSEL 275
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
105-293 |
4.44e-10 |
|
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: 58.79 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAYVPQR 184
Cdd:cd03300 3 LENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQLF-NTTVWRNLT-------LDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQ 256
Cdd:cd03300 81 YALFpHLTVFENIAfglrlkkLPKAEIKERVAEALDLVQLEGYANRKPS----------QLSGGQQQRVAIARALVNEPK 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 257 FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII--TH 293
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVfvTH 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
105-293 |
5.18e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvnEKGQQrtqfqgaLAYVPQR 184
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--PKGLR-------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQLF-NTTVW--------RNLTLDKPYDRQDVHQALQAVNMDRI------IDALpDGWHTEV-----------------G 232
Cdd:COG0488 70 PPLDdDLTVLdtvldgdaELRALEAELEELEAKLAEPDEDLERLaelqeeFEAL-GGWEAEAraeeilsglgfpeedldR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 233 KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDArnqselmHTVREL-----SQKIGVLIITH 293
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLeeflkNYPGTVLVVSH 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
118-309 |
5.26e-10 |
|
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: 60.41 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQ-FQGALAYVPQRNQLF-NTTVWRN 195
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDaVRQSLGMCPQHNILFhHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LTLD---KPYDRQDVHQALQAVNMDRIIDalpdgwHTEVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQ 272
Cdd:TIGR01257 1024 ILFYaqlKGRSWEEAQLEMEAMLEDTGLH------HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1714390902 273 SELMHTVRELSQKIGVLIITHTF---DLIQDSDTVIKVGK 309
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMdeaDLLGDRIAIISQGR 1137
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
124-309 |
5.69e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.85 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS------------AVNEKGQQRTqFQGALAY----------V 181
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhieglpghQIARMGVVRT-FQHVRLFremtvienllV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 182 PQRNQLfNTTVWRNLtLDKPYDRQDVHQALQ--AVNMDRIidALPDGWHTEVGkvtNFSEGQMRRLSIARALLAHKQFLI 259
Cdd:PRK11300 104 AQHQQL-KTGLFSGL-LKTPAFRRAESEALDraATWLERV--GLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQ--KIGVLIITHTFDL---IQDSDTVIKVGK 309
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLvmgISDRIYVVNQGT 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-293 |
6.60e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.51 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 100 LQKLI----FHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLD-----PGKGSISAVNEKGQQ 170
Cdd:PRK14258 1 MSKLIpaikVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 171 R----TQFQGALAYVPQRNQLFNTTVWRNLTLD------KPYDRQD--VHQALQAVNMdriIDALPDGWHTEVgkvTNFS 238
Cdd:PRK14258 79 RrvnlNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDdiVESALKDADL---WDEIKHKIHKSA---LDLS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 239 EGQMRRLSIARALLAHKQFLIMDEPFSDLD---ARNQSELMHTVReLSQKIGVLIITH 293
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDpiaSMKVESLIQSLR-LRSELTMVIVSH 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
123-291 |
7.10e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQrTQFQGALA-----------YVPQRNQLFN-- 189
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRT-VQREGRLArdirksrantgYIFQQFNLVNrl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 -------------TTVWRN-LTLDKPYDRQDVHQALQAVNMDriidalpdgwHTEVGKVTNFSEGQMRRLSIARALLAHK 255
Cdd:PRK09984 102 svlenvligalgsTPFWRTcFSWFTREQKQRALQALTRVGMV----------HFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII 291
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVV 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
107-298 |
7.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQ--------FQGaL 178
Cdd:PRK13652 8 DLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI---RGEPITKenirevrkFVG-L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 179 AYVPQRNQLFNTTVWR-------NLTLDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARAL 251
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPH----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 252 LAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII--THTFDLI 298
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLV 201
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
123-263 |
7.18e-10 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 57.92 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGA---LAYVPQRNQLFNT-TVWRNLTL 198
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVPQGREIFPRlTVEENLLT 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 199 DKPYdRQDVHQALQavnmDRIID---ALPDGWHTEVGkvtNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:TIGR03410 99 GLAA-LPRRSRKIP----DEIYElfpVLKEMLGRRGG---DLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
119-305 |
7.33e-10 |
|
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: 57.92 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKGQQRTQFQGALAYVPQRNQLF-NTTVW 193
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglKLTDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 194 RNLTL--------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFS 265
Cdd:cd03262 95 ENITLapikvkgmSKAEAEERALELLEKVGLADKADAYPA----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1714390902 266 DLDARNQSELMHTVRELSQ-KIGVLIITHTFDLIQD-SDTVI 305
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVI 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
107-305 |
8.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.46 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQG-----ALAYV 181
Cdd:PRK13644 6 NVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGirklvGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 182 PQRNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAH 254
Cdd:PRK13644 85 NPETQFVGRTVEedlafgpENLCLPPIEIRKRVDRALAEIGLEKYRHRSP----------KTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLI-ITHTFDLIQDSDTVI 305
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRII 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
107-297 |
8.83e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVNEK---GQQRTQFQGALAYVPQ 183
Cdd:PRK10575 16 NVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQpleSWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 R-NQLFNTTVwRNLTLDKPY------------DRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLS 246
Cdd:PRK10575 93 QlPAAEGMTV-RELVAIGRYpwhgalgrfgaaDREKVEEAISLVGLkplaHRLVDSL--------------SGGERQRAW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 247 IARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
103-293 |
1.02e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.15 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNE-----KGQQRTQFQGA 177
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaeaREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 lAYVPQRnqlfntTVWRNLTLDKPYD-RQDVHQALQAVNM-DRIID---ALpdgwhtevgkvtnfSEGQMRRLSIARALL 252
Cdd:PRK11247 91 -RLLPWK------KVIDNVGLGLKGQwRDAALQALAAVGLaDRANEwpaAL--------------SGGQKQRVALARALI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1714390902 253 AHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITH 293
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGftVLLVTH 192
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
103-293 |
1.23e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQ---QRTQFQGALA 179
Cdd:PRK10895 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNT-TVWRNLtLDKPYDRQDVHQALQAVNMDRIIDALPDGwHTEVGKVTNFSEGQMRRLSIARALLAHKQFL 258
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNL-MAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1714390902 259 IMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITH 293
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDH 195
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
204-297 |
1.54e-09 |
|
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: 58.14 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 204 RQDVHQALQAVNMD---RIIDALPdgwHtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVR 280
Cdd:COG0444 125 RERAIELLERVGLPdpeRRLDRYP---H-------ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLK 194
|
90
....*....|....*....
gi 1714390902 281 ELSQKIG--VLIITHtfDL 297
Cdd:COG0444 195 DLQRELGlaILFITH--DL 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
109-293 |
1.64e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 109 DFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKG--SISAVNEKGQQRTQFQGALAYVPQRNQ 186
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGqiQIDGKTATRGDRSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 187 LFNTTvwRNL----TLDKPYDRQDVHQALQAVNMDRIIDALpdgwhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:PRK13543 96 DLSTL--ENLhflcGLHGRRAKQMPGSALAIVGLAGYEDTL----------VRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 263 PFSDLDARNQSELMHTVR-ELSQKIGVLIITH 293
Cdd:PRK13543 164 PYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
124-296 |
1.80e-09 |
|
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: 57.27 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGS-------ISAVNEKGQQRTQ-------FQgALAYVPQRNQLFN 189
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKvlidgqdIAAMSRKELRELRrkkismvFQ-SFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 TTVWRNLT-LDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLD 268
Cdd:cd03294 123 VAFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPD----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 269 A--RN--QSELMHTVRELsqKIGVLIITHTFD 296
Cdd:cd03294 193 PliRRemQDELLRLQAEL--QKTIVFITHDLD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
119-299 |
2.00e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGA------LAYVPQRNQLFN-TT 191
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF---DGKDITDWQTAkimreaVAIVPEGRRVFSrMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 192 VWRNLTLDKPY-DRQDVHQALQavnmdRIIDALPDGWHTEVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPfsdldar 270
Cdd:PRK11614 97 VEENLAMGGFFaERDQFQERIK-----WVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP------- 164
|
170 180
....*....|....*....|....*....
gi 1714390902 271 nqselmhtvrelSQKIGVLIITHTFDLIQ 299
Cdd:PRK11614 165 ------------SLGLAPIIIQQIFDTIE 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
109-296 |
3.29e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 109 DFTYPSQTEPVfeKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAYVPQRNQLF 188
Cdd:PRK10771 6 DITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 189 N-TTVWRN--------LTLDkPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLI 259
Cdd:PRK10771 84 ShLTVAQNiglglnpgLKLN-AAQREKLHAIARQMGIEDLLARLP----------GQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 260 MDEPFSDLDARNQSELMHTVREL--SQKIGVLIITHTFD 296
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLE 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
129-309 |
3.57e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 129 KSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAYVPQRN--------------------QLF 188
Cdd:PRK13631 51 KNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKiknfkelrrrvsmvfqfpeyQLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 189 NTTVWR-------NLTLDKPYDRQDVHQALQAVNMDR-IIDALPDGwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:PRK13631 131 KDTIEKdimfgpvALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFG----------LSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1714390902 261 DEPFSDLDARNQSELMHTVRElSQKIG--VLIITHTFD-LIQDSDTVIKVGK 309
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNktVFVITHTMEhVLEVADEVIVMDK 251
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
103-293 |
3.72e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 57.08 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSqtEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS------AVNEKGQQRtqfqg 176
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlFTNLPPRER----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 177 ALAYVPQRNQLF-NTTVWRN-------LTLDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIA 248
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENiafglrvRPPSKAEIRARVEELLELVQLEGLADRYP----------SQLSGGQRQRVALA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 249 RALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGttVFVTH 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
107-297 |
3.94e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEK-GQQRTQFQGALAYVPQRn 185
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSiKKDLCTYQKQLCFVGHR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 186 qlfnTTVWRNLTLdkpydRQ----DVHQALQAVNMDRIIDALpdgwhtEVGKVTNF-----SEGQMRRLSIARALLAHKQ 256
Cdd:PRK13540 83 ----SGINPYLTL-----REnclyDIHFSPGAVGITELCRLF------SLEHLIDYpcgllSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1714390902 257 FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
119-293 |
4.39e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.07 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLD--PGKGSISAVNEKGQ-----------QRTQ--FQgalayVPq 183
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEARVSGEVYLDGQdifkmdvielrRRVQmvFQ-----IP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 rNQLFNTTVWRNLTLDKPYDR---------QDVHQALQAVnmdRIIDALPDGWHTEVGKVtnfSEGQMRRLSIARALLAH 254
Cdd:PRK14247 92 -NPIPNLSIFENVALGLKLNRlvkskkelqERVRWALEKA---QLWDEVKDRLDAPAGKL---SGGQQQRLCIARALAFQ 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITH 293
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
196-293 |
4.98e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LTLDKPYDRQDVHQALQAV---NMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQ 272
Cdd:PRK10418 107 LALGKPADDATLTAALEAVgleNAARVLKLYP----------FEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
90 100
....*....|....*....|...
gi 1714390902 273 SELMHTVRELSQK--IGVLIITH 293
Cdd:PRK10418 177 ARILDLLESIVQKraLGMLLVTH 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
122-298 |
5.16e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 122 KLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVN-------EKGQQRTQFQGALAYVPQRNQLF-NTTVW 193
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIV-LNgrvlfdaEKGICLPPEKRRIGYVFQDARLFpHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 194 RNLTLD-KPYDRQDVHQALQAVNMDRIIDALPdgwHTevgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQ 272
Cdd:PRK11144 95 GNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP---GS-------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180
....*....|....*....|....*...
gi 1714390902 273 SELMHTVRELSQ--KIGVLIITHTFDLI 298
Cdd:PRK11144 165 RELLPYLERLAReiNIPILYVSHSLDEI 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
103-305 |
5.19e-09 |
|
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: 55.36 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEKGQQrTQFQGALAYVP 182
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-FDGKPLD-IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQLF-NTTVWRNLT-------LDKPYDRQDVhqalqavnmDRIIDALPDGWHTEVgKVTNFSEGQMRRLSIARALLAH 254
Cdd:cd03269 77 EERGLYpKMKVIDQLVylaqlkgLKKEEARRRI---------DEWLERLELSEYANK-RVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQKiGVLII--THTFDLIQD-SDTVI 305
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVIlsTHQMELVEElCDRVL 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
123-291 |
5.39e-09 |
|
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: 55.76 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISavnekgqqrtqFQGA--------------LAYVPQRNQLF 188
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR-----------FDGEditglpphriarlgIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 189 -NTTVWRNLTL--DKPYDRQDVHQALqavnmDRIIDALP---DGWHTEVGkvtNFSEG--QMrrLSIARALLAHKQFLIM 260
Cdd:COG0410 91 pSLTVEENLLLgaYARRDRAEVRADL-----ERVYELFPrlkERRRQRAG---TLSGGeqQM--LAIGRALMSRPKLLLL 160
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 261 DEPFSDLDARNQSELMHTVREL-SQKIGVLII 291
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLnREGVTILLV 192
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
107-305 |
6.35e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.82 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEpvFEK-----LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--SAVN--EKGQQRTQFQGA 177
Cdd:PRK13637 7 NLTHIYMEGTP--FEKkaldnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiiDGVDitDKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 LAYVPQ--RNQLFNTTVW-------RNLTLDKPYDRQDVHQALQAVNMDRiiDALPDGWHTEVgkvtnfSEGQMRRLSIA 248
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLDY--EDYKDKSPFEL------SGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 249 RALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLII--THTF-DLIQDSDTVI 305
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHSMeDVAKLADRII 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
135-297 |
7.54e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 135 VVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAyvpQRNQLFNTT---VWRNltldkPYD-------- 203
Cdd:PRK11701 37 IVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA---ERRRLLRTEwgfVHQH-----PRDglrmqvsa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 204 -------------------RQDVHQALQAVNMDRI-IDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:PRK11701 109 ggnigerlmavgarhygdiRATAGDWLERVEIDAArIDDLP----------TTFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1714390902 264 FSDLDARNQSELMHTVRELSQKIG--VLIITHtfDL 297
Cdd:PRK11701 179 TGGLDVSVQARLLDLLRGLVRELGlaVVIVTH--DL 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
118-297 |
9.47e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.16 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGA-----LAYVPQRNQL-FNTT 191
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL---NGRPLADWSPAelarrRAVLPQHSSLsFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 192 V----------WRnltLDKPYDRQDVHQALQAVNM----DRIIDALpdgwhtevgkvtnfSEGQMRRLSIARAL--LAH- 254
Cdd:PRK13548 93 VeevvamgrapHG---LSRAEDDALVAAALAQVDLahlaGRDYPQL--------------SGGEQQRVQLARVLaqLWEp 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1714390902 255 ---KQFLIMDEPFSDLDARNQSELMHTVREL--SQKIGVLIITHtfDL 297
Cdd:PRK13548 156 dgpPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLH--DL 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
137-293 |
1.04e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.65 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 137 GHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQ--------QRTQFqGaLAYVPQRNQLF-NTTVWRNL-------TLDK 200
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIFL---DGEdithlpmhKRARL-G-IGYLPQEASIFrKLTVEDNIlavlelrKLSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 201 PYDRQDVHQALQAVNMDRIID----ALpdgwhtevgkvtnfSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELM 276
Cdd:COG1137 111 KEREERLEELLEEFGITHLRKskaySL--------------SGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQ 176
|
170
....*....|....*...
gi 1714390902 277 HTVRELSQK-IGVLIITH 293
Cdd:COG1137 177 KIIRHLKERgIGVLITDH 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
103-299 |
1.55e-08 |
|
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: 52.93 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnekgqQRTQfQGALAYVP 182
Cdd:cd03223 1 IELENLSLATPDGR-VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPE-GEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRnqlfnttvwrnltldkPYdrqdvhqalqavnmdriidaLPDG---------WHTEvgkvtnFSEGQMRRLSIARALLA 253
Cdd:cd03223 71 QR----------------PY--------------------LPLGtlreqliypWDDV------LSGGEQQRLAFARLLLH 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1714390902 254 HKQFLIMDEPFSDLDARNQSELMHTVRELSqkIGVLIITHTFDLIQ 299
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRPSLWK 152
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
119-293 |
1.71e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQG---ALAYVPQRNQLF-NTTVWR 194
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF---HGTDVSRLHArdrKVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 195 NLTL-----------DKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:PRK10851 94 NIAFgltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 264 FSDLDARNQSELMHTVRELSQ--KIGVLIITH 293
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVTH 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
123-299 |
2.37e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 54.34 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKGQQRtqfqgaLAYVPQRNQLF-NTTVWRNLT 197
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgePLDPEDRRR------IGYLPEERGLYpKMKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 ----LdKPYDRQDVHQALQAVnMDRIidALPDGWHTEVGKvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQS 273
Cdd:COG4152 94 ylarL-KGLSKAEAKRRADEW-LERL--GLGDRANKKVEE---LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVE 166
|
170 180
....*....|....*....|....*...
gi 1714390902 274 ELMHTVRELSQKiGVLII--THTFDLIQ 299
Cdd:COG4152 167 LLKDVIRELAAK-GTTVIfsSHQMELVE 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
117-293 |
2.68e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 117 EPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQrtqfqgaLAYVP--QR--NQLFNT-- 190
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML---DGVD-------LSHVPpyQRpiNMMFQSya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 191 -----TVWRNLTLDKPYDR-------QDVHQALQAVNMDRIIDALPdgwHtevgkvtNFSEGQMRRLSIARALLAHKQFL 258
Cdd:PRK11607 102 lfphmTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKP---H-------QLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1714390902 259 IMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVtcVMVTH 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
124-304 |
3.79e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNekGqQRTQFQGAL-------AYVPQRNQLFNT-TVWRN 195
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-LD--G-EPVRFRSPRdaqaagiAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 L----------TLDKPYDRQDVHQALQAVNMDriIDalPDgwhTEVGkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFS 265
Cdd:COG1129 100 IflgreprrggLIDWRAMRRRARELLARLGLD--ID--PD---TPVG---DLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1714390902 266 DLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQD-SDTV 304
Cdd:COG1129 170 SLTEREVERLFRIIRRLkAQGVAIIYISHRLDEVFEiADRV 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
107-305 |
4.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTE-PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEK--GQQRTQFQGALAYVPQ 183
Cdd:PRK13642 9 NLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 184 R--NQLFNTTVWRNLTL---DKPYDRQD----VHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAH 254
Cdd:PRK13642 89 NpdNQFVGATVEDDVAFgmeNQGIPREEmikrVDEALLAVNMLDFKTREP----------ARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 255 KQFLIMDEPFSDLDARNQSELMHTVRELSQK--IGVLIITHTFDLIQDSDTVI 305
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRIL 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
103-299 |
4.98e-08 |
|
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: 51.30 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSQtePVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavnEKGQQRTqfqgaLAYVP 182
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTVK-----IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QrnqlfnttvwrnltldkpydrqdvhqalqavnmdriidalpdgwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIMDE 262
Cdd:cd03221 70 Q-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|....*...
gi 1714390902 263 PFSDLDARNQSELmhtVRELSQ-KIGVLIITHTFDLIQ 299
Cdd:cd03221 97 PTNHLDLESIEAL---EEALKEyPGTVILVSHDRYFLD 131
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
135-292 |
5.95e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 135 VVGHNGAGKTTLIKLLLNLLDPG--KGSISAVNEKGQQRTQFQGALAYVPQRNQLFNT-TVWRNLT----------LDKP 201
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKGvkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTlTVREHLMfqahlrmprrVTKK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 202 YDRQDVHQALQAVNmdriidaLPDGWHTEVG---KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHT 278
Cdd:TIGR00955 136 EKRERVDEVLQALG-------LRKCANTRIGvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170
....*....|....
gi 1714390902 279 VRELSQKIGVLIIT 292
Cdd:TIGR00955 209 LKGLAQKGKTIICT 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
103-309 |
7.44e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYPSqtepV--FEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEKGQQRTQFQGALA- 179
Cdd:PRK11288 5 LSFDGIGKTFPG----VkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL-IDGQEMRFASTTAALAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 ----------YVPqrnqlfNTTVWRNLTL----------DKPYDRQDVHQALQAVNMDriIDalPDGwhtevgKVTNFSE 239
Cdd:PRK11288 80 gvaiiyqelhLVP------EMTVAENLYLgqlphkggivNRRLLNYEAREQLEHLGVD--ID--PDT------PLKYLSI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 240 GQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLI-ITHTFDLI---QDSDTVIKVGK 309
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIfalCDAITVFKDGR 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
123-300 |
8.58e-08 |
|
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: 53.27 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS-------------AVNEKGQQrTQFQGAL----AYVPQRN 185
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtkpGPDGRGRA-KRYIGILhqeyDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 186 QLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDR-----IIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLKMVGFDEekaeeILDKYPD----------ELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 261 DEPFSDLD--ARNQ--SELMHTVRELSQKIgvLIITHTFDLIQD 300
Cdd:TIGR03269 452 DEPTGTMDpiTKVDvtHSILKAREEMEQTF--IIVSHDMDFVLD 493
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
205-293 |
1.10e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 205 QDVHQALQAVNMDriidalPDGWHTevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQ 284
Cdd:PRK15134 403 QQVIAVMEEVGLD------PETRHR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQ 473
|
90
....*....|.
gi 1714390902 285 K--IGVLIITH 293
Cdd:PRK15134 474 KhqLAYLFISH 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
121-309 |
1.28e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 121 EKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI----SAVNEKGQQRTQFQGALAYVPQRNQLFNTTVWRNL 196
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgKEIDFKSSKEALENGISMVHQELNLVLQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 TLDKpY-------DRQDVHQALQAVNMDRIIDALPDGwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDA 269
Cdd:PRK10982 95 WLGR-YptkgmfvDQDKMYRDTKAIFDELDIDIDPRA------KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 270 RNQSELMHTVRELSQK-IGVLIITHTFD---LIQDSDTVIKVGK 309
Cdd:PRK10982 168 KEVNHLFTIIRKLKERgCGIVYISHKMEeifQLCDEITILRDGQ 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
207-280 |
1.74e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 207 VHQALQAVNMDRIIDALpdgwhteVG--KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVR 280
Cdd:PLN03140 995 VDEVMELVELDNLKDAI-------VGlpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
126-305 |
2.03e-07 |
|
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: 51.25 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 126 SILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKgqqrtqfqgaLAYVPQRNQL-FNTTVwRNLTLDK---- 200
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----------VSYKPQYIKAdYEGTV-RDLLSSItkdf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 201 ---PYDRQDVHQALQavnMDRIIDALpdgwhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMH 277
Cdd:cd03237 90 ythPYFKTEIAKPLQ---IEQILDRE----------VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 278 TVRE--LSQKIGVLIITHTFdLIQD--SDTVI 305
Cdd:cd03237 157 VIRRfaENNEKTAFVVEHDI-IMIDylADRLI 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
238-309 |
2.04e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 2.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKI--GVLIITHTFDLIQ---DSDTVIKVGK 309
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELnmGLLFITHNLSIVRklaDRVAVMQNGR 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
110-309 |
2.17e-07 |
|
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: 50.83 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 110 FTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS-----AVNEKGQQRTQfqgaLAYVPQR 184
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdVVKEPAEARRR----LGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 185 NQLFN-TTVWRNLTLDKPYDRQDVHQALQAVnmDRIIDALPDGWHTEVgKVTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:cd03266 87 TGLYDrLTARENLEYFAGLYGLKGDELTARL--EELADRLGMEELLDR-RVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1714390902 264 FSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQ---DSDTVIKVGK 309
Cdd:cd03266 164 TTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVErlcDRVVVLHRGR 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
101-293 |
2.53e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 101 QKLIFH--NVDFTYPSQTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIklllnlldpgkgSISAVNEK---GQQRTQFQ 175
Cdd:TIGR03719 1 AQYIYTmnRVSKVVPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMAGVDKdfnGEARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 176 GALAYVPQRNQLFNT-TVWRNLTL----------------------DKPYDR--------QDVHQALQAVNMDRII---- 220
Cdd:TIGR03719 68 IKVGYLPQEPQLDPTkTVRENVEEgvaeikdaldrfneisakyaepDADFDKlaaeqaelQEIIDAADAWDLDSQLeiam 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 221 DAL--PDGwhteVGKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELsqKIGVLIITH 293
Cdd:TIGR03719 148 DALrcPPW----DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
106-293 |
2.74e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.78 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 106 HNVDFTYPSqTEPVFEkLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEK---GQQRTQFQGAL---- 178
Cdd:PRK11124 6 NGINCFYGA-HQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRElrrn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 179 -AYVPQRNQLF-NTTVWRNLT--------LDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIA 248
Cdd:PRK11124 84 vGMVFQQYNLWpHLTVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP----------LHLSGGQQQRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1714390902 249 RALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQ-KIGVLIITH 293
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTH 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
125-293 |
2.77e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 125 LSILKSQITFVVGHNGAGKTTLIKLLLNLLD--PG---KGSI----SAVNEKGQQRTQFQGALAYVPQRNQLFNTTVWRN 195
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVtfhgKNLYAPDVDPVEVRRRIGMVFQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 196 LT-----------LDkpydrQDVHQAL-QAVNMDRIIDALPDGWhtevgkvTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:PRK14243 111 IAygaringykgdMD-----ELVERSLrQAALWDEVKDKLKQSG-------LSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|...
gi 1714390902 264 FSDLD---ARNQSELMHtvrELSQKIGVLIITH 293
Cdd:PRK14243 179 CSALDpisTLRIEELMH---ELKEQYTIIIVTH 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
204-297 |
2.83e-07 |
|
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: 51.61 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 204 RQDVHQALQAVNMDR-IIDALPdgwHtEvgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL 282
Cdd:COG4172 402 RARVAEALEEVGLDPaARHRYP---H-E------FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL 471
|
90
....*....|....*..
gi 1714390902 283 SQKIGV--LIITHtfDL 297
Cdd:COG4172 472 QREHGLayLFISH--DL 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
112-268 |
2.90e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 112 YPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDP-GKGSISAVNEKGQQRTQFQGALAYVPQRNQLFNT 190
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTeGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 191 TVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEV---GKVtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDL 267
Cdd:TIGR01271 1307 TFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLvdgGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
.
gi 1714390902 268 D 268
Cdd:TIGR01271 1385 D 1385
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
119-305 |
2.99e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.52 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--------SAVNEKGQQRT--QFQGALAYVPQRNQLF 188
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidTARSLSQQKGLirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 189 -NTTVWRNL----TLDKPYDRQDV----HQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLI 259
Cdd:PRK11264 98 pHRTVLENIiegpVIVKGEPKEEAtaraRELLAKVGLAGKETSYP----------RRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQ-KIGVLIITHTFDLIQD-SDTVI 305
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
107-307 |
3.15e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEP--VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVnekGQQRTQFQG-ALA---- 179
Cdd:PRK10535 9 DIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA---GQDVATLDAdALAqlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 ----YVPQRNQLF-NTTVWRNLTLDKPY-------DRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSI 247
Cdd:PRK10535 86 ehfgFIFQRYHLLsHLTAAQNVEVPAVYaglerkqRLLRAQELLQRLGLEDRVEYQP----------SQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1714390902 248 ARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKiG--VLIITHTFDLIQDSDTVIKV 307
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GhtVIIVTHDPQVAAQAERVIEI 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
124-309 |
4.49e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVNEKGQQRTQFQGALAY----VPQRNQLFNT-TVWRNLTL 198
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEI-LIDGKPVRIRSPRDAIALgigmVHQHFMLVPNlTVAENIVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 199 ---DKPY---DRQDVHQALQA--------VNMDRIIDALPdgwhteVgkvtnfseGQMRRLSIARALLAHKQFLIMDEPF 264
Cdd:COG3845 104 glePTKGgrlDRKAARARIRElserygldVDPDAKVEDLS------V--------GEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 265 SDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQD-SD--TVIKVGK 309
Cdd:COG3845 170 AVLTPQEADELFEILRRLaAEGKSIIFITHKLREVMAiADrvTVLRRGK 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
65-293 |
4.60e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 65 LAQQKVAIDRVNK-RLAAVKteqthEDNVKSTTQEPLQKLIFHNVDFTYPsqtEPVFE--KLNLSILKSQITFVVGHNGA 141
Cdd:PRK10522 289 LLSAQVAFNKLNKlALAPYK-----AEFPRPQAFPDWQTLELRNVTFAYQ---DNGFSvgPINLTIKRGELLFLIGGNGS 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 142 GKTTLIKLLLNLLDPGKGSISAVNEK--GQQRTQFQgalayvpqrnQLFN---TTVW---RNLTLD-KPYDRQDVHQALQ 212
Cdd:PRK10522 361 GKSTLAMLLTGLYQPQSGEILLDGKPvtAEQPEDYR----------KLFSavfTDFHlfdQLLGPEgKPANPALVEKWLE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 213 AVNMDRIIdalpdgwHTEVGKVTN--FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--V 288
Cdd:PRK10522 431 RLKMAHKL-------ELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGktI 503
|
....*
gi 1714390902 289 LIITH 293
Cdd:PRK10522 504 FAISH 508
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
119-297 |
4.93e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLdPGKGSISAVNEKGQ-----------QRTQFQGALAYVPQRNQ- 186
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGAPRGARVTGDvtlngeplaaiDAPRLARLRAVLPQAAQp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 187 LFNTTVwRNLTLDKPYDRQDVHQALQAVNMDRIIDALP-DGWHTEVGK-VTNFSEGQMRRLSIARAL---------LAHK 255
Cdd:PRK13547 95 AFAFSA-REIVLLGRYPHARRAGALTHRDGEIAWQALAlAGATALVGRdVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVRELSQ--KIGVLIITHTFDL 297
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNL 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
115-297 |
5.62e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.81 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 115 QTEpVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSisaVNEKGQQRTQFQGA---------LAYVPQRN 185
Cdd:PRK11629 21 QTD-VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD---VIFNGQPMSKLSSAakaelrnqkLGFIYQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 186 QLF-NTTVWRNLTL------DKPYDRQD-VHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQF 257
Cdd:PRK11629 97 HLLpDFTALENVAMplligkKKPAEINSrALEMLAAVGLEHRANHRP----------SELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1714390902 258 LIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITHTFDL 297
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQL 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
235-293 |
5.88e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.65 E-value: 5.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1714390902 235 TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQS---ELMHtvrELSQKIGVLIITH 293
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAkieELIL---ELKKDYTIVIVTH 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
91-293 |
7.35e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.95 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 91 NVKSTTQEPLQKLifHNVDFTYPSQTepVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQ 170
Cdd:PRK09452 5 NKQPSSLSPLVEL--RGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML---DGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 171 RTQF---QGALAYVPQRNQLF-NTTVWRN----LTLDK-PYD--RQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSE 239
Cdd:PRK09452 78 ITHVpaeNRHVNTVFQSYALFpHMTVFENvafgLRMQKtPAAeiTPRVMEALRMVQLEEFAQR----------KPHQLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390902 240 GQMRRLSIARALLAHKQFLIMDEPFSDLDAR----NQSELMHTVRELSqkIGVLIITH 293
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKlrkqMQNELKALQRKLG--ITFVFVTH 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
103-293 |
8.28e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 49.69 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTYpsQTEPVFEKLNLSILKSQITFVVGHNGAGKTTliklllnllDPGKGSIS----AVNEKG-QQRtqfqgA 177
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmiagleDPTSGEILiggrDVTDLPpKDR-----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 178 LAYVPQRNQLF-NTTVWRNLT-------LDKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIAR 249
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAfplklrkVPKAEIDRRVREAAELLGLEDLLDRKPK----------QLSGGQRQRVALGR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1714390902 250 ALLAHKQFLIMDEPFSDLDA--RNQ--SELmhtvRELSQKIGVLII--TH 293
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAklRVEmrAEI----KRLHRRLGTTTIyvTH 192
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
118-293 |
8.38e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI--SAVNEKGQQRTQFQGA---LAYVPQRNQLF-NTT 191
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfDGENIPAMSRSRLYTVrkrMSMLFQSGALFtDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 192 VWRNLT--------LDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:PRK11831 101 VFDNVAyplrehtqLPAPLLHSTVMMKLEAVGLRGAAKLMP----------SELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190
....*....|....*....|....*....|..
gi 1714390902 264 FSDLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELNSALGVtcVVVSH 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
237-297 |
8.58e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 8.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
235-294 |
9.96e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.07 E-value: 9.96e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 235 TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHT 294
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHS 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
119-299 |
1.10e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.21 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFqgALAYVPQRNQLF--NTTVWRNL 196
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL---DGEHIQHY--ASKEVARRIGLLaqNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 TLDKPYDR-QDVHQAL----QAVNMDRIIDALPDGWHTEVG--KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDA 269
Cdd:PRK10253 97 TVQELVARgRYPHQPLftrwRKEDEEAVTKAMQATGITHLAdqSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 270 RNQSELMHTVRELSQKIGVLIITHTFDLIQ 299
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQ 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
123-297 |
1.36e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLdPGKGSIS---------AVNEKGQQRtqfqgalAYVPQR-NQLFNTTV 192
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQfagqpleawSAAELARHR-------AYLSQQqTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 193 WRNLTLDKP-----YDRQD-VHQALQAVNMDriiDALPDgwhtevgKVTNFSEGQMRR-------LSIARALLAHKQFLI 259
Cdd:PRK03695 87 FQYLTLHQPdktrtEAVASaLNEVAEALGLD---DKLGR-------SVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHtfDL 297
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQgIAVVMSSH--DL 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
123-294 |
1.44e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLD--PGKGSISAVNEKGQQ----RT---QFQGALAYVPQRNQLFNTTVW 193
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEVTITGSIVYNGHNiyspRTdtvDLRKEIGMVFQQPNPFPMSIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 194 RNLTL--------DKPYDRQDVHQALQAVNM-DRIIDALPDgwhTEVGkvtnFSEGQMRRLSIARALLAHKQFLIMDEPF 264
Cdd:PRK14239 104 ENVVYglrlkgikDKQVLDEAVEKSLKGASIwDEVKDRLHD---SALG----LSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 265 SDLDARNQSELMHTVRELSQKIGVLIITHT 294
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDYTMLLVTRS 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
123-308 |
1.45e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsavNEKGQQRTQFQGALAY-------------VPQRNQLFN 189
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI---TINNINYNKLDHKLAAqlgigiiyqelsvIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 TTVWRNLT--------LDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMD 261
Cdd:PRK09700 101 LYIGRHLTkkvcgvniIDWREMRVRAAMMLLRVGLKVDLDE----------KVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 262 EPFSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQ---DSDTVIKVG 308
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRricDRYTVMKDG 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
237-297 |
1.46e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.93 E-value: 1.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
235-293 |
1.64e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.50 E-value: 1.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 235 TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITH 293
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
72-283 |
2.29e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 72 IDRVNKRLAAVKTEQTHEDNVKSTTQEPLQK--LIFHNVDFTYPSQtepvFEKLNLSILKS--------QITFVVGHNGA 141
Cdd:TIGR00956 725 NDIEAGEVLGSTDLTDESDDVNDEKDMEKESgeDIFHWRNLTYEVK----IKKEKRVILNNvdgwvkpgTLTALMGASGA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 142 GKTTLIKLLLNLLDPG--KGSISAVNEKGQQRTqFQGALAYVPQRN-QLFNTTVWRNLT----LDKP-----YDRQD-VH 208
Cdd:TIGR00956 801 GKTTLLNVLAERVTTGviTGGDRLVNGRPLDSS-FQRSIGYVQQQDlHLPTSTVRESLRfsayLRQPksvskSEKMEyVE 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 209 QALQAVNMDRIIDALpdgwhteVGKVtnfSEG----QMRRLSIARALLAHKQFLI-MDEPFSDLDARNQSELMHTVRELS 283
Cdd:TIGR00956 880 EVIKLLEMESYADAV-------VGVP---GEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA 949
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
238-309 |
3.49e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 3.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 238 SEGQMRRLSIARAL-LAHKQ---FLIMDEPFSDLDARNQSELMHTVRELSQKIG-VLIITHTFDLIQDSDTVIKVGK 309
Cdd:cd03227 79 SGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAqVIVITHLPELAELADKLIHIKK 155
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
118-293 |
3.74e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 118 PVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvneKGQQRTQFQGALAY------VPQRNQLF-NT 190
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI---GGNPCARLTPAKAHqlgiylVPQEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 191 TVWRNLTLDKPY---DRQDVHQALQAVNMDRIIDALpdgwhtevGKVTNFSEGQMrrLSIARALLAHKQFLIMDEPFSDL 267
Cdd:PRK15439 102 SVKENILFGLPKrqaSMQKMKQLLAALGCQLDLDSS--------AGSLEVADRQI--VEILRGLMRDSRILILDEPTASL 171
|
170 180
....*....|....*....|....*..
gi 1714390902 268 DARNQSELMHTVRELSQK-IGVLIITH 293
Cdd:PRK15439 172 TPAETERLFSRIRELLAQgVGIVFISH 198
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
237-297 |
3.98e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.80 E-value: 3.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITHtfDL 297
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLtyLFISH--DL 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
102-297 |
4.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 102 KLIFHNVDFTYPSQTEPVFEKL---NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNE-------KGQQR 171
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYEHQAIhdvNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDitithktKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 172 TQFQGALAYVPQ--RNQLFNTTVWRNLTLDKPYDRQDVHQAlqavnMDRIIDALPD-GWHTEVGKVTNF--SEGQMRRLS 246
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEV-----KNYAHRLLMDlGFSRDVMSQSPFqmSGGQMRKIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 247 IARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDL 297
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDM 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
119-293 |
4.66e-06 |
|
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: 48.01 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVNEKGQqrtqfqgaLAYVPQ-RNQLF-NTTVWRNL 196
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVK--------LAYVDQsRDALDpNKTVWEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 197 TldkpyDRQDvhqalqavnmdriidalpdgwHTEVGKVT----------NF------------SEGQMRRLSIARALLAH 254
Cdd:TIGR03719 408 S-----GGLD---------------------IIKLGKREipsrayvgrfNFkgsdqqkkvgqlSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 255 KQFLIMDEPFSDLDarnqselMHTVRELSQKI-----GVLIITH 293
Cdd:TIGR03719 462 GNVLLLDEPTNDLD-------VETLRALEEALlnfagCAVVISH 498
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
124-296 |
5.39e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 124 NLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGS----------ISAVNEKGQQRTQ----FQgALAYVPQRNQLFN 189
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlidgvdiakISDAELREVRRKKiamvFQ-SFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 TTVWRNLTLDKPYDRQD-VHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLD 268
Cdd:PRK10070 127 TAFGMELAGINAEERREkALDALRQVGLENYAHSYPD----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 269 ARNQSELMHTVRELSQK--IGVLIITHTFD 296
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhqRTIVFISHDLD 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
238-297 |
5.44e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 46.93 E-value: 5.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDL 297
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEF 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
123-309 |
6.36e-06 |
|
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: 47.51 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 123 LNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPG--KGSI----SAVNEKGQQRTQFQG------ALAYVPQRNQLFNT 190
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIywsgSPLKASNIRDTERAGiviihqELTLVPELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 191 TVWRNLTLdkPYDRQD-------VHQALQAVNMDRIIDALPdgwhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDEP 263
Cdd:TIGR02633 100 FLGNEITL--PGGRMAynamylrAKNLLRELQLDADNVTRP---------VGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1714390902 264 FSDLDARNQSELMHTVRELSQK-IGVLIITHTFD---LIQDSDTVIKVGK 309
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHgVACVYISHKLNevkAVCDTICVIRDGQ 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
119-293 |
7.38e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.50 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQGALAyVPQRNQL----------- 187
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLK-VADKNQLrllrtrltmvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 188 --FN----TTVWRN--------LTLDKPYDRQDVHQALQAVNMD-RIIDALPdgwhtevgkvTNFSEGQMRRLSIARALL 252
Cdd:PRK10619 99 qhFNlwshMTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIDeRAQGKYP----------VHLSGGQQQRVSIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1714390902 253 AHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITH 293
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTH 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
131-291 |
8.04e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 131 QITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQ--------QRTQ--FQGALAYVPQR---NQLFNTTVWRNLT 197
Cdd:PRK15112 40 QTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrsQRIRmiFQDPSTSLNPRqriSQILDFPLRLNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 LDKPYDRQDVHQALQAVNMdriidaLPD--GWHTEVgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSEL 275
Cdd:PRK15112 120 LEPEQREKQIIETLRQVGL------LPDhaSYYPHM-----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170
....*....|....*.
gi 1714390902 276 MHTVRELSQKIGVLII 291
Cdd:PRK15112 189 INLMLELQEKQGISYI 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
131-283 |
8.47e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 131 QITFVVGHNGAGKTTLIKLLLNLLDPG--KGSISAvneKGQQRTQ-FQGALAYVPQrnqlfnttvwrnltldkpydrQDV 207
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLAGRKTAGviTGEILI---NGRPLDKnFQRSTGYVEQ---------------------QDV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 208 HQALQAVNMDRIIDALPDGWHTEvgkvtnfsegQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELS 283
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVE----------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
119-293 |
1.22e-05 |
|
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: 46.00 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 119 VFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLD-PGKGSISAVNEKGQQRTQFQGALAYVPQRNQLFNTTVWRNLT 197
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNtEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 LDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEV---GKVtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSE 274
Cdd:cd03289 99 PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLvdgGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170
....*....|....*....
gi 1714390902 275 LMHTVRELSQKIGVLIITH 293
Cdd:cd03289 177 IRKTLKQAFADCTVILSEH 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
94-305 |
1.35e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 94 STTQEPLQ--KLIFHNVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISaVN--EKG- 168
Cdd:PTZ00243 1298 SAAPHPVQagSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR-VNgrEIGa 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 169 ----QQRTQFqgalAYVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDALPDGWHTEV---GkvTNFSEGQ 241
Cdd:PTZ00243 1377 yglrELRRQF----SMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVlegG--SNYSVGQ 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 242 MRRLSIARALLAHKQ-FLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTFDLIQDSDTVI 305
Cdd:PTZ00243 1451 RQLMCMARALLKKGSgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKII 1515
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
237-293 |
1.49e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 1.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISH 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
233-309 |
1.88e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 233 KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFD---LIQDSDTVIKVG 308
Cdd:PRK13549 140 PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNevkAISDTICVIRDG 219
|
.
gi 1714390902 309 K 309
Cdd:PRK13549 220 R 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
108-295 |
2.68e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 108 VDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRT--------QFQGALA 179
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifnyrdvlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVWRNLTLDKPYDRQDVHQALQAVNMDRIIDAlpDGWHTEVGKVTN----FSEGQMRRLSIARALLAHK 255
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1714390902 256 QFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTF 295
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
244-309 |
3.47e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 3.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELM----HTVRELSQKIGVLIITHTFDLIQDSDTVIKVGK 309
Cdd:PRK01156 815 RVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKdiieYSLKDSSDIPQVIMISHHRELLSVADVAYEVKK 884
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
107-305 |
7.44e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 107 NVDFTYPSQTEPVFEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS--------------AVNEKGQQRT 172
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqviELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 173 Q-FQGA-LAYVPQR-----NQLFNT--TVWRNLTLDKPYDRQD-VHQALQAVNMDRIIDAlpdgwHTEVGKVTNFSEGQM 242
Cdd:PRK10261 99 RhVRGAdMAMIFQEpmtslNPVFTVgeQIAESIRLHQGASREEaMVEAKRMLDQVRIPEA-----QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 243 R-RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKI--GVLIITHTFDLIQD-SDTVI 305
Cdd:PRK10261 174 RqRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsmGVIFITHDMGVVAEiADRVL 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
105-293 |
7.59e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.16 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYpSQTePVFEKLNLSILKSQITFVVGHNGAGKTTLI--KLLLNLLDPGK---GSISAVNEKGQQRTQFQGAlA 179
Cdd:PRK09493 4 FKNVSKHF-GPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcINKLEEITSGDlivDGLKVNDPKVDERLIRQEA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLF-NTTVWRNLT--------LDKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLSIARA 250
Cdd:PRK09493 81 MVFQQFYLFpHLTALENVMfgplrvrgASKEEAEKQARELLAKVGLAERAHHYP----------SELSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1714390902 251 LLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITH 293
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTH 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
238-300 |
8.13e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 8.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFDLIQD 300
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgITLVLVLNRFDEIPD 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
235-282 |
8.56e-05 |
|
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: 43.19 E-value: 8.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1714390902 235 TNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSelmhTVREL 282
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVEL 194
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
105-293 |
1.05e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPV--FEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-------SAVNEKG--QQRTQ 173
Cdd:COG1135 4 LENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgvdlTALSERElrAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 174 ----FQGAlayvpqrNqLFNT-TVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPDgwhtevgkvtNFSEGQ 241
Cdd:COG1135 84 igmiFQHF-------N-LLSSrTVAENVALpleiagvPKAEIRKRVAELLELVGLSDKADAYPS----------QLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 242 MRRLSIARALLAHKQFLIMDEPFSDLDARN-QS--ELmhtVRELSQKIG--VLIITH 293
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETtRSilDL---LKDINRELGltIVLITH 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
125-309 |
1.41e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 125 LSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIS----AVNEKGQQRTQFQG------ALAYVPQRNQLFN----- 189
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkEVTFNGPKSSQEAGigiihqELNLIPQLTIAENiflgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 190 --TTVWRNLTLDKPYDRQDvhQALQAVNmdriidaLPDGWHTEVGKVTnFSEGQMrrLSIARALLAHKQFLIMDEPFSDL 267
Cdd:PRK10762 105 efVNRFGRIDWKKMYAEAD--KLLARLN-------LRFSSDKLVGELS-IGEQQM--VEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1714390902 268 DARNQSELMHTVREL-SQKIGVLIITH----TFDlIQDSDTVIKVGK 309
Cdd:PRK10762 173 TDTETESLFRVIRELkSQGRGIVYISHrlkeIFE-ICDDVTVFRDGQ 218
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
244-309 |
1.49e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHT-VRELSQKIG--VLIITHTFDLIQDSDTVIKVGK 309
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEESLAEiIEERKSQKNfqLIVITHDEELVDAADHIYRVEK 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
238-292 |
1.75e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 1.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKiGVLIIT 292
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVT 261
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
105-298 |
1.94e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.48 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 105 FHNVDFTYPSQTEPV--FEKLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSIsAVNekGQQRTQFQGALAYVP 182
Cdd:PRK11153 4 LKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVD--GQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRN-----QLFN----TTVWRNLTL-------DKPYDRQDVHQALQAVNMDRIIDALPdgwhtevgkvTNFSEGQMRRLS 246
Cdd:PRK11153 81 RRQigmifQHFNllssRTVFDNVALplelagtPKAEIKARVTELLELVGLSDKADRYP----------AQLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 247 IARALLAHKQFLIMDEPFSDLD-ARNQS--ELMhtvRELSQKIG--VLIITHTFDLI 298
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDpATTRSilELL---KDINRELGltIVLITHEMDVV 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
238-302 |
2.20e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNqselmhtvRELSQK-IGVLI--------------------ITHTFD 296
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN--------RQLVRRfVDVLIsegetqllfvshhaedapacITHRLE 474
|
....*.
gi 1714390902 297 LIQDSD 302
Cdd:PRK10938 475 FVPDGD 480
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
198-308 |
2.35e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 198 LDKPYDRQDVHqALQAVNMDriidalpdgwHTEVGK-VTNFSEGQMRRLSIARALLA---HKQFLIMDEPFSDLDARNQS 273
Cdd:PRK00635 781 LDEPSIHEKIH-ALCSLGLD----------YLPLGRpLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIK 849
|
90 100 110
....*....|....*....|....*....|....*.
gi 1714390902 274 ELMHTVRELS-QKIGVLIITHTFDLIQDSDTVIKVG 308
Cdd:PRK00635 850 ALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLELG 885
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
238-309 |
2.35e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 2.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 238 SEGQMRRLSIARALLAHKQ--FLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQDSDTVIKVGK 309
Cdd:cd03238 89 SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWIIDFGP 163
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
236-304 |
2.73e-04 |
|
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: 41.36 E-value: 2.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 236 NFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITHT---FDLIQdSDTV 304
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHYqrlLDYIK-PDRV 175
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
238-305 |
4.71e-04 |
|
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: 40.11 E-value: 4.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK-IGVLIITHTFD-LIQDSDTVI 305
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDeLLGLCDRIL 175
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
205-293 |
5.68e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 205 QDVHQALQAVNMDRII----DAL---PDGWhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMH 277
Cdd:PRK11819 130 QEIIDAADAWDLDSQLeiamDALrcpPWDA-----KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ 204
|
90
....*....|....*..
gi 1714390902 278 TVRELSqkiG-VLIITH 293
Cdd:PRK11819 205 FLHDYP---GtVVAVTH 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
130-298 |
7.09e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.94 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 130 SQITFVVGHNGAGKTTLIKLLLNLLDPG---KGSISAVNEKGQQ-RTQFQGALAYVPQrnqlfnttvwrnltldkpydrQ 205
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKYPGEIIYVSE---------------------E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 206 DVHQALQAV--NMDRIIDALPDGWhtevgkVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELS 283
Cdd:cd03233 92 DVHFPTLTVreTLDFALRCKGNEF------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMA 165
|
170 180
....*....|....*....|....*
gi 1714390902 284 QKIGV----------LIITHTFDLI 298
Cdd:cd03233 166 DVLKTttfvslyqasDEIYDLFDKV 190
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
238-301 |
8.73e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 8.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390902 238 SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQK--IGVLIITHTFDLIQDS 301
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEA 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
120-304 |
1.07e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 120 FEKLNLSILKS-QITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEKGQQRTQFQG--------ALA----------- 179
Cdd:COG1245 88 FRLYGLPVPKKgKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGtelqdyfkKLAngeikvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 180 YVPQRNQLFNTTVwRNLtLDKPYDRQDVHQALQAVNMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLI 259
Cdd:COG1245 168 YVDLIPKVFKGTV-REL-LEKVDERGKLDELAEKLGLENILDR----------DISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1714390902 260 MDEPFSDLDARNQSELMHTVRELSQKIG-VLIITHtfDL-IQD--SDTV 304
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKyVLVVEH--DLaILDylADYV 282
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
135-305 |
1.24e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.15 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 135 VVGHNGAGKTTLIKLLLNLLDPGKGSISavnekgqqrtqFQGALAYVPQrnqlfnttvwrnltldkpYDRQDVHQALQAV 214
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVD-----------EDLKISYKPQ------------------YISPDYDGTVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 215 NMDRIIDALPDGWH-TEVGK-----------VTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVREL 282
Cdd:COG1245 422 LRSANTDDFGSSYYkTEIIKplgleklldknVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*...
gi 1714390902 283 --SQKIGVLIITHTF---DLIqdSDTVI 305
Cdd:COG1245 502 aeNRGKTAMVVDHDIyliDYI--SDRLM 527
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
237-297 |
1.41e-03 |
|
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: 40.05 E-value: 1.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIG--VLIITHtfDL 297
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGmaLLLITH--DL 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
237-293 |
1.79e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.84 E-value: 1.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGV--LIITH 293
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISH 522
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
234-308 |
1.89e-03 |
|
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: 40.00 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 234 VTNFSEGQMRRLSIARALLA---HKQFLIMDEPFSDLDARNQSELMHTVREL-SQKIGVLIITHTFDLIQDSDTVIKVG 308
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVIEHNLDVIKTADYIIDLG 905
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
131-298 |
2.17e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 38.70 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 131 QITFVVGHNGAGKTTLIKLLLNLLDPGKGSI-----SAVNEKGQQRTQFQGALAYVPQRNQLF-NTTVWRNLTLD---KP 201
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNREVPFLRRQIGMIFQDHHLLmDRTVYDNVAIPliiAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 202 YDRQDVHQALQAVnMDRIidALPDgwhtevgKVTNF----SEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMH 277
Cdd:PRK10908 109 ASGDDIRRRVSAA-LDKV--GLLD-------KAKNFpiqlSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180
....*....|....*....|..
gi 1714390902 278 TVRELSQ-KIGVLIITHTFDLI 298
Cdd:PRK10908 179 LFEEFNRvGVTVLMATHDIGLI 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
233-298 |
2.42e-03 |
|
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: 38.89 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390902 233 KVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQ-KIGVLIITHtfDLI 298
Cdd:cd03236 136 NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEH--DLA 200
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
237-295 |
2.66e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.95 E-value: 2.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1714390902 237 FSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIITHTF 295
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
199-309 |
3.47e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 38.86 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 199 DKPYDRQDVHQALQAVNMDRIIDALPDGwhtevgkvtnFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHT 278
Cdd:PRK11000 106 KKEEINQRVNQVAEVLQLAHLLDRKPKA----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1714390902 279 VRELSQKIGVLIITHTFDLIQ-----------DSDTVIKVGK 309
Cdd:PRK11000 176 ISRLHKRLGRTMIYVTHDQVEamtladkivvlDAGRVAQVGK 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-305 |
3.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 3.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1714390902 244 RLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKIGVLIIT---HTFDLIQDSDTVI 305
Cdd:COG4717 572 RLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTcheELVELFQEEGAHV 636
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
236-296 |
4.14e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 38.14 E-value: 4.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390902 236 NFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVRELSQKiG--VLIITHTFD 296
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GktIILVTHDLD 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
127-305 |
6.77e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.87 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 127 ILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAvNEKgqqrtqfqgaLAYVPQRNQL-FNTTVWRNL-----TLDK 200
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELK----------ISYKPQYIKPdYDGTVEDLLrsitdDLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 201 PYDRQDVHQALQavnMDRIIDAlpdgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIMDEPFSDLDARNQSELMHTVR 280
Cdd:PRK13409 431 SYYKSEIIKPLQ---LERLLDK----------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|
gi 1714390902 281 EL--SQKIGVLIITHTF---DLIqdSDTVI 305
Cdd:PRK13409 498 RIaeEREATALVVDHDIymiDYI--SDRLM 525
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
103-275 |
8.44e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.77 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 103 LIFHNVDFTypSQTEPVFEkLNLSILKSQITFVVGHNGAGKTTLIKLLLNLLDPGKGSISAVNEkgQQRTQFQGALAYVP 182
Cdd:PRK13541 2 LSLHQLQFN--IEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC--NINNIAKPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390902 183 QRNQL-FNTTVWRNLTL-DKPYDRQDVHQAlqAVNMDRIIDALPDgwhtevgKVTNFSEGQMRRLSIARALLAHKQFLIM 260
Cdd:PRK13541 77 HNLGLkLEMTVFENLKFwSEIYNSAETLYA--AIHYFKLHDLLDE-------KCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170
....*....|....*
gi 1714390902 261 DEPFSDLDARNQSEL 275
Cdd:PRK13541 148 DEVETNLSKENRDLL 162
|
|
| |
