|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-265 |
0e+00 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 569.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 1 MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 81 KAFARKVAYLPQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
Cdd:PRK10575 81 KAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGET 240
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
250 260
....*....|....*....|....*
gi 15829409 241 LEMIYGIPMGILPHPAGAAPVSFVY 265
Cdd:PRK10575 241 LEQIYGIPMGILPHPAGAAPVSFVY 265
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-261 |
5.99e-135 |
|
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: 380.93 E-value: 5.99e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGI 251
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|
gi 15829409 252 LPHPAGAAPV 261
Cdd:COG1120 242 IEDPVTGRPL 251
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-255 |
1.91e-108 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 313.56 E-value: 1.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIGRYPWHGalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:COG4604 84 NHINSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILP 253
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVEE 241
|
..
gi 15829409 254 HP 255
Cdd:COG4604 242 ID 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-260 |
1.48e-98 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 288.84 E-value: 1.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVR 103
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
Cdd:PRK11231 95 ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 184 VDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILPHPAGAAP 260
Cdd:PRK11231 175 VELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIHPEPVSGTP 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-261 |
5.71e-94 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 277.00 E-value: 5.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 95 PPAEGMTVRELVAIGRYPWhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ-------DSR 167
Cdd:COG4559 85 SLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdgGPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGI 247
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGA 239
|
250
....*....|....
gi 15829409 248 PMGILPHPAGAAPV 261
Cdd:COG4559 240 DLRVLAHPEGGCPQ 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-261 |
1.29e-92 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 273.57 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 95 PPAEGMTVRELVAIGRYPWhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ------DSRC 168
Cdd:PRK13548 86 SLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIP 248
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGAD 241
|
250
....*....|...
gi 15829409 249 MGILPHPAGAAPV 261
Cdd:PRK13548 242 VLVQPHPETGAPL 254
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-230 |
2.10e-90 |
|
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: 265.07 E-value: 2.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 qlppaegmtvrelvaigrypwhgalgrfgaadrekveeAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-254 |
1.57e-82 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 247.69 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHqPPSEGEILLDAQPLeswssKAFARKVAYLPQ 92
Cdd:COG1121 9 LENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPP-----RRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 Q------LPpaegMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
Cdd:COG1121 83 RaevdwdFP----ITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGeMIAQGTPAEIMRGETLEMIYG 246
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYG 236
|
....*...
gi 15829409 247 IPMGILPH 254
Cdd:COG1121 237 GPVALLAH 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-261 |
2.67e-74 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 227.56 E-value: 2.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVR 103
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
Cdd:PRK10253 100 ELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILPHPAGAAPV 261
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAGTPL 257
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-230 |
1.54e-67 |
|
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: 208.16 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHqPPSEGEILLDAQPLESWSskafaRKVAYLPQQL 94
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLEKER-----KRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 95 ------PpaegMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:cd03235 78 sidrdfP----ISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYlVALRGGEMIAQG 230
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-242 |
5.25e-64 |
|
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: 199.87 E-value: 5.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQ----QLppaEGMTVRELVAIGrypwhgaLGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
Cdd:COG1122 81 FQnpddQL---FAPTVEEDVAFG-------PENLGLPReeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM-RGETLE 242
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFsDYELLE 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-260 |
1.72e-60 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 196.22 E-value: 1.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMG 250
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
250
....*....|
gi 15829409 251 ILPHPAGAAP 260
Cdd:PRK09536 242 VGTDPATGAP 251
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-245 |
1.15e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLPQQ 93
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIgrypwHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:COG1131 82 PALYPDLTVRENLRF-----FARLyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRgETLEMIY 245
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA-RLLEDVF 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-225 |
2.28e-58 |
|
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: 184.59 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQlppAEGM----TVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:cd03225 82 QN---PDDQffgpTVEEEVAFGL----ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-245 |
2.02e-57 |
|
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: 183.54 E-value: 2.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKV 87
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 88 AYLPQQLPPAEGMTVRELVAIGRYP----WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGrrstWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRgETLEM 243
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD-EVLDE 239
|
..
gi 15829409 244 IY 245
Cdd:cd03256 240 IY 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-226 |
2.06e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 182.32 E-value: 2.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQlPPAEGMTVRELVaigRYPWHGALGRFgaaDREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:COG4619 81 QE-PALWGGTVRDNL---PFPFQLRERKF---DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-248 |
7.86e-57 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 181.96 E-value: 7.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISfrVPGRtlLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHqpPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:COG4138 2 QLNDVA--VAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVrelvaigrypWHG-ALGRFGAADREKVEEAISLV----GLKPLAHRLVDSLSGGERQRAWIAMLVAQ-- 164
Cdd:COG4138 76 QQQSPPFAMPV----------FQYlALHQPAGASSEAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 165 -----DSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGE 239
Cdd:COG4138 146 ptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
....*....
gi 15829409 240 TLEMIYGIP 248
Cdd:COG4138 225 NLSEVFGVK 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-261 |
1.44e-56 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 182.33 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--------EGEILLDAQPLESWSSKAFARKVAYLPQQL 94
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 95 PPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ---------D 165
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIY 245
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
250
....*....|....*.
gi 15829409 246 GIPMGILPHPAGAAPV 261
Cdd:PRK13547 253 GFAVRLVDAGDGVPPV 268
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-237 |
6.03e-56 |
|
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: 187.03 E-value: 6.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGR-----TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFAR 85
Cdd:COG1123 263 VRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQ----QLPPAegMTVRELVAigrYPWHgALGRFGAADR-EKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIA 159
Cdd:COG1123 343 RVQMVFQdpysSLNPR--MTVGDIIA---EPLR-LHGLLSRAERrERVAELLERVGLPPdLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-242 |
4.91e-53 |
|
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: 172.35 E-value: 4.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQ 93
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVaigRYpwHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:COG4555 83 RGLYDRLTVRENI---RY--FAELyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLE 242
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-238 |
7.32e-53 |
|
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: 171.91 E-value: 7.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
Cdd:COG1124 4 VRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQ----LPPaeGMTVRELVAigrYPWHgALGRFGAADRekVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQ 164
Cdd:COG1124 84 VFQDpyasLHP--RHTVDRILA---EPLR-IHGLPDREER--IAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRG 238
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-237 |
3.41e-52 |
|
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: 169.93 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPPAEGMTVRELVAI 108
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 109 GRYPWHGALGRFG------AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
Cdd:cd03219 99 AAQARTGSGLLLArarreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 183 QVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:cd03219 179 TEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-213 |
2.35e-51 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 166.26 E-value: 2.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 20 RVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsSKAFARKVAYLPQQ--LPPA 97
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRseVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 98 EGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
Cdd:NF040873 70 LPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 15829409 178 LDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAAR 213
Cdd:NF040873 150 LDAESRERIIALLAEEH-ARGATVVVVTHDLELVRR 184
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-237 |
9.26e-51 |
|
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: 166.75 E-value: 9.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK- 86
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQLPPAEGMTVRELVAIG-----RYPWHGALGRFG------AADREKVEEAISLVGLKPLAHRLVDSLSGGERQR 155
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAaharlGRGLLAALLRLPrarreeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
..
gi 15829409 236 MR 237
Cdd:COG0411 241 RA 242
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-237 |
8.46e-48 |
|
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: 166.47 E-value: 8.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 2 QEYTNHSDTTFALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 81 KAFARKVAYLPQQ--LPPAegmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------S 147
Cdd:COG4988 407 ASWRRQIAWVPQNpyLFAG---TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAALPDgldtplgeggrG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMI 227
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIV 550
|
250
....*....|
gi 15829409 228 AQGTPAEIMR 237
Cdd:COG4988 551 EQGTHEELLA 560
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-225 |
1.30e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 157.65 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 3 EYTNHSDTTFALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
Cdd:cd03255 9 TYGGGGEKVQALKGVSLSIE-------------KGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FA----RKVAYLPQQ---LPpaeGMTVRELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQR 155
Cdd:cd03255 76 LAafrrRHIGFVFQSfnlLP---DLTALENVEL---PLLLA-GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGE 225
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-203 |
2.48e-47 |
|
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: 156.49 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkAFARKVAYLPQQ 93
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIgrypWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:COG4133 84 DGLKPELTVRENLRF----WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|
gi 15829409 174 PTSALDIAHQVDVLALVHRLSQERGLTVIA 203
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-237 |
4.70e-47 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 156.68 E-value: 4.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARKVAYL 90
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQlppaeG-----MTVRELVAIG-RYpwHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
Cdd:COG1127 88 FQG-----GalfdsLTVFENVAFPlRE--HTDLSE--AEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 165 DSRCLLLDEPTSALDI--AHQVDvlALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1127 159 DPEILLYDEPTAGLDPitSAVID--ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-237 |
5.95e-47 |
|
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: 163.54 E-value: 5.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLESWSSKAFARKVA 88
Cdd:COG1123 7 VRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQ----QLPPAegmTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
Cdd:COG1123 87 MVFQdpmtQLNPV---TVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-237 |
7.26e-47 |
|
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: 156.12 E-value: 7.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARKVAYL 90
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAigrYPW--HGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:cd03261 83 FQSGALFDSLTVFENVA---FPLreHTRLSE--EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALD-IAHQVdVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:cd03261 158 LLYDEPTAGLDpIASGV-IDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-230 |
1.45e-46 |
|
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: 154.97 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYL 90
Cdd:cd03257 8 SVSFPTGGGsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQ----LPPAegMTVRELVAIGRYPWHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQD 165
Cdd:cd03257 88 FQDpmssLNPR--MTIGEQIAEPLRIHGKLSKK--EARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
14-248 |
2.17e-46 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 155.48 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISfrVPGRtlLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGrhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:PRK03695 3 LNDVA--VSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLaRMAG--LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIgrypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ-------D 165
Cdd:PRK03695 77 QQTPPFAMPVFQYLTL-----HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIY 245
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
...
gi 15829409 246 GIP 248
Cdd:PRK03695 231 GVN 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-176 |
4.29e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 148.95 E-value: 4.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVRELV 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 107 AIGRYPWhgalGRFGAADREKVEEAISLVGLKPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
Cdd:pfam00005 81 RLGLLLK----GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-229 |
4.52e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.35 E-value: 4.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----R 85
Cdd:COG1136 7 LRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlrrR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQ---LPpaeGMTVRELVAIGRYPwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
Cdd:COG1136 87 HIGFVFQFfnlLP---ELTALENVALPLLL----AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQ 229
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-225 |
9.45e-45 |
|
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: 148.16 E-value: 9.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQq 93
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 lppaegmtvrelvaigrypwhgalgrfgaadrekveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15829409 174 PTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-237 |
3.13e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.61 E-value: 3.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkAFARKVAYLPQQ 93
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP-PRERRVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 --LPPAegMTVRELVAIG-RypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:COG1118 84 yaLFPH--MTVAENIAFGlR-----VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-244 |
5.41e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 148.75 E-value: 5.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLlhPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkaFARKVAYLPQQ 93
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 --LPPAegMTVRELVAIGRYPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:COG3840 80 nnLFPH--LTVAQNIGLGLRP---GL-KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMI 244
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-242 |
6.41e-44 |
|
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: 149.91 E-value: 6.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFR-VPG----RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ---PLESWSSKAFAR 85
Cdd:TIGR04521 3 LKNVSYIyQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQ----QLpPAEgmTVRELVAIGrypwhgaLGRFGAAD---REKVEEAISLVGLKP-LAHRLVDSLSGGERQRAW 157
Cdd:TIGR04521 83 KVGLVFQfpehQL-FEE--TVYKDIAFG-------PKNLGLSEeeaEERVKEALELVGLDEeYLERSPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI-M 236
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVfS 232
|
....*.
gi 15829409 237 RGETLE 242
Cdd:TIGR04521 233 DVDELE 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-248 |
6.48e-44 |
|
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: 149.08 E-value: 6.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGE--ILLDaQPLESWSSKAFARK 86
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFG-ERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAY----LPQQLPPaeGMTVRELVAIGRYpwhGALGRF---GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
Cdd:COG1119 80 IGLvspaLQLRFPR--DETVLDVVLSGFF---DSIGLYrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 160 -MLVAqDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRG 238
Cdd:COG1119 155 rALVK-DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
250
....*....|
gi 15829409 239 ETLEMIYGIP 248
Cdd:COG1119 234 ENLSEAFGLP 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-244 |
5.57e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 147.47 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:PRK13635 8 VEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQlPPAE--GMTVRELVAigrypwhgalgrFGAADR--------EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
Cdd:PRK13635 88 QN-PDNQfvGATVQDDVA------------FGLENIgvpreemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMR-GET 240
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKsGHM 233
|
....
gi 15829409 241 LEMI 244
Cdd:PRK13635 234 LQEI 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-237 |
6.08e-43 |
|
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: 146.29 E-value: 6.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIgrYPwhGALGRFGAADREKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:cd03295 83 QIGLFPHMTVEENIAL--VP--KLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-236 |
9.91e-43 |
|
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: 154.22 E-value: 9.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:COG2274 476 LENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAM 160
Cdd:COG2274 556 QDVFLFSG-TIRENITLGD----------PDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-244 |
1.58e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.04 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYL 90
Cdd:TIGR04520 3 VENVSFSYPESEKpaLKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRkKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQ----QLPpaeGMTVRELVAigrypwhgalgrFG----AADREK----VEEAISLVGLKPLAHRLVDSLSGGERQRAWI 158
Cdd:TIGR04520 83 FQnpdnQFV---GATVEDDVA------------FGlenlGVPREEmrkrVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIM-R 237
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFsQ 226
|
....*..
gi 15829409 238 GETLEMI 244
Cdd:TIGR04520 227 VELLKEI 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-235 |
1.79e-42 |
|
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: 144.63 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR---HQP--PSEGEILLDAQPLESWSSKAFA-- 84
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPgaPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 85 RKVAYLPQQLPPAEgMTVRELVAIGryPW-HGALGRFGAADRekVEEAISLVGLKPLAHRLVD--SLSGGERQRAWIAML 161
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG--LRlHGIKLKEELDER--VEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-235 |
7.34e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.40 E-value: 7.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSskAFARKVAYLPQQ 93
Cdd:COG3842 8 LENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP--PEKRNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 L---PPaegMTVRELVAIG-RypwhgaLGRFGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:COG3842 86 YalfPH---LTVAENVAFGlR------MRGVPKAEIrARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-237 |
1.08e-41 |
|
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: 149.92 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
Cdd:COG4987 330 GGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQlPPAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQ 154
Cdd:COG4987 410 RIAVVPQR-PHLFDTTLRENLRLAR----------PDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAE 234
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
...
gi 15829409 235 IMR 237
Cdd:COG4987 556 LLA 558
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-230 |
1.43e-41 |
|
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: 141.56 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQ 93
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAigrypWHGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03264 81 FGVYPNFTVREFLD-----YIAWLKGIPSKEvKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-225 |
2.50e-41 |
|
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: 139.83 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:cd03228 3 FKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQlPPAEGMTVRELVaigrypwhgalgrfgaadrekveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:cd03228 83 QD-PFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMaARYCDYLVALRGGE 225
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGK--TVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-230 |
4.56e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 140.35 E-value: 4.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSskAFARKVAYLPQQ 93
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIGrypwhGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03259 81 YALFPHLTVAENIAFG-----LKLRGVPKAEiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-225 |
1.01e-40 |
|
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: 138.47 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL--ESWSSKAFARKVAYLP 91
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQ--LPPaeGMTVRELVAIGrypwhgalgrfgaadrekveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCL 169
Cdd:cd03229 83 QDfaLFP--HLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-226 |
1.84e-40 |
|
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: 137.53 E-value: 1.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQ 93
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVaigrypwhgalgrfgaadrekveeaislvglkplahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:cd03230 82 PSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829409 174 PTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-223 |
2.40e-39 |
|
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: 136.06 E-value: 2.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGR----TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSskafaRKVAY 89
Cdd:cd03293 3 VRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQ---LPpaeGMTVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
Cdd:cd03293 78 VFQQdalLP---WLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG 223
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-235 |
4.21e-39 |
|
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: 136.17 E-value: 4.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 3 EYTNHSDTTFALRNISfrvpgrtllhplsLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
Cdd:cd03258 10 VFGDTGGKVTALKDVS-------------LSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 ---FARKVAYLPQQLPPAEGMTVRELVAigrYPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
Cdd:cd03258 77 lrkARRRIGMIFQHFNLLSSRTVFENVA---LPLEIA-GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-245 |
5.96e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.69 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQ 92
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGRYPwhgalGRFGAAD----REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:COG1129 87 ELNLVPNLSVAENIFLGREP-----RRGGLIDwramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALDiAHQVDVL-ALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI--------MRGE 239
Cdd:COG1129 162 LILDEPTASLT-EREVERLfRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELtedelvrlMVGR 239
|
....*.
gi 15829409 240 TLEMIY 245
Cdd:COG1129 240 ELEDLF 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-237 |
1.44e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 141.84 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:COG1132 342 FENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 qlppaEG----MTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAW 157
Cdd:COG1132 422 -----DTflfsGTIRENIRYGR----------PDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELLA 563
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-224 |
1.51e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.22 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 6 NHSDTTFALRNIS--FRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswssk 81
Cdd:COG1116 2 SAAAPALELRGVSkrFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 82 AFARKVAYLPQQ--LPPAegMTVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
Cdd:COG1116 77 GPGPDRGVVFQEpaLLPW--LTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-221 |
2.02e-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: 137.80 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPGRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQ--LPPAegmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLA-------HRLVDS----LSGGER 153
Cdd:TIGR02857 398 IAWVPQHpfLFAG---TIAENIRLAR----------PDASDAEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVAL 221
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
30-235 |
3.06e-37 |
|
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: 130.70 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPPAEGMTVRELVAIg 109
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGYCPQFDALFDELTVREHLRF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 110 rypwHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
Cdd:cd03263 99 ----YARLkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15829409 189 LVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03263 175 LILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-236 |
8.49e-37 |
|
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: 129.86 E-value: 8.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQ--QLPPaeGMTVR 103
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEgrRIFP--ELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELVAIGRYPwhgalgRFGAADREKVEEAISLV-GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL--DI 180
Cdd:cd03224 94 ENLLLGAYA------RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLapKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 181 AHQvdVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:cd03224 168 VEE--IFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-237 |
1.70e-36 |
|
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: 132.53 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQ--LPPAegMTVRE 104
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlpphRRRIGYVFQEarLFPH--LSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 105 LVAIGRypWHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
Cdd:COG4148 97 NLLYGR--KRAP----RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829409 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-225 |
1.46e-35 |
|
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: 125.83 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswSSKAFARKVAYLPQ-- 92
Cdd:cd03226 4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 --QLppaEGMTVRELVAIGRypwhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:cd03226 81 dyQL---FTDSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-235 |
1.96e-35 |
|
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: 126.58 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkvaylpQQ 93
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----------------TN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAE--------------GMTVRELVAIGRypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWI 158
Cdd:cd03300 67 LPPHKrpvntvfqnyalfpHLTVFENIAFGL-----RLKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-230 |
2.61e-35 |
|
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: 125.68 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVpGRTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQ 92
Cdd:cd03298 2 RLDKIRFSY-GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGRYPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLSP---GL-KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-237 |
4.02e-35 |
|
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: 127.86 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKM-LGRHQPP--SEGEILLDAQPLESWSSKAF----ARK 86
Cdd:COG0444 8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAiLGLLPPPgiTSGEILFDGEDLLKLSEKELrkirGRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQ----LPPAegMTVRELVAIG-RYpwHGALGRfgAADREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAW 157
Cdd:COG0444 88 IQMIFQDpmtsLNPV--MTVGDQIAEPlRI--HGGLSK--AEARERAIELLERVGL-PDPERRLDRypheLSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-237 |
1.80e-34 |
|
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: 130.25 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:COG4618 333 VENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 Q--QLPPAegmTVRELVAigrypwhgalgRFGAADREKVEEAISLVGlkplAHRLVDS---------------LSGGERQ 154
Cdd:COG4618 413 QdvELFDG---TIAENIA-----------RFGDADPEKVVAAAKLAG----VHEMILRlpdgydtrigeggarLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 155 RAWIAMLVAQDSRCLLLDEPTSALDiahQVDVLALVHRLSQ--ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTP 232
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLD---DEGEAALAAAIRAlkARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPR 550
|
....*
gi 15829409 233 AEIMR 237
Cdd:COG4618 551 DEVLA 555
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-234 |
2.03e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQ 92
Cdd:COG2884 4 FENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL----SRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLppaeGM-----------TVRELVAIgrypwhgAL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWI 158
Cdd:COG2884 80 RI----GVvfqdfrllpdrTVYENVAL-------PLrvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-256 |
2.65e-34 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 124.61 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNisfrvpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswssKAFARK- 86
Cdd:PRK15056 10 NDVTVTWRN------GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQ--QLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
Cdd:PRK15056 80 VAYVPQseEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRgGEMIAQGTPAEIMRGETLEMI 244
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELA 237
|
250
....*....|..
gi 15829409 245 YGipmGILPHPA 256
Cdd:PRK15056 238 FS---GVLRHVA 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
1.13e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.94 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAQPLESWSSKAFARK 86
Cdd:PRK13648 19 SDASFTLKDVSFNIP-------------KGQWTSIVGHNGSGKSTIAKlMIGIEK-VKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQlPPAE--GMTVRELVAIGrypwhgaLGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
Cdd:PRK13648 85 IGIVFQN-PDNQfvGSIVKYDVAFG-------LENHAVPYdemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMR-GET 240
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDhAEE 235
|
....
gi 15829409 241 LEMI 244
Cdd:PRK13648 236 LTRI 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-246 |
1.44e-33 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 121.68 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQL 94
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 95 PPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
Cdd:cd03296 84 ALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYG 246
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-245 |
1.83e-33 |
|
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: 121.50 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQ 92
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRE-LVAIGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:cd03218 83 EASIFRKLTVEEnILAVLEI-----RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 172 DEPTSALD-IAHQvDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIY 245
Cdd:cd03218 158 DEPFAGVDpIAVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-237 |
5.31e-33 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 123.30 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQLPPAEGMTVREL 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 106 VAIGRYpwhgalgRFGAADREKVEEAI-SLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
Cdd:TIGR02142 96 LRYGMK-------RARPSERRISFERViELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829409 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-237 |
5.64e-33 |
|
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: 121.21 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKV 87
Cdd:cd03294 34 TGQTVGVNDVSLDVR-------------EGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKEL-REL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 88 ------------AYLPQqlppaegMTVRELVAIGrypwhgaL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGE 152
Cdd:cd03294 100 rrkkismvfqsfALLPH-------RTVLENVAFG-------LevqGVPRAEREERAAEALELVGLEGWEHKYPDELSGGM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
....*
gi 15829409 233 AEIMR 237
Cdd:cd03294 246 EEILT 250
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-236 |
7.22e-33 |
|
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: 119.95 E-value: 7.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQlPPAEGMTVRELVAIGRYPwhgalgrfgaADREKVEEAISLVGlkplAHRLVDS---------------LSGGERQR 155
Cdd:cd03249 83 SQE-PVLFDGTIAENIRYGKPD----------ATDEEVEEAAKKAN----IHDFIMSlpdgydtlvgergsqLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDEL 224
|
.
gi 15829409 236 M 236
Cdd:cd03249 225 M 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-263 |
1.43e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.60 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQ 92
Cdd:COG4152 16 AVDDVSFTVP-------------KGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 Q--LPPAegMTVRE-LVAIGRYpwHGaLGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
Cdd:COG4152 79 ErgLYPK--MKVGEqLVYLARL--KG-LSK--AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 170 LLDEPTSALD-IAhqVDVLA-LVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI---MRGETLEMI 244
Cdd:COG4152 152 ILDEPFSGLDpVN--VELLKdVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIrrqFGRNTLRLE 228
|
250
....*....|....*....
gi 15829409 245 YGIPMGILPHPAGAAPVSF 263
Cdd:COG4152 229 ADGDAGWLRALPGVTVVEE 247
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-235 |
1.97e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 121.72 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHqPPSEGEILLDAQPLESWSSKafARKVAYLPQ 92
Cdd:COG3839 6 LENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIaGLE-DPTSGEILIGGRDVTDLPPK--DRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 Q--LPPAegMTVRELVAIG-RypwhgaLGRFGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRawIAM---LVAqD 165
Cdd:COG3839 83 SyaLYPH--MTVYENIAFPlK------LRKVPKAEIdRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALgraLVR-E 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHD----INMAarycDYLVALRGGEMIAQGTPAEI 235
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEEL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-235 |
2.23e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.95 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNIS--FRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARK 86
Cdd:COG1135 4 LENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelrAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VaylpqqlppaeGM-----------TVRELVAigrYPwhgaL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGE 152
Cdd:COG1135 84 I-----------GMifqhfnllssrTVAENVA---LP----LeiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
...
gi 15829409 233 AEI 235
Cdd:COG1135 226 LDV 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
27-241 |
3.65e-32 |
|
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: 118.16 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQ--QLPPaeGMTVR 103
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEgrRIFP--SLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 E-LVaigrypwhgaLGRFGAADREKVEEAISLVG-----LKPLAHRLVDSLSGGERQ-----RAwiamLVAqDSRCLLLD 172
Cdd:COG0410 97 EnLL----------LGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQmlaigRA----LMS-RPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 173 EPTsaLDIAHQV--DVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETL 241
Cdd:COG0410 162 EPS--LGLAPLIveEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEV 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
27-231 |
5.43e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.58 E-value: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-----GRHQPPSEGEILLDAQPLESWSSKAFARKVA---YLPQQLPPAE 98
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitGDKSAGSHIELLGRTVQREGRLARDIRKSRAntgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 GMTVRELV---AIGRYP-WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
Cdd:PRK09984 100 RLSVLENVligALGSTPfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-229 |
6.89e-32 |
|
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: 115.22 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYL 90
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQqlppaegmtvrelvaigrypwhgalgrfgaadrekveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-235 |
8.64e-32 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 116.70 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVA 88
Cdd:cd03265 11 GDFEAVRGVSFRVR-------------RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQQLPPAEGMTVRELVAigrypWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:cd03265 77 IVFQDLSVDDELTGWENLY-----IHARLyGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-207 |
1.17e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.10 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafaRKVAYLPQQ 93
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIGRYPWHGAL------------------------GRFGAAD----REKVEEAISLVGLKPLAH-RL 144
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEaeleeleaklaepdedlerlaelqEEFEALGgweaEARAEEILSGLGFPEEDLdRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHD 207
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWLEEFLKNYPG-TVLVVSHD 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
27-235 |
1.33e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.63 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAFA---RKVAYLPQQ--LPPAegMT 101
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINklrRKVGMVFQQfnLFPH--LT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 102 VRELVAIGryPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-- 179
Cdd:COG1126 94 VLENVTLA--PIK-VKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpe 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 180 -IAhqvDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:COG1126 171 lVG---EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-235 |
1.59e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNIS--FRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARK 86
Cdd:PRK11153 4 LKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQLPPAEGMTVRELVAIgrypwhgAL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVAL-------PLelaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-230 |
1.72e-31 |
|
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: 115.86 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 17 ISFRVPGRTLlhPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQ 92
Cdd:cd03297 6 IEKRLPDFTL--KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAigrypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03297 83 QYALFPHLNVRENLA------FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
9-247 |
1.76e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 117.64 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEsWSSKAFA--R 85
Cdd:PRK13636 3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMklR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQLPPAE--GMTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
Cdd:PRK13636 82 ESVGMVFQDPDNQlfSASVYQDVSFGAV----NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGEtlEM 243
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK--EM 235
|
....
gi 15829409 244 IYGI 247
Cdd:PRK13636 236 LRKV 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
2.81e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.63 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 5 TNHSDTTFALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKA 82
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-SKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FARKVAYLPQQLPPAE--GMTVRELVAIG----RYPwhgalgrfgaadREK----VEEAISLVGLKPLAHRLVDSLSGGE 152
Cdd:PRK13632 80 EIRKKIGIIFQNPDNQfiGATVEDDIAFGlenkKVP------------PKKmkdiIDDLAKKVGMEDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTP 232
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKP 226
|
....*..
gi 15829409 233 AEIMRGE 239
Cdd:PRK13632 227 KEILNNK 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-236 |
3.26e-31 |
|
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: 115.41 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:cd03253 2 EFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGmTVRELVaigRYpwhgalGRFGAADrEKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAM 160
Cdd:cd03253 82 QDTVLFND-TIGYNI---RY------GRPDATD-EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIM 236
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-251 |
3.32e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.04 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS----KAFARKVAYLPQ----QLP 95
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQfpehQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 96 PAegmTVRELVAIGryPWHgalgrFGAADRE---KVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK13634 100 EE---TVEKDICFG--PMN-----FGVSEEDakqKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR-GETLEMI-YGIPM 249
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdPDELEAIgLDLPE 249
|
..
gi 15829409 250 GI 251
Cdd:PRK13634 250 TV 251
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-237 |
4.78e-31 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 116.73 E-value: 4.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:COG1125 4 FENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 Q---LPpaeGMTVRELVAIgrYPwhGALGRFGAADREKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:COG1125 84 QiglFP---HMTVAENIAT--VP--RLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 168 CLLLDEPTSALD-IAH---QVDVLalvhRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1125 157 ILLMDEPFGALDpITReqlQDELL----RLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-230 |
5.16e-31 |
|
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: 114.68 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS--EGEILLDAQPLeswSSKAFARKVAYLPQQLPPAEGM 100
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVaigRYPWHGALGR-FGAADREKVEE--AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
Cdd:cd03234 97 TVRETL---TYTAILRLPRkSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 178 LD--IAHQvdvlaLVHRLSQ--ERGLTVIAVLH----DInmaARYCDYLVALRGGEMIAQG 230
Cdd:cd03234 174 LDsfTALN-----LVSTLSQlaRRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-246 |
8.15e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQ 92
Cdd:COG3845 8 LRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdAIALGIGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGRYPWHGALGRFGAAdREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:COG3845 88 HFMLVPNLTVAENIVLGLEPTKGGRLDRKAA-RARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYG 246
Cdd:COG3845 167 EPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVG 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
8.56e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.13 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 1 MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR---HQPPS--EGEILLDAQPL 75
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGArvEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 76 ESWSSKAFA--RKVAYLPQQ---LPpaegMTVRELVAIG-RYpwHGALGRfGAADrEKVEEAISLVGL-KPLAHRLVDS- 147
Cdd:COG1117 81 YDPDVDVVElrRRVGMVFQKpnpFP----KSIYDNVAYGlRL--HGIKSK-SELD-EIVEESLRKAALwDEVKDRLKKSa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 148 --LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAHQVdVLALVHRLSQErgLTVIAVLHdiNM--AARYCDYLVALR 222
Cdd:COG1117 153 lgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKD--YTIVIVTH--NMqqAARVSDYTAFFY 227
|
250
....*....|...
gi 15829409 223 GGEMIAQGTPAEI 235
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-242 |
8.71e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 115.49 E-value: 8.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEsWSSK---AFARKVA 88
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQQlpPAEGMTVRELVAIGRYpwhgALGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
Cdd:PRK13638 81 TVFQD--PEQQIFYTDIDSDIAF----SLRNLGVPEAEitrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM-RGETLE 242
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAME 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-230 |
1.01e-30 |
|
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: 113.84 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQLPPAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGA----------PLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVdvlALVHRLSQE-RGLTVIAVLHDINMAArYCDYLVALRGGEMIAQG 230
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQLlGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-236 |
1.15e-30 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 119.82 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:TIGR02203 334 RNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGmTVRELVAigrypwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAML 161
Cdd:TIGR02203 414 DVVLFND-TIANNIA---------YGRTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAEIM 236
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAhRLSTIEKA----DRIVVMDDGRIVERGTHNELL 555
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-236 |
5.40e-30 |
|
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: 112.32 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLV 162
Cdd:cd03254 86 TFLFSG-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA--HRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-230 |
8.65e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 111.11 E-value: 8.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQLPPAEGMTVRELVAIGR 110
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 111 YPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
Cdd:TIGR01277 96 HP---GL-KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829409 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-230 |
1.00e-29 |
|
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: 110.83 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQQ 93
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRE-LVAIGRYpwHGaLGRFGAadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03269 79 RGLYPKMKVIDqLVYLAQL--KG-LKKEEA--RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHqVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03269 154 EPFSGLDPVN-VELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-232 |
1.05e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.52 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAyLPQ 92
Cdd:PRK13647 7 VEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG-LVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAE--GMTVRELVAIGryPWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK13647 86 QDPDDQvfSSTVWDDVAFG--PVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-229 |
1.12e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 112.21 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP---LESWSSKAFARKVAYLPQQLPPAEG-- 99
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlyqLDRKQRRAFRRDVQLVFQDSPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 100 MTVRELVaigRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
Cdd:TIGR02769 105 MTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829409 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-226 |
2.02e-29 |
|
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: 110.19 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQ 92
Cdd:cd03292 3 FINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV----SDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLppaeGM-----------TVRELVAIgrypwhgALGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWI 158
Cdd:cd03292 79 KI----GVvfqdfrllpdrNVYENVAF-------ALEVTGVPPREirkRVPAALELVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-241 |
2.57e-29 |
|
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: 110.65 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
Cdd:cd03252 2 TFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGlkplAHRLV---------------DSLSGGERQR 155
Cdd:cd03252 82 LQENVLFNR-SIRDNIALAD----------PGMSMERVIEAAKLAG----AHDFIselpegydtivgeqgAGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
|
....*.
gi 15829409 236 MRGETL 241
Cdd:cd03252 224 LAENGL 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-236 |
7.46e-29 |
|
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: 109.24 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:cd03251 3 FKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGmTVRELVAIGRypwHGalgrfgaADREKVEEAISLVGlkplAHRLVDS---------------LSGGERQRA 156
Cdd:cd03251 83 QDVFLFND-TVAENIAYGR---PG-------ATREEVEEAARAAN----AHEFIMElpegydtvigergvkLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-226 |
7.57e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 6 NHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQlPPAEGMTVRELVAigrYPWhgaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQ 164
Cdd:PRK10247 82 QVSYCAQT-PTLFGDTVYDNLI---FPW---QIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINmAARYCDYLVAL--RGGEM 226
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITLqpHAGEM 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-226 |
9.20e-29 |
|
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: 107.30 E-value: 9.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQLPPAEGmTVRELVaigrypwhgalgrfgaadrekveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCL 169
Cdd:cd03246 81 LPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 170 LLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-234 |
1.03e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 109.06 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 5 TNHSDTTFALRNISFRVPGR----TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 81 KAFAR----KVAYLPQ--QLPPAegMTVRELVAIgryPwhgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGER 153
Cdd:COG4181 82 DARARlrarHVGFVFQsfQLLPT--LTALENVML---P----LELAGRRDaRARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPA 233
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
.
gi 15829409 234 E 234
Cdd:COG4181 232 A 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-235 |
1.06e-28 |
|
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: 108.96 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLP 91
Cdd:cd03299 13 FKLKNVSLEVE-------------RGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGlkkrKVD--------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
36-247 |
1.09e-28 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 108.78 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsSKAFARKVAYLPQQLPPAEG--MTVRELVAIGRYPW 113
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAWDfpISVAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 114 HGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
Cdd:TIGR03771 80 IGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829409 194 SQErGLTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAEIMRGETLEMIYGI 247
Cdd:TIGR03771 160 AGA-GTAILMTTHDLAQAMATCDRVV-LLNGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-235 |
1.24e-28 |
|
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: 113.63 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKS----TLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---- 85
Cdd:COG4172 13 SVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQqlppaEGMT-----------VRELVAIgrypwHGALGRfgAADREKVEEAISLVGLKPLAHRLvDS----LSG 150
Cdd:COG4172 93 RIAMIFQ-----EPMTslnplhtigkqIAEVLRL-----HRGLSG--AAARARALELLERVGIPDPERRL-DAyphqLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
....*
gi 15829409 231 TPAEI 235
Cdd:COG4172 240 PTAEL 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-235 |
2.99e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTL-LKMLGRHQPpSEGEILLDAQPLeSWSSKAF--ARKVAYL 90
Cdd:PRK13639 5 RDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILKP-TSGEVLIKGEPI-KYDKKSLleVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAE--GMTVRELVAIGryPWHgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK13639 83 VFQNPDDQlfAPTVEEDVAFG--PLN--LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-253 |
4.42e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.35 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfARKVAYLPQ 92
Cdd:PRK13652 19 ALNNINFIAPRNSRI-------------AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAE--GMTVRELVAIGryPWHgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK13652 85 QNPDDQifSPTVEQDIAFG--PIN--LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMG 250
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLP 240
|
...
gi 15829409 251 ILP 253
Cdd:PRK13652 241 SLP 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-241 |
5.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPP---SEGEILLDAQPLESWSSKA 82
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FARKVAYLPQQlPPAE--GMTVRELVAIG---RypwhgalgrfgAADREK----VEEAISLVGLKPLAHRLVDSLSGGER 153
Cdd:PRK13640 82 IREKVGIVFQN-PDNQfvGATVGDDVAFGlenR-----------AVPRPEmikiVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPA 233
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPV 228
|
....*...
gi 15829409 234 EIMRGETL 241
Cdd:PRK13640 229 EIFSKVEM 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-237 |
6.52e-28 |
|
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: 111.70 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPpSEGEILLDAQPLESWSSKAFA---RKVa 88
Cdd:COG4172 301 AVDGVSLTLrRGETL--------------GLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRplrRRM- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 ylpqQ---------LPPAegMTVRELVAIGRYPWHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWI 158
Cdd:COG4172 365 ----QvvfqdpfgsLSPR--MTVGQIIAEGLRVHGPGLSA--AERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-245 |
9.63e-28 |
|
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: 106.59 E-value: 9.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAY 89
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQLPPAEGMTVRE-LVAIGRYpwHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:TIGR04406 81 LPQEASIFRKLTVEEnIMAVLEI--RKDLDR--AEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCD--YLVAlrGGEMIAQGTPAEIMRGETLEMIY 245
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDraYIIS--DGKVLAEGTPAEIVANEKVRRVY 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-230 |
1.63e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.57 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 25 TLLHPLSLTFPAGKVTGLIGHNGSGKST----LLKMLgrhqpPSEGEILLDAQPLESWSSKA---FARKVAYLPQQ---- 93
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDpnss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAegMTVRELVAIGRYPWHGALGrfgAADRE-KVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK15134 375 LNPR--LNVLQIIEEGLRVHQPTLS---AAQREqQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-236 |
1.85e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 110.52 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88
Cdd:TIGR01842 316 HLSVENVTIVPPGgkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQQLPPAEGmTVRELVAigrypwhgalgRFG-AADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRA 156
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIA-----------RFGeNADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIM 236
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGC-VDKILVLQDGRIARFGERDEVL 541
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-248 |
1.85e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQQLPPAEGM--TVR 103
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQYPEYQLFeeTIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELVAIGrypwhgaLGRFGAADRE---KVEEAISLVGLK--PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
Cdd:PRK13637 103 KDIAFG-------PINLGLSEEEienRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRG-ETLEMI-YGIP 248
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESIgLAVP 247
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-227 |
2.25e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.32 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGK-VTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ--QLPPAEGM 100
Cdd:COG1101 19 KRALDGLNLTIEEGDfVT-VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQdpMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVAI-----GRYPWHGALGRfgaADREKVEEAISLVGLKpLAHRL---VDSLSGGERQrAwIAMLVA--QDSRCLL 170
Cdd:COG1101 98 TIEENLALayrrgKRRGLRRGLTK---KRRELFRELLATLGLG-LENRLdtkVGLLSGGQRQ-A-LSLLMAtlTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-225 |
2.65e-27 |
|
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: 104.53 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFA---RKVAYL 90
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINelrQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAIGryP-WhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
Cdd:cd03262 82 FQQFNLFPHLTVLENITLA--PiK--VKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-227 |
2.82e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSKAfarKVAYLPQ- 92
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV---KIGYFDQh 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 --QLPPaeGMTVRELV---AIGRYPWH--GALGRFG-AADRekveeaislvglkplAHRLVDSLSGGERQRAWIAMLVAQ 164
Cdd:COG0488 387 qeELDP--DKTVLDELrdgAPGGTEQEvrGYLGRFLfSGDD---------------AFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 165 DSRCLLLDEPTSALDIahqvDVL-ALVHRLSQERGlTVIAVLHDinmaaRY-----CDYLVALRGGEMI 227
Cdd:COG0488 450 PPNVLLLDEPTNHLDI----ETLeALEEALDDFPG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-223 |
4.64e-27 |
|
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: 104.80 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 33 TFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarKVAYLPQQLPPAEGMTVRELVaigryp 112
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD------------TVSYKPQYIKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 113 wHGALGRFGAADREKVEEAISLvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|.
gi 15829409 193 LSQERGLTVIAVLHDINMAARYCDYLVALRG 223
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-227 |
1.02e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 104.38 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQLPPAE 98
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRaqrKAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 G--MTVRELVaigRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
Cdd:PRK10419 103 NprKTVREII---REPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15829409 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
31-210 |
1.07e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.58 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQ----QLPPaeGMTVR 103
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQdpyaSLNP--RMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELVAigrYPW--HGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:COG4608 116 DIIA---EPLriHGLASK--AERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
170 180 190
....*....|....*....|....*....|
gi 15829409 181 AHQVDVLALVHRLSQERGLTVIAVLHDINM 210
Cdd:COG4608 191 SIQAQVLNLLEDLQDELGLTYLFISHDLSV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-236 |
1.12e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK--AFARKVAYLP 91
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVAIGryPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK09493 84 QQFYLFPHLTALENVMFG--PLR-VRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-228 |
1.62e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.30 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLP 91
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVAIGRYPwhgalGRFGAADREK----VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGQLP-----HKGGIVNRRLlnyeAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 168 CLLLDEPTSALDiAHQVDVL-ALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
Cdd:PRK11288 161 VIAFDEPTSSLS-AREIEQLfRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-208 |
2.57e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.40 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG----RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAY 89
Cdd:COG4525 6 VRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQLPPaeGMTVRELVAIGRypwhgALGRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:COG4525 83 QKDALLP--WLNVLDNVAFGL-----RLRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI 208
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
25-213 |
5.05e-26 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 101.66 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQ--QLPPAe 98
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKLGFIYQfhHLLPD- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 gMTVRELVAIgryPWhgALGRFGAAD-REKVEEAISLVGLKplaHRLV---DSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
Cdd:TIGR02211 98 -FTALENVAM---PL--LIGKKSVKEaKERAYEMLEKVGLE---HRINhrpSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 15829409 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAAR 213
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-230 |
5.86e-26 |
|
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: 101.64 E-value: 5.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESwsSKAFARKVAYLPQQ-------LPPAEGMT 101
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKR--RKKFLRRIGVVFGQktqlwwdLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 102 VreLVAIGRYPWhgalGRFgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
Cdd:cd03267 118 L--LAAIYDLPP----ARF----KKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829409 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-230 |
1.79e-25 |
|
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: 99.16 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPG------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLeswSSKA 82
Cdd:cd03213 3 TLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FARKVAYLPQQLPPAEGMTVRElvaigrypwhgALgRFGAADRekveeaislvglkplahrlvdSLSGGERQRAWIAMLV 162
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRE-----------TL-MFAAKLR---------------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH-----DINMaaryCDYLVALRGGEMIAQG 230
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHqpsseIFEL----FDKLLLLSQGRVIYFG 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-241 |
1.97e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.80 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAyLP 91
Cdd:TIGR00958 482 QDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA-LV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVAIGRypwhgalgrfgaadREKVEEAISLVGLKPLAHRLVDS---------------LSGGERQRA 156
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGL--------------TDTPDEEIMAAAKAANAHDFIMEfpngydtevgekgsqLSGGQKQRI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIM 236
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLM 701
|
....*
gi 15829409 237 RGETL 241
Cdd:TIGR00958 702 EDQGC 706
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-213 |
2.12e-25 |
|
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: 99.64 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQ 93
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIGRypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03301 81 YALYPHMTVYDNIAFGL-----KLRKVPKDEiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHD----INMAAR 213
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqveaMTMADR 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-235 |
2.37e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQq 93
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 lppaE-----GMTVRE-LVAIGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:COG1137 86 ----EasifrKLTVEDnILAVLEL-----RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 168 CLLLDEPTSALD-IAhqV-DVLALVHRLsQERGltvIAVL---HDINMAARYCD--YLvaLRGGEMIAQGTPAEI 235
Cdd:COG1137 157 FILLDEPFAGVDpIA--VaDIQKIIRHL-KERG---IGVLitdHNVRETLGICDraYI--ISEGKVLAEGTPEEI 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-235 |
2.42e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQ 93
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIGRYpwHGALGRFGAADRekVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLK--QDKLPKAEIASR--VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 174 PTSALDIA----HQVDVLALVHRLsqerGLTVIAVLHD----INMAARycdyLVALRGGEMIAQGTPAEI 235
Cdd:PRK11607 176 PMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDqeeaMTMAGR----IAIMNRGKFVQIGEPEEI 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-255 |
2.80e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 99.85 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYLPQQLPPaeGMTVRELV 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD---RMVVFQNYSLLP--WLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 107 AIGRypwHGALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
Cdd:TIGR01184 76 ALAV---DRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLValrggeMIAQGTPAEImrGETLEMIYGIP---MGILPHP 255
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVV------MLTNGPAANI--GQILEVPFPRPrdrLEVVEDP 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
3.13e-25 |
|
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: 103.98 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:TIGR02868 337 LRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QlPPAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAML 161
Cdd:TIGR02868 417 D-AHLFDTTVRENLRLAR----------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHD 207
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-230 |
3.88e-25 |
|
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: 98.83 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQ 93
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 lpPA--EGMTVRE-LVAIGRYpwhgaLGRfgaaDREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:cd03268 81 --PGfyPNLTAREnLRLLARL-----LGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-237 |
4.32e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 6 NHSDTTFALRNISFrvpgrtllhplslTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD---AQPLEswsska 82
Cdd:COG1134 34 TRREEFWALKDVSF-------------EVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNgrvSALLE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FArkVAYLPQqlppaegMTVRELV-AIGRypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
Cdd:COG1134 95 LG--AGFHPE-------LTGRENIyLNGR-----LLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-248 |
4.52e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.27 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKafaRKVAYLPQQLPPAEGMTVRELVAIG 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpSR---RPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 110 RYPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
Cdd:PRK10771 96 LNP---GL-KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLE-MIYGIP 248
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAsALLGIK 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-242 |
5.49e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 4 YTNHSDTT-FALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
Cdd:PRK13650 12 FKYKEDQEkYTLNDVSFHVK-------------QGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FARKVAYLPQQlPPAE--GMTVRELVAIGrypwhgaLGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
Cdd:PRK13650 79 IRHKIGMVFQN-PDNQfvGATVEDDVAFG-------LENKGIPHeemKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAEI-M 236
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELfS 229
|
....*.
gi 15829409 237 RGETLE 242
Cdd:PRK13650 230 RGNDLL 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-235 |
6.03e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.95 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 1 MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-----PL 75
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 76 EswsskafARKVAYLPQQ--LPPAegMTVRELVAIG-RypwhgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGG 151
Cdd:PRK09452 84 E-------NRHVNTVFQSyaLFPH--MTVFENVAFGlR------MQKTPAAEiTPRVMEALRMVQLEEFAQRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
....
gi 15829409 232 PAEI 235
Cdd:PRK09452 229 PREI 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-226 |
8.51e-25 |
|
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: 98.31 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNisfrVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88
Cdd:cd03248 16 NVTFAYPT----RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQQlPPAEGMTVRELVAIGrypwhgalgrFGAADREKVEEAISlvglKPLAHRLV---------------DSLSGGER 153
Cdd:cd03248 92 LVGQE-PVLFARSLQDNIAYG----------LQSCSFECVKEAAQ----KAHAHSFIselasgydtevgekgSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARyCDYLVALRGGEM 226
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA--HRLSTVER-ADQILVLDGGRI 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-243 |
1.69e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 3 EYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR------HQPPSEGEILLDAQPLE 76
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiydSKIKVDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 77 SWSSKAFARKVAYLPQQLPPAEGMTVRELVAigrYPwhgaLGRFGAADREK----VEEAISLVGLKPLAHRLVDS----L 148
Cdd:PRK14246 82 QIDAIKLRKEVGMVFQQPNPFPHLSIYDNIA---YP----LKSHGIKEKREikkiVEECLRKVGLWKEVYDRLNSpasqL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
250
....*....|....*
gi 15829409 229 QGTPAEIMRGETLEM 243
Cdd:PRK14246 233 WGSSNEIFTSPKNEL 247
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-235 |
2.45e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 99.49 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 42 LIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQLPPAEGMTVRELVAIGRypwhgALGRFG 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFPHMTVEENVAFGL-----KMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 122 AADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI----AHQVDVLALVHRLsqe 196
Cdd:TIGR01187 74 RAEIkPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKklrdQMQLELKTIQEQL--- 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 15829409 197 rGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:TIGR01187 151 -GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-236 |
2.52e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:PRK11160 341 LNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGL-------KPLAHRLVD---SLSGGERQRAWIAML 161
Cdd:PRK11160 421 QRVHLFSA-TLRDNLLLAA----------PNASDEALIEVLQQVGLeklleddKGLNAWLGEggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
30-230 |
2.66e-24 |
|
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: 97.05 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-----QPLESwsskafARKVAYLPQQLPPAEGMTVRE 104
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA------RRRLGFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 105 LVAigrypWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
Cdd:cd03266 98 NLE-----YFAGLyGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15829409 184 VDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03266 173 RALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-206 |
5.20e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 7 HSDTTFALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafAR 85
Cdd:COG4178 358 SEDGALALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQ--LPPAegmTVRELVAigrYPwHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDS------LSGGERQRAW 157
Cdd:COG4178 427 RVLFLPQRpyLPLG---TLREALL---YP-ATA----EAFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlsQERGLTVIAVLH 206
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-235 |
5.71e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.51 E-value: 5.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 4 YTNHSDTTFAlrnisfrvpGRTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA- 82
Cdd:PRK13649 10 YTYQAGTPFE---------GRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 --FARKVAYLPQQLPPAE--GMTVRELVAIGryPWHgalgrFGAADREKV---EEAISLVGL-KPLAHRLVDSLSGGERQ 154
Cdd:PRK13649 80 ikQIRKKVGLVFQFPESQlfEETVLKDVAFG--PQN-----FGVSQEEAEalaREKLALVGIsESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
.
gi 15829409 235 I 235
Cdd:PRK13649 232 I 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-235 |
6.77e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 8 SDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK- 86
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQLPPAEGMTVRE--LVAIGRYPWHGALG------RFGAADREKVEEA---ISLVGLKPLAHRLVDSLSGGERQR 155
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIEnlLVAQHQQLKTGLFSgllktpAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-235 |
1.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAE--GMTVRELVA 107
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQivATIVEEDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 108 IGryPWHgaLGRFGAADREKVEEAISLVGL---KPLAHRLvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
Cdd:PRK13633 109 FG--PEN--LGIPPEEIRERVDESLKKVGMyeyRRHAPHL---LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829409 185 DVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-245 |
1.31e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAY 89
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQLPPAEGMTVRE-LVAIGRYpwHGALGRFGAADRekVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK10895 83 LPQEASIFRRLSVYDnLMAVLQI--RDDLSAEQREDR--ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIY 245
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-225 |
1.55e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.90 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 10 TTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafARKVAY 89
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------AREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQ---LPPAEgmTVRELVAIG-RYPWhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
Cdd:PRK11247 85 LMFQdarLLPWK--KVIDNVGLGlKGQW-----------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-257 |
2.33e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.60 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFA--RKVAYL 90
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrSRLYTvrKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAigrYPW--HGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK11831 90 FQSGALFTDMNVFDNVA---YPLreHTQLPA--PLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGE---TLEMIY 245
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdprVRQFLD 244
|
250
....*....|....
gi 15829409 246 GIPMGILP--HPAG 257
Cdd:PRK11831 245 GIADGPVPfrYPAG 258
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-236 |
2.57e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.80 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPPAEGMTVRELV 106
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 107 AIGRypwhgALGRFGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
Cdd:PRK10070 128 AFGM-----ELAGINAEERrEKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829409 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-241 |
3.68e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRT-----LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKM-------------LGRHQPPSEGEILLDAQPL 75
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtiVGDYAIPANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 76 eswsskafaRKVAYLPQQLPPAEGM--TVRELVAIGryPWHgaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGE 152
Cdd:PRK13645 89 ---------RKEIGLVFQFPEYQLFqeTIEKDIAFG--PVN--LGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
....*....
gi 15829409 233 AEIMRGETL 241
Cdd:PRK13645 236 FEIFSNQEL 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-218 |
4.95e-23 |
|
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: 94.36 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKML--------GRHQ-PPSEGEILLDAQPLESwsSKAFAR------KVAYLPQ---QLPPAE 98
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILagklkpnlGKFDdPPDWDEILDEFRGSEL--QNYFTKllegdvKVIVKPQyvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 GMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
Cdd:cd03236 104 KGKVGELLK-------------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829409 179 DIAHQVDVLALVHRLSQErGLTVIAVLHDINMaaryCDYL 218
Cdd:cd03236 171 DIKQRLNAARLIRELAED-DNYVLVVEHDLAV----LDYL 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-225 |
5.66e-23 |
|
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: 91.36 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSKAfarKVAYLPQq 93
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTV---KIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 lppaegmtvrelvaigrypwhgalgrfgaadrekveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:cd03221 71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15829409 174 PTSALDIAHqvdVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGE 225
Cdd:cd03221 97 PTNHLDLES---IEALEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-232 |
5.88e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GR-HQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHpKYEVTSGSILLDGEDILELSPDERARAGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPA-EGMTVRELV-----AIGRYPWHgalgrfGAADREKVEEAISLVGLKP-LAHRLVD-SLSGGERQRAWIAMLVA 163
Cdd:COG0396 83 FQYPVEiPGVSVSNFLrtalnARRGEELS------AREFLKLLKEKMKELGLDEdFLDRYVNeGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 164 QDSRCLLLDEPTSALDIahqvDVLALVHR-----LSQERGLTVIA----VLHDINmaaryCDYLVALRGGEMIAQGTP 232
Cdd:COG0396 157 LEPKLAILDETDSGLDI----DALRIVAEgvnklRSPDRGILIIThyqrILDYIK-----PDFVHVLVDGRIVKSGGK 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-236 |
6.08e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.67 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 6 NHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 kVAYLPQQLPPAEGMTVRE-LVAIGRYpwhgalgrFGAADREkVEEAI-SLVGLKPL---AHRLVDSLSGGERQRAWIAM 160
Cdd:PRK13536 116 -IGVVPQFDNLDLEFTVREnLLVFGRY--------FGMSTRE-IEAVIpSLLEFARLeskADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 161 LVAQDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLD-PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-213 |
7.71e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQ--QLPPaeG 99
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQfhHLLP--D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 100 MTVRELVA----IGrypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
Cdd:PRK11629 102 FTALENVAmpllIG--------KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 15829409 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAAR 213
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-210 |
8.95e-23 |
|
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: 97.16 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafarKVAYLPQQLPPAEGMTVRELVaigrypwHGA 116
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDL-------------KISYKPQYISPDYDGTVEEFL-------RSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 117 LGRFGAADREKVEEAISLvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
Cdd:COG1245 426 NTDDFGSSYYKTEIIKPL-GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|....
gi 15829409 197 RGLTVIAVLHDINM 210
Cdd:COG1245 505 RGKTAMVVDHDIYL 518
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-242 |
9.14e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:PRK13644 4 LENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAE--GMTVRELVAIGryPWHGALGRFGAadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK13644 84 QNPETQfvGRTVEEDLAFG--PENLCLPPIEI--RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEIMRGETLE 242
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-235 |
1.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR-----HQPPSEGEILLDAQPLESWSSKAFARKVA 88
Cdd:PRK14247 6 IRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDVIELRRRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQQLPPAEGMTVRELVAIGRypwhgALGRFGAADRE---KVEEAISLVGL-KPLAHRL---VDSLSGGERQRAWIAML 161
Cdd:PRK14247 86 MVFQIPNPIPNLSIFENVALGL-----KLNRLVKSKKElqeRVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-237 |
1.12e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 4 YTNHSDTTFALRnisfrvpgrtLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83
Cdd:PRK13643 9 YTYQPNSPFASR----------ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 84 ---ARKVAYLPQQLPPAEGM--TVRELVAIGryPWHGALGRfgaADREKVE-EAISLVGL-KPLAHRLVDSLSGGERQRA 156
Cdd:PRK13643 79 ikpVRKKVGVVFQFPESQLFeeTVLKDVAFG--PQNFGIPK---EKAEKIAaEKLEMVGLaDEFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
.
gi 15829409 237 R 237
Cdd:PRK13643 233 Q 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-224 |
1.23e-22 |
|
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: 92.88 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWS--SKAFARKVAYLPQQ----- 93
Cdd:COG4778 21 GKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD--GGWVdlAQASPREILALRRRtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 ------LP--PAegmtvRELVAigrypwhGALGRFGAAD---REKVEEAISLVGLKPlahRLVDS----LSGGERQRAWI 158
Cdd:COG4778 99 sqflrvIPrvSA-----LDVVA-------EPLLERGVDReeaRARARELLARLNLPE---RLWDLppatFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGG 224
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-239 |
1.43e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLPQ- 92
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 -QLPPaeGMTVRE-LVAIGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK13537 89 dNLDP--DFTVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 171 LDEPTSALDiaHQVDVLaLVHRLSQ--ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGE 239
Cdd:PRK13537 162 LDEPTTGLD--PQARHL-MWERLRSllARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-206 |
1.74e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 91.79 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPPAEGMTV 102
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 103 RELVaigrypwhgalgRFGAAD--REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:cd03231 91 LENL------------RFWHADhsDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*.
gi 15829409 181 AhQVDVLALVHRLSQERGLTVIAVLH 206
Cdd:cd03231 159 A-GVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-235 |
2.52e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPPAE--GMTVRE 104
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN-PDNQfvGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 105 LVAIGrypwhgaLGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
Cdd:PRK13642 102 DVAFG-------MENQGIPREEmikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829409 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-210 |
3.40e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 95.26 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafarKVAYLPQQLPPAEGMTVRELVAigrypwhGA 116
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-------------KISYKPQYIKPDYDGTVEDLLR-------SI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 117 LGRFGAADREkvEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
Cdd:PRK13409 425 TDDLGSSYYK--SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEE 502
|
170
....*....|....
gi 15829409 197 RGLTVIAVLHDINM 210
Cdd:PRK13409 503 REATALVVDHDIYM 516
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-211 |
3.46e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYLPQQ 93
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEgmTVRELVAIGRypwhgALGRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:PRK11248 81 LLPWR--NVQDNVAFGL-----QLAGVEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMA 211
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-237 |
3.50e-22 |
|
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: 95.27 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
Cdd:COG5265 361 ENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 lppaegmTV------RELVAIGRyPwhgalgrfgAADREKVEEAISLVGLkplaHRLVDS---------------LSGGE 152
Cdd:COG5265 441 -------TVlfndtiAYNIAYGR-P---------DASEEEVEAAARAAQI----HDFIESlpdgydtrvgerglkLSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTP 232
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERGTH 576
|
....*
gi 15829409 233 AEIMR 237
Cdd:COG5265 577 AELLA 581
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-206 |
4.65e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.50 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAFARKVAYLPQ 92
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIgrypWHgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:TIGR01189 81 LPGLKPELSALENLHF----WA----AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....
gi 15829409 173 EPTSALDIAhQVDVLALVHRLSQERGLTVIAVLH 206
Cdd:TIGR01189 153 EPTTALDKA-GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-206 |
4.95e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.70 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARkVAYLPQQ--LPPAegM 100
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD--PDVAEA-CHYLGHRnaMKPA--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVAIgrypWHGALGrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:PRK13539 89 TVAENLEF----WAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*...
gi 15829409 181 AHQVDVLALV--HRlsqERGLTVIAVLH 206
Cdd:PRK13539 161 AAVALFAELIraHL---AQGGIVIAATH 185
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-231 |
5.20e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.19 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 4 YTNHSDTTFALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
Cdd:TIGR01193 466 ELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 83 FARKVAYLPQQlPPAEGMTVRELVAIGRYPwhgalgrfgAADREKVEEAISLVGLK------PLAH--RLVD---SLSGG 151
Cdd:TIGR01193 546 LRQFINYLPQE-PYIFSGSILENLLLGAKE---------NVSQDEIWAACEIAEIKddienmPLGYqtELSEegsSISGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErglTVIAVLHDINMAARyCDYLVALRGGEMIAQGT 231
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGS 691
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-237 |
5.77e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPPAEGMT 101
Cdd:PRK10851 13 GRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 102 VRELVAIGR--YPWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
Cdd:PRK10851 91 VFDNIAFGLtvLPRRERPNA--AAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-237 |
6.23e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPgRTLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRhQPP----SEGEILLDAQPLESWSSKAfaR 85
Cdd:PRK10418 4 QIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGI-LPAgvrqTAGRVLLDGKPVAPCALRG--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQlPPAEGMTVRELVAIGRYPWHgALGRfgAADREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAWIAML 161
Cdd:PRK10418 80 KIATIMQN-PRSAFNPLHTMHTHARETCL-ALGK--PADDATLTAALEAVGL-ENAARVLKLypfeMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-214 |
6.97e-22 |
|
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: 94.23 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldAQPleswsskafARKVAYLPQ--QLPPAEg 99
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--PQP---------GIKVGYLPQepQLDPTK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 100 mTVRELVAIGRYPWHGALGRFG----------------AADREKVEEAISLVGLKPLAHRL---------------VDSL 148
Cdd:TIGR03719 84 -TVRENVEEGVAEIKDALDRFNeisakyaepdadfdklAAEQAELQEIIDAADAWDLDSQLeiamdalrcppwdadVTKL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLAlvHRLSQERGlTVIAVLHDinmaaRY 214
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPG-TVVAVTHD-----RY 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-218 |
7.34e-22 |
|
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: 94.47 E-value: 7.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKML--------GRHQ-PPSEGEILldaqpleswssKAFAR---------------KVAYLPQ 92
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILsgelkpnlGDYDeEPSWDEVL-----------KRFRGtelqdyfkklangeiKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 ---QLPPAEGMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
Cdd:COG1245 168 yvdLIPKVFKGTVRELLE-------------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829409 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMaaryCDYL 218
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAI----LDYL 278
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-257 |
7.71e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.23 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLESWSSKAFARK-VAYL 90
Cdd:PRK13549 8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAgIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREkVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK13549 88 HQELALVKELSVLENIFLGNEITPGGIMDYDAMYLR-AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMG 250
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGRELT 245
|
250
....*....|.
gi 15829409 251 IL----PHPAG 257
Cdd:PRK13549 246 ALyprePHTIG 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-237 |
8.67e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISfrvpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHqPPSEGEILLDAQPLESWS-SKAFARK 86
Cdd:COG1129 254 EVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfGAD-PADSGEIRLDGKPVRIRSpRDAIRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPqqlppaE---------GMTVRE---LVAIGRYPWHGALGRfgAADREKVEEAISLVGLK-PLAHRLVDSLSGGER 153
Cdd:COG1129 329 IAYVP------EdrkgeglvlDLSIREnitLASLDRLSRGGLLDR--RRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIA----- 228
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGeldre 479
|
....*....
gi 15829409 229 QGTPAEIMR 237
Cdd:COG1129 480 EATEEAIMA 488
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-230 |
1.39e-21 |
|
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: 88.52 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsSKAFARKVAY 89
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQlPPAEGMTVRElvaigrypwhgALGRfgaadrekveeaislvglkplahrlvdSLSGGERQRAWIAMLVAQDSRCL 169
Cdd:cd03247 80 LNQR-PYLFDTTLRN-----------NLGR---------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 170 LLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDInMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-206 |
1.49e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.63 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNisfrvpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88
Cdd:PRK10790 345 NVSFAYRD------DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 yLPQQLPPAEGMTVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAW 157
Cdd:PRK10790 419 -MVQQDPVVLADTFLANVTLGR-----------DISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALD-------------IAHQVDVLALVHRLSQERGLTVIAVLH 206
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDsgteqaiqqalaaVREHTTLVVIAHRLSTIVEADTILVLH 548
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-258 |
1.78e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 93.33 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKML--------GRHQ-PPSEGEILldaqpleswssKAFAR---------------KVAYLPQ 92
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILsgelipnlGDYEeEPSWDEVL-----------KRFRGtelqnyfkklyngeiKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 ---QLPPAEGMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
Cdd:PRK13409 168 yvdLIPKVFKGKVRELLK-------------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 170 LLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMaaryCDYLValrggemiaqgtpaeimrgETLEMIYGIP- 248
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAV----LDYLA-------------------DNVHIAYGEPg 289
|
250
....*....|.
gi 15829409 249 -MGILPHPAGA 258
Cdd:PRK13409 290 aYGVVSKPKGV 300
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-246 |
2.05e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.93 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQ 92
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGRYPWHGALGrFGAAD----REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK09700 88 ELSVIDELTVLENLYIGRHLTKKVCG-VNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 169 LLLDEPTSALDIAhQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYG 246
Cdd:PRK09700 167 IIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-230 |
2.34e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.13 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFrvpgrtllhplslTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDaqpleswsskafaRKVAYLpq 92
Cdd:cd03220 37 ALKDVSF-------------EVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR-------------GRVSSL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 qLPPAEGM----TVRE-LVAIGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:cd03220 89 -LGLGGGFnpelTGREnIYLNGRL-----LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-236 |
3.82e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:PRK11176 345 RNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLppaegMTVRELVA--IgrypwhgALGRFGAADREKVEEAISLVG----LKPLAHRLvD--------SLSGGERQRAWI 158
Cdd:PRK11176 425 NV-----HLFNDTIAnnI-------AYARTEQYSREQIEEAARMAYamdfINKMDNGL-DtvigengvLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhRLSTIEKA----DEILVVEDGEIVERGTHAELL 566
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-237 |
3.99e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQ 93
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGMTVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:PRK11432 87 YALFPHMSLGENVGYGL----KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-231 |
7.85e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD------AQPLESWSSKAFARKV 87
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfSQKPSEKAIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 88 AYLPQQ--LPPAegMTVRE--LVAIGRypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
Cdd:COG4161 85 GMVFQQynLWPH--LTVMEnlIEAPCK-----VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 164 QDSRCLLLDEPTSALD--IAHQvdVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
Cdd:COG4161 158 MEPQVLLFDEPTAALDpeITAQ--VVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-235 |
2.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTL----LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS----KAFARKVAyLPQQ 93
Cdd:PRK13641 14 PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVS-LVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGM--TVRELVAIGryPWHgalgrFGAADREKVEEA---ISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:PRK13641 93 FPEAQLFenTVLKDVEFG--PKN-----FGFSEDEAKEKAlkwLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-236 |
2.45e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.33 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA-------------YLPQ 92
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVAdknqlrllrtrltMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAigRYPWHgALGRFGAADREKVEEAISLVGLKPLAH-RLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK10619 100 HFNLWSHMTVLENVM--EAPIQ-VLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-257 |
6.64e-20 |
|
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: 88.73 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLESWSSKAFARK-VAYL 90
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAIGRYPWH-GALGRFGAADReKVEEAISLVGLKPL-AHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:TIGR02633 84 HQELTLVPELSVAENIFLGNEITLpGGRMAYNAMYL-RAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQgTPAEIMRGE-TLEMIYGI 247
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSEDdIITMMVGR 240
|
250
....*....|....
gi 15829409 248 PMGIL----PHPAG 257
Cdd:TIGR02633 241 EITSLyphePHEIG 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-235 |
8.41e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpSEGEILLDAQpLESWSSKAFARKVAY--LP 91
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-VEFFNQNIYERRVNLnrLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQL------PPAEGMTVRELVAIGR--YPWHGALGRFGAadrekVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIA 159
Cdd:PRK14258 88 RQVsmvhpkPNLFPMSVYDNVAYGVkiVGWRPKLEIDDI-----VESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG-----GEMIAQGTPAE 234
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242
|
.
gi 15829409 235 I 235
Cdd:PRK14258 243 I 243
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
11-235 |
1.04e-19 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 88.02 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
Cdd:TIGR01192 334 AVEFRHITFEFANSSQgVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQlppaEGM---TVRELVAIGRYpwhgalgrfGAADREKVEEAISLVglkplAHRLVDS---------------LSGG 151
Cdd:TIGR01192 414 VFQD----AGLfnrSIRENIRLGRE---------GATDEEVYEAAKAAA-----AHDFILKrsngydtlvgergnrLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGT 231
Cdd:TIGR01192 476 ERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIA--HRLS-TVRNADLVLFLDQGRLIEKGS 552
|
....
gi 15829409 232 PAEI 235
Cdd:TIGR01192 553 FQEL 556
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
31-235 |
1.76e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQ----LPPAE--GMT 101
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNpygsLNPRKkvGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 102 VRELVAIgrypwHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIA---MLvaqDSRCLLLDEPTSA 177
Cdd:PRK11308 115 LEEPLLI-----NTSLSA--AERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIAralML---DPDVVVADEPVSA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-214 |
1.95e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 87.10 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTLLHPLSLTF-PAGKVtGLIGHNGSGKSTLLK-MLGRHQpPSEGEilldAQPLESWsskafarKVAYLPQQLPPAEG 99
Cdd:PRK11819 18 PKKQILKDISLSFfPGAKI-GVLGLNGAGKSTLLRiMAGVDK-EFEGE----ARPAPGI-------KVGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 100 MTVRELVAIGRYPWHGALGRFG----------------AADREKVEEAISLVGLKPLAHRL---------------VDSL 148
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDRFNeiyaayaepdadfdalAAEQGELQEIIDAADAWDLDSQLeiamdalrcppwdakVTKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLAlvHRLSQERGlTVIAVLHDinmaaRY 214
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--QFLHDYPG-TVVAVTHD-----RY 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-234 |
2.03e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLESWSskaFARKVAYLPQQ---LP 95
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKE---MRAISAYVQQDdlfIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 96 paeGMTVRE-LVaigrYPWHGALGRFGAAD--REKVEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAMLVAQDS 166
Cdd:TIGR00955 113 ---TLTVREhLM----FQAHLRMPRRVTKKekRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 167 RCLLLDEPTSALD--IAHQvdVLALVHRLSQeRGLTVIAVLHDINmAARYC--DYLVALRGGEMIAQGTPAE 234
Cdd:TIGR00955 186 PLLFCDEPTSGLDsfMAYS--VVQVLKGLAQ-KGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-247 |
2.29e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPLESWSSK-AFARKVAY 89
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrySGDVLLGGRSIFNYRDVlEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQlPPAEGMTVRELVAIGRYPwHGALGRfgAADREKVEEAISLVGL-KPLAHRLVDS---LSGGERQRAWIAMLVAQD 165
Cdd:PRK14271 106 LFQR-PNPFPMSIMDNVLAGVRA-HKLVPR--KEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM----RGETL 241
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFsspkHAETA 259
|
....*.
gi 15829409 242 EMIYGI 247
Cdd:PRK14271 260 RYVAGL 265
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-206 |
2.30e-19 |
|
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: 82.20 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsSKAFARKVAYL 90
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQ--LPPAegmTVRELVAigrYPWHgalgrfgaadrekveeaislvglkplahrlvDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:cd03223 70 PQRpyLPLG---TLREQLI---YPWD-------------------------------DVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 15829409 169 LLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLH 206
Cdd:cd03223 113 VFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-231 |
3.71e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 17 ISFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGR-HQPPSE---GEILLDAQPLESWSSKAF----AR 85
Cdd:PRK15134 13 VAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLlPSPPVVypsGDIRFHGESLLHASEQTLrgvrGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQ----LPPAEGM--TVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD---SLSGGERQRA 156
Cdd:PRK15134 93 KIAMIFQEpmvsLNPLHTLekQLYEVLSLHR-------GMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-245 |
4.28e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPPAEGMTVREL 105
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 106 VAIGrypwhgalGRFgaADREKVEEAISLV-GLKP-LAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:PRK11614 101 LAMG--------GFF--AERDQFQERIKWVyELFPrLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 181 AHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIY 245
Cdd:PRK11614 171 IIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-225 |
4.43e-19 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 82.52 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 5 TNHSDTTFALRNISFrvpgrtllhplslTFPAGKVTGLIGHNGSGKSTLLK-MLGrHQPPSEGEIlldaqpleswsskAF 83
Cdd:cd03250 12 SGEQETSFTLKDINL-------------EVPKGELVAIVGPVGSGKSSLLSaLLG-ELEKLSGSV-------------SV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 84 ARKVAYLPQQlPPAEGMTVRELVAIGrYPWhgalgrfgaaDREKVEEAISLVGLKPLAHRLVD-----------SLSGGE 152
Cdd:cd03250 65 PGSIAYVSQE-PWIQNGTIRENILFG-KPF----------DEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVL---ALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGE 225
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVD-AHVGRHIfenCILGLLLNNK--TRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-231 |
6.81e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-------LDAQPLESwSSKAFARK 86
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDK-AIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQ--LPPAegMTVRE-LV-AIGRypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
Cdd:PRK11124 84 VGMVFQQynLWPH--LTVQQnLIeAPCR-----VLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 163 AQDSRCLLLDEPTSALD--IAHQvdVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDpeITAQ--IVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-235 |
8.31e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKML-G-RHqpPSEGEIL-LDAQPLEswSSKAFARKVAY 89
Cdd:COG4586 37 AVDDISFTIE-------------PGEIVGFIGPNGAGKSTTIKMLtGiLV--PTSGEVRvLGYVPFK--RRKEFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 L---PQQL----PPAEGmtvrelvaigrYPWHGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
Cdd:COG4586 100 VfgqRSQLwwdlPAIDS-----------FRLLKAIYRIPDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-237 |
9.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.29 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF---ARKVAYLPQQLPPA---EGM 100
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpVRKRIGMVFQFPESqlfEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVaigrypwhgalgrFGAAD-REKVEEAislvglKPLAHRLVDSL--------------SGGERQRAWIAMLVAQD 165
Cdd:PRK13646 103 VEREII-------------FGPKNfKMNLDEV------KNYAHRLLMDLgfsrdvmsqspfqmSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-230 |
1.11e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.67 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL---DAQPLESWS-SKAFARKVA-- 88
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlSEAERRRLLrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 ---YLPQQlpPAEG--MTV-------RELVAIG-RYpwHGALgRFGAAD-REKVEEAISlvglkplahRLVD---SLSGG 151
Cdd:PRK11701 90 ewgFVHQH--PRDGlrMQVsaggnigERLMAVGaRH--YGDI-RATAGDwLERVEIDAA---------RIDDlptTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-242 |
1.18e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPPAEGMTVRE-LVAig 109
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRVGYMSQAFSLYGELTVRQnLEL-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 110 rypwHGALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAldiahqVDVLA 188
Cdd:NF033858 363 ----HARLFHLPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG------VDPVA 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 189 ------LVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMR---GETLE 242
Cdd:NF033858 433 rdmfwrLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAargAATLE 494
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-228 |
1.22e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----------KVAYLPQQLPP 96
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfgfifQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 97 AEGMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:PRK10535 104 AQNVEVPAVYA-------------GLERKQRLLRAQELLQRLGLEDRVeyqPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 174 PTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIA 228
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVR 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-237 |
1.56e-18 |
|
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: 84.47 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI----------LLDAQPLESWSSKafaRKVAYLPQQLPPAEG 99
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdMTKPGPDGRGRAK---RYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 100 MTVRELV--AIG-RYPWHgaLGRFGAA--------DREKVEEAISlvglkplahRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:TIGR03269 380 RTVLDNLteAIGlELPDE--LARMKAVitlkmvgfDEEKAEEILD---------KYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-226 |
1.75e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL----ESWSSKAFARKVAYLPQQLPPAEGM 100
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVAIgrypwhGALGRfGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
Cdd:PRK10584 104 NALENVEL------PALLR-GESSRQSRNGAKALleqLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829409 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-227 |
2.33e-18 |
|
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: 80.37 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPG----RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG--RHQPPSEGEILLDAQPLEswssKAFAR 85
Cdd:cd03232 4 LTWKNLNYTVPVkggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQLPPAEGMTVRElvaigrypwhgALgRFGAADREkveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQD 165
Cdd:cd03232 80 STGYVEQQDVHSPNLTVRE-----------AL-RFSALLRG---------------------LSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829409 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAA-RYCDYLVAL-RGGEMI 227
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHQPSASIfEKFDRLLLLkRGGKTV 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-235 |
3.27e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQ--QLPPAegMTVRel 105
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQdaRLFPH--YKVR-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 106 vaigrypwhGALgRFGAA--DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWI--AMLVAQDsrCLLLDEPTSALDIA 181
Cdd:PRK11144 95 ---------GNL-RYGMAksMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIgrALLTAPE--LLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829409 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
27-246 |
4.71e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.98 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDAQPLESWSSKAFA-RKVAYLPQQLPPAEGM 100
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDlRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVAIGrypwhgaLGRFGAADREKVEEAI--SLVGLK---PLAHRLVDS---LSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:PRK14239 101 SIYENVVYG-------LRLKGIKDKQVLDEAVekSLKGASiwdEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM----RGETLEMIYG 246
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFmnpkHKETEDYISG 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-226 |
5.05e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQQLppaeGM-- 100
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI----TRLKNREVPFLRRQI----GMif 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 ---------TVRELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK10908 86 qdhhllmdrTVYDNVAI---PLIIA-GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-237 |
5.54e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.97 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKM-LGRHqpPSEGEILLDAQPLESWSSKAFARKVAYLPQ--QLPPAeg 99
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAlLGFL--PYQGSLKINGIELRELDPESWRKHLSWVGQnpQLPHG-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 100 mTVRELVAIGRYpwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK11174 438 -TLRDNVLLGNP----------DASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQerGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-250 |
7.78e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.47 E-value: 7.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQ 92
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGRYPWHGALgrfgaADREKV---EEAI-SLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMF-----VDQDKMyrdTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 169 LLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAqgtpAEIMRGETLEMIYGIP 248
Cdd:PRK10982 156 VIMDEPTSSLT-EKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA----TQPLAGLTMDKIIAMM 230
|
..
gi 15829409 249 MG 250
Cdd:PRK10982 231 VG 232
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
14-202 |
1.18e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 79.61 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHqPPSE---GEILLDAQPLESWSSKAFARKVAYL 90
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-PSYEvtsGTILFKGQDLLELEPDERARAGLFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPA-EGMTVRELV-----AIGRYPWHGALGRFgaADREKVEEAISLVGLKP-LAHRLV-DSLSGGERQRAWIAMLV 162
Cdd:TIGR01978 82 AFQYPEEiPGVSNLEFLrsalnARRSARGEEPLDLL--DFEKLLKEKLALLDMDEeFLNRSVnEGFSGGEKKRNEILQMA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15829409 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRL-SQERGLTVI 202
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDIDALKIVAEGINRLrEPDRSFLII 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-236 |
2.12e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
Cdd:PRK15112 13 TFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQlpPAEGMTVRELVA-IGRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK15112 93 FQD--PSTSLNPRQRISqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-242 |
2.64e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG---RHQppsEGEI-LLDAQPLESWSSKAFARKVAY 89
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarKIQ---QGRVeVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQLppaeG------MTVRELVAigrypWHGALgrFG--AADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQR----- 155
Cdd:NF033858 81 MPQGL----GknlyptLSVFENLD-----FFGRL--FGqdAAERRrRIDELLRATGLAPFADRPAGKLSGGMKQKlglcc 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 156 AWIamlvaQDSRCLLLDEPTSAldiahqVDVLA------LVHRLSQER-GLTVIAVLHDINMAARYcDYLVALRGGEMIA 228
Cdd:NF033858 150 ALI-----HDPDLLILDEPTTG------VDPLSrrqfweLIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217
|
250
....*....|....*..
gi 15829409 229 QGTPAEIMR---GETLE 242
Cdd:NF033858 218 TGTPAELLArtgADTLE 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-180 |
2.72e-17 |
|
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: 81.13 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDAqpleswsskafARKVAYLPQQ---LPPAE 98
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMItGQEQPDS-GTIEIGE-----------TVKLAYVDQSrdaLDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 gmTVRELVA-------IGRY--PWHGALGRFG--AADREKveeaislvglkplahrLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:TIGR03719 402 --TVWEEISggldiikLGKReiPSRAYVGRFNfkGSDQQK----------------KVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|...
gi 15829409 168 CLLLDEPTSALDI 180
Cdd:TIGR03719 464 VLLLDEPTNDLDV 476
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-232 |
3.02e-17 |
|
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: 77.92 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlP 95
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQD-P 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 96 PAEGMTVRElvaigrypwhgALGRFGAADREKVEEAISLVGLK------PLAHRLV-----DSLSGGERQ-----RawiA 159
Cdd:cd03244 88 VLFSGTIRS-----------NLDPFGEYSDEELWQALERVGLKefveslPGGLDTVveeggENLSVGQRQllclaR---A 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 160 MLvaQDSRCLLLDEPTSALDiaHQVDvlALVHRLSQE--RGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTP 232
Cdd:cd03244 154 LL--RKSKILVLDEATASVD--PETD--ALIQKTIREafKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-230 |
3.96e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.25 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEG-----EILLDA-QPLESWSS--KAFAR 85
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQKGliRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLPQQLPPAEGMTVRELVAIGRYpwhgalgrfgAADREKVEEAISL-------VGLKPLAHRLVDSLSGGERQRAWI 158
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPV----------IVKGEPKEEATARarellakVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-180 |
6.85e-17 |
|
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: 76.41 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQP-PSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKYeVTEGEILFKGEDITDLPPEERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPA-EGMTVRELVaigRYpwhgalgrfgaadrekveeaislvglkplahrLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:cd03217 83 FQYPPEiPGVKNADFL---RY--------------------------------VNEGFSGGEKKRNEILQLLLLEPDLAI 127
|
170
....*....|
gi 15829409 171 LDEPTSALDI 180
Cdd:cd03217 128 LDEPDSGLDI 137
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-203 |
7.13e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQq 93
Cdd:PRK13657 338 DDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 lppaEGM----TVRELVAIGR-----YPWHGALGRFGAAD-REKVEEaislvGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
Cdd:PRK13657 417 ----DAGlfnrSIEDNIRVGRpdatdEEMRAAAERAQAHDfIERKPD-----GYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829409 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA 203
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-246 |
8.59e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF-ARKVAYLP 91
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVAIGRYPwhgaLGRFGAADREKV-EEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGREF----VNRFGRIDWKKMyAEADKLlarLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 168 CLLLDEPTSALDIAHQVDVLALVHRL-SQERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYG 246
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELkSQGRGIVYIS--HRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVG 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-235 |
1.01e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.46 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQ-PPSEGEIL---------------------- 69
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrGMDQyEPTSGRIIyhvalcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 70 ------LDAQPLESWS-----SKAFARKVAYLPQQ-LPPAEGMTVRELVAigrypwhGALGRFGAADREKVEEAISLVGL 137
Cdd:TIGR03269 83 pvcggtLEPEEVDFWNlsdklRRRIRKRIAIMLQRtFALYGDDTVLDNVL-------EALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 138 KPLAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARY 214
Cdd:TIGR03269 156 VQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|.
gi 15829409 215 CDYLVALRGGEMIAQGTPAEI 235
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEV 256
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-232 |
1.08e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 19 FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPPAE 98
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 GMTVRELVAIgrypWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
Cdd:TIGR01257 1017 HLTVAEHILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829409 179 DIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
Cdd:TIGR01257 1093 DPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-235 |
1.94e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.42 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR-----HQPPSEGEILL--------DAQPLE 76
Cdd:PRK14267 3 FAIETVNLRVyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllelnEEARVEGEVRLfgrniyspDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 77 swsskaFARKVAYLPQQLPPAEGMTVRELVAIGrYPWHGALGRFGAADrEKVEEAISLVGL-KPLAHRLVD---SLSGGE 152
Cdd:PRK14267 83 ------VRREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELD-ERVEWALKKAALwDEVKDRLNDypsNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
...
gi 15829409 233 AEI 235
Cdd:PRK14267 233 RKV 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-226 |
5.13e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 20 RVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQQlPPAE 98
Cdd:PRK11288 262 GLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdAIRAGIMLCPED-RKAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 GM----TVRELVAIGRYPWHGALGRF--GAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK11288 341 GIipvhSVADNINISARRHHLRAGCLinNRWEAENADRFIRSLNIKtPSREQLIMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-208 |
5.83e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF--ARKVAYLPQQLPPAE---GMTVREL 105
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDPLASlnpRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 106 VAIGRYPWHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
Cdd:PRK15079 121 IAEPLRTYHPKLSR--QEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180
....*....|....*....|....
gi 15829409 185 DVLALVHRLSQERGLTVIAVLHDI 208
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-228 |
7.07e-16 |
|
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: 76.76 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 10 TTFALRNISFRVPGRT-----LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA 84
Cdd:COG4615 326 QTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 85 RKVA------YLPQQLPPAEGMTVRELVAigRYpwhgaLGRFGAADREKVEEaislvglkplaHRLVD-SLSGGERQRaw 157
Cdd:COG4615 406 QLFSavfsdfHLFDRLLGLDGEADPARAR--EL-----LERLELDHKVSVED-----------GRFSTtDLSQGQRKR-- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVA--QDSRCLLLDEPTsaldiAHQ------VDVLALVHRLsQERGLTVIAVLHDinmaARY---CDYLVALRGGEM 226
Cdd:COG4615 466 LALLVAllEDRPILVFDEWA-----ADQdpefrrVFYTELLPEL-KARGKTVIAISHD----DRYfdlADRVLKMDYGKL 535
|
..
gi 15829409 227 IA 228
Cdd:COG4615 536 VE 537
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-207 |
1.10e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.08 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSKAfarKVAYLPQQ 93
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA---NIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPP--AEGMTVRELVAIGRYPWH------GALGR--FGAADREKVeeaislvglkplahrlVDSLSGGERQRAWIAMLVA 163
Cdd:PRK15064 391 HAYdfENDLTLFDWMSQWRQEGDdeqavrGTLGRllFSQDDIKKS----------------VKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15829409 164 QDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHD 207
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDME---SIESLNMALEKYEG-TLIFVSHD 494
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-202 |
1.28e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 15 RNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQ- 93
Cdd:PRK13538 5 RNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDLLYLGHQp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 -----LPPAEGMTvrelvaigrypWHGALGrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
Cdd:PRK13538 84 gikteLTALENLR-----------FYQRLH--GPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 15829409 169 LLLDEPTSALDiAHQVDVLAlvHRLSQ--ERGLTVI 202
Cdd:PRK13538 151 WILDEPFTAID-KQGVARLE--ALLAQhaEQGGMVI 183
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-230 |
1.47e-15 |
|
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: 73.07 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRV----PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLESWSSKaF 83
Cdd:cd03233 3 TLSWRNISFTTgkgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK-Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 84 ARKVAYLPQQ-LPPAEgMTVRELVaigrypwhgalgrfgaadrekvEEAISLVGlkplaHRLVDSLSGGERQRAWIAMLV 162
Cdd:cd03233 82 PGEIIYVSEEdVHFPT-LTVRETL----------------------DFALRCKG-----NEFVRGISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYC-DYLVALRGGEMIAQG 230
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-206 |
1.87e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPP---SEGEILLDAQPLESwsskAF 83
Cdd:TIGR00956 759 IFHWRNLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS----SF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 84 ARKVAYLPQQLPPAEGMTVRElvaigrypwhgALgRFGAADR--------EK---VEEAISLVGLKPLAHRLV----DSL 148
Cdd:TIGR00956 835 QRSIGYVQQQDLHLPTSTVRE-----------SL-RFSAYLRqpksvsksEKmeyVEEVIKLLEMESYADAVVgvpgEGL 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 149 SGGERQRAWIAM-LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLH 206
Cdd:TIGR00956 903 NVEQRKRLTIGVeLVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-226 |
1.94e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.08 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISfrVPGRtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYL 90
Cdd:cd03215 5 LEVRGLS--VKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PqqlppaegmtvrelvaigrypwhgalgrfgaADREKVeeaiSLVGLKPLAHRLV--DSLSGGERQRAWIAMLVAQDSRC 168
Cdd:cd03215 81 P-------------------------------EDRKRE----GLVLDLSVAENIAlsSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 169 LLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
10-232 |
2.53e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 10 TTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafaRKVAY 89
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----------LRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 90 LPQQ--LPPAEGMTVRELVAIgrypwhgalgrfgaadREKVEEAISLVGLKPL-AHRLVDS----LSGGERQRAWIAMLV 162
Cdd:PRK09544 72 VPQKlyLDTTLPLTVNRFLRL----------------RPGTKKEDILPALKRVqAGHLIDApmqkLSGGETQRVLLARAL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALrGGEMIAQGTP 232
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTP 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-180 |
5.14e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDaqplESwsskafaRKVAYLPQQ---LPPAE 98
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMItGQEQPDS-GTIKIG----ET-------VKLAYVDQSrdaLDPNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 gmTVRELVA-------IGRY--PWHGALGRFG--AADREKveeaislvglkplahrLVDSLSGGERQRAWIAMLVAQDSR 167
Cdd:PRK11819 404 --TVWEEISggldiikVGNReiPSRAYVGRFNfkGGDQQK----------------KVGVLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|...
gi 15829409 168 CLLLDEPTSALDI 180
Cdd:PRK11819 466 VLLLDEPTNDLDV 478
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-237 |
5.17e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 19 FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqplesWSskafARKVAYLPQQlPPAE 98
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WA----ERSIAYVPQQ-AWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 99 GMTVRelvaigrypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSR 167
Cdd:PTZ00243 734 NATVR-----------GNILFFDEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 168 CLLLDEPTSALDiAHqvdvlaLVHRLSQE------RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PTZ00243 803 VYLLDDPLSALD-AH------VGERVVEEcflgalAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMR 870
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-240 |
5.36e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.63 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 26 LLHPLSL-TFPAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPPAEGMTVRe 104
Cdd:PLN03232 1251 VLHGLSFfVSPSEKV-GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-PVLFSGTVR- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 105 lVAIGRYPWHGALGRFGAADREKVEEAI--SLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIah 182
Cdd:PLN03232 1328 -FNIDPFSEHNDADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV-- 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 183 QVDvlALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMRGET 240
Cdd:PLN03232 1405 RTD--SLIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
43-235 |
5.37e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkvaylpQQLPPAE---GM-----------TVRELVAI 108
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM----------------NDVPPAErgvGMvfqsyalyphlSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 109 GRypwhgALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIA-MLVAQdSRCLLLDEPTSALDIAHQVDV 186
Cdd:PRK11000 99 GL-----KLAGAKKEEINQrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGrTLVAE-PSVFLLDEPLSNLDAALRVQM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829409 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEmIAQ-GTPAEI 235
Cdd:PRK11000 173 RIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR-VAQvGKPLEL 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-239 |
5.58e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI---LLDAQPLESWS-----------SKAFARKVAYLPQ 92
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKekekvleklviQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 --------------QLPPAegmTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLkPLAH--RLVDSLSGGERQRA 156
Cdd:PRK13651 103 irrrvgvvfqfaeyQLFEQ---TIEKDIIFGPV----SMGVSKEEAKKRAAKYIELVGL-DESYlqRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
...
gi 15829409 237 RGE 239
Cdd:PRK13651 254 SDN 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-243 |
1.80e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLEswsskaF-------A 84
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPHGSyEGEILFDGEVCR------FkdirdseA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 85 RKVAYLPQQLPPAEGMTVRELVAIGRYPwhgalGRFGAADREKV-EEAISL---VGLKPLAHRLVDSLSGGERQRAWIAM 160
Cdd:NF040905 78 LGIVIIHQELALIPYLSIAENIFLGNER-----AKRGVIDWNETnRRARELlakVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 161 LVAQDSRCLLLDEPTSAL---DIAHqvdVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIaqgtpaeimr 237
Cdd:NF040905 153 ALSKDVKLLILDEPTAALneeDSAA---LLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI---------- 218
|
....*.
gi 15829409 238 gETLEM 243
Cdd:NF040905 219 -ETLDC 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-244 |
3.21e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQ 92
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGrypwhgaLGRfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:PRK15439 94 EPLLFPNLSVKENILFG-------LPK-RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 173 EPTSALdIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMI 244
Cdd:PRK15439 166 EPTASL-TPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
31-237 |
3.32e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS----------EGEILLDAQPLESwsSKAFARKVAYLPQQ----LPP 96
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKLSPRER--RKIIGREIAMIFQEpsscLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 97 AEgmTV-RELV-AIgryPWHGALGRFGAADREKVEEAISL---VGLKplAHRLVDS-----LSGGERQRAWIAMLVAQDS 166
Cdd:COG4170 105 SA--KIgDQLIeAI---PSWTFKGKWWQRFKWRKKRAIELlhrVGIK--DHKDIMNsypheLTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-207 |
3.65e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.93 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 11 TFALRNISFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDAQPLESWSSKAFARKVA 88
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLtGLYQPQS-GEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 ------YLPQQLPPAEGMTVR-ELVAIgrypWhgaLGRFGAADREKVEEaislvglkplaHRLVD-SLSGGERQRAWIAM 160
Cdd:PRK10522 401 avftdfHLFDQLLGPEGKPANpALVEK----W---LERLKMAHKLELED-----------GRISNlKLSKGQKKRLALLL 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15829409 161 LVAQDSRCLLLDEPTSALD-----IAHQVdvlaLVHRLsQERGLTVIAVLHD 207
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDphfrrEFYQV----LLPLL-QEMGKTIFAISHD 509
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-207 |
1.01e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSeGEILLDAQpLEswsskafarkVAYL 90
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTK-LE----------VAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQ---QLPP--------AEGmtvRELVAIGRYPWH--GALGRFgaadrekveeaisLVGLKPlAHRLVDSLSGGERQRAW 157
Cdd:PRK11147 388 DQhraELDPektvmdnlAEG---KQEVMVNGRPRHvlGYLQDF-------------LFHPKR-AMTPVKALSGGERNRLL 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD 207
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-232 |
1.19e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.82 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTllhplsltfpagKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
Cdd:cd03369 23 VLKNVSFKVKAGE------------KI-GIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QlPPAEGMTVRElvaigrypwhgALGRFGAADREKVEEAISLVGLKplahrlvDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:cd03369 90 D-PTLFSGTIRS-----------NLDPFDEYSDEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829409 173 EPTSALDIAHQvdvlALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTP 232
Cdd:cd03369 151 EATASIDYATD----ALIQKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-241 |
1.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL------DAQPLESWSSKAFARKVAYLPQ------ 92
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKKIKNFKElrrrvs 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 ---QLPPAEGM--TVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDS 166
Cdd:PRK13631 120 mvfQFPEYQLFkdTIEKDIMFGPV----ALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 167 RCLLLDEPTSALDIAHQVDVLALVhRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETL 241
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-206 |
1.78e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP--PSEGEILLDAQPLeswsskafarkvaylPQQ 93
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF---------------GRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEgmtvrelvaigrypwhgALGRFGAADrEKVEeAISLVGLK--PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:COG2401 100 ASLID-----------------AIGRKGDFK-DAVE-LLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 15829409 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLH 206
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
30-237 |
1.81e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.00 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPP---SEGEILLDAQPLESWSSKA----FARKVAYLPQ----QLPPA 97
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKErrnlVGAEVAMIFQdpmtSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 98 E--GMTVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:PRK11022 106 YtvGFQIMEAIKVHQ-------GGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
30-236 |
2.02e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.06 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKML----GRHQPPSEGEILLDAQPLESWSSKAFARKVAY-------LPQQ-LPPA 97
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHnvsmifqEPQScLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 98 EGMTVRELVAIGRYPWHGA-LGRFGAADREKVEeAISLVGLK---PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
Cdd:PRK15093 106 ERVGRQLMQNIPGWTYKGRwWQRFGWRKRRAIE-LLHRVGIKdhkDAMRSFPYELTEGECQKVMIAIALANQPRLLIADE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK15093 185 PTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-248 |
2.32e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISFRVPGRtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS-KAFARKV 87
Cdd:PRK09700 263 ETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 88 AYLPQ---------QLPPAEGMTVRELVAIGRypWHGALGRFGAADREKV-EEAISLVGLKplAHRL---VDSLSGGERQ 154
Cdd:PRK09700 341 AYITEsrrdngffpNFSIAQNMAISRSLKDGG--YKGAMGLFHEVDEQRTaENQRELLALK--CHSVnqnITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
250
....*....|....
gi 15829409 235 IMRGETLeMIYGIP 248
Cdd:PRK09700 496 DMSEEEI-MAWALP 508
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-235 |
3.59e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafaRKVaylpQ 92
Cdd:PRK11650 6 LQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG------------RVV----N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAE--------------GMTVRELVAIG---RypwhgalgRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQ 154
Cdd:PRK11650 70 ELEPADrdiamvfqnyalypHMSVRENMAYGlkiR--------GMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 155 RawIAMLVA--QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGeMIAQ-GT 231
Cdd:PRK11650 142 R--VAMGRAivREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG-VAEQiGT 218
|
....
gi 15829409 232 PAEI 235
Cdd:PRK11650 219 PVEV 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-231 |
3.64e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 18 SFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-----LESWSSKaFArkvayL 90
Cdd:PRK10789 320 QFTYPQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPltklqLDSWRSR-LA-----V 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLPPAEGMTVRELVAIGRyPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIA 159
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGR-P---------DATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 160 MLVAQDSRCLLLDEPTSALD--IAHQVdvlalVHRLSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGT 231
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDgrTEHQI-----LHNLRQwGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGN 532
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-237 |
5.65e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS---------SKAFA 84
Cdd:PRK10261 19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielseqSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 85 RKVAYLPQQLPPAEGMT-------VRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
Cdd:PRK10261 99 RHVRGADMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMR 237
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-257 |
6.45e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 25 TLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGrhqppsegeiLLDAQPLESWSSKAFARKVAYLPQ-QLppaEGMTV 102
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMG----------LLAANGRIGGSATFNGREILNLPEkEL---NKLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 103 RELVAIGRYPW-------------------HGALGRFGA-------ADREKVEEAISLVGLKPlaHRLvdslSGGERQRA 156
Cdd:PRK09473 97 EQISMIFQDPMtslnpymrvgeqlmevlmlHKGMSKAEAfeesvrmLDAVKMPEARKRMKMYP--HEF----SGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVF 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15829409 237 --------------------RGETLEMIYGIPMGILPHPAG 257
Cdd:PRK09473 251 yqpshpysigllnavprldaEGESLLTIPGNPPNLLRLPKG 291
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-224 |
7.34e-13 |
|
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: 65.82 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPPSEGEILLDAQPLESWSSKAFARK---VAYLPQQlPPA 97
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQK-PWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 98 EGMTVRELVAIGrypwhgalGRFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVAQDSRC 168
Cdd:cd03290 91 LNATVEENITFG--------SPFNKQRYKAVTDACSLqpdIDLLPfgdqteIGERGIN-LSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 169 LLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGG 224
Cdd:cd03290 162 VFLDDPFSALDI-HLSDHLmqEGILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-217 |
8.67e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 5 TNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP--PS---EGEILL--------D 71
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFhgknlyapD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 72 AQPLEswsskaFARKVAYLPQQlPPAEGMTVRELVAIGRYpwhgALGRFGAADrEKVEEAISLVGL-KPLAHRLVDS--- 147
Cdd:PRK14243 84 VDPVE------VRRRIGMVFQK-PNPFPKSIYDNIAYGAR----INGYKGDMD-ELVERSLRQAALwDEVKDKLKQSgls 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDY 217
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDM 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-226 |
1.00e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.01 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTV 102
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 103 RELVAIGRYpwhgalgrfgaADRE--KVEEAislVGLKP--------LAHRLVDS---LSGGERQRAWIAMLVAQDSRCL 169
Cdd:TIGR01271 1310 KNLDPYEQW-----------SDEEiwKVAEE---VGLKSvieqfpdkLDFVLVDGgyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 170 LLDEPTSALD-IAHQVDVLALVHRLSQergLTVIAVLHDINmAARYCDYLVALRGGEM 226
Cdd:TIGR01271 1376 LLDEPSAHLDpVTLQIIRKTLKQSFSN---CTVILSEHRVE-ALLECQQFLVIEGSSV 1429
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-230 |
1.11e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVA 88
Cdd:PRK10261 339 AVEKVSFDLwPGETL--------------SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 89 YLPQ----QLPPAE--GMTVRELVAIgrypwHGALGrfGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAML 161
Cdd:PRK10261 405 FIFQdpyaSLDPRQtvGDSIMEPLRV-----HGLLP--GKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
Cdd:PRK10261 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-181 |
2.10e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF-ARK 86
Cdd:COG3845 255 EVVLEVENLSVRDDrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 87 VAYLPQQlPPAEG----MTVRELVAIGRYpWHGALGRFGAADREKVEE-AISLVG----LKPLAHRLVDSLSGGERQRAW 157
Cdd:COG3845 335 VAYIPED-RLGRGlvpdMSVAENLILGRY-RRPPFSRGGFLDRKAIRAfAEELIEefdvRTPGPDTPARSLSGGNQQKVI 412
|
170 180
....*....|....*....|....
gi 15829409 158 IAMLVAQDSRCLLLDEPTSALDIA 181
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVG 436
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-238 |
2.12e-12 |
|
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: 66.89 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRV-PGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
Cdd:TIGR00957 1287 FRNYCLRYrEDLDLvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQlPPAEGMTVRElvaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAM 160
Cdd:TIGR00957 1367 QD-PVLFSGSLRM-----------NLDPFSQYSDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 161 LVAQDSRCLLLDEPTSALDIahQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAEIM--RG 238
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDL--ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV-LDKGEVAEFGAPSNLLqqRG 1511
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-180 |
5.30e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 5 TNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHqpPS----EGEILLDAQPLESWSS 80
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 81 KAFARKVAYLPQQLP---PaeGMTVRELVaigRYPWHGALGRFGAADREKVE------EAISLVGLKP-LAHRLV-DSLS 149
Cdd:CHL00131 79 EERAHLGIFLAFQYPieiP--GVSNADFL---RLAYNSKRKFQGLPELDPLEfleiinEKLKLVGMDPsFLSRNVnEGFS 153
|
170 180 190
....*....|....*....|....*....|.
gi 15829409 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-204 |
7.52e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQ------- 92
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEdrkrhgi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 --QLPPAEGMTvreLVAIGRYPWHGALGrfGAADREKVEEAISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCL 169
Cdd:TIGR02633 351 vpILGVGKNIT---LSVLKSFCFKMRID--AAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190
....*....|....*....|....*....|....*
gi 15829409 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAV 204
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVV 459
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-223 |
1.19e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.82 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 34 FPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarKVAYLPQQLppaegmtvrelvaigrypw 113
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYI------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 114 hgalgrfgaadrekveeaislvglkplahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|
gi 15829409 194 SQERGLTVIAVLHDINMAARYCDYLVALRG 223
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-204 |
1.65e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 9 DTTFALRNISFR---VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLE-SWSSKAF 83
Cdd:PRK13549 257 EVILEVRNLTAWdpvNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKiRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 84 ARKVAYLPQ---------QLPPAEGMTvreLVAIGRYPWHGALGrfGAADREKVEEAISLVGLKPLAHRL-VDSLSGGER 153
Cdd:PRK13549 337 AQGIAMVPEdrkrdgivpVMGVGKNIT---LAALDRFTGGSRID--DAAELKTILESIQRLKVKTASPELaIARLSGGNQ 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829409 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAV 204
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-204 |
2.30e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 6 NHSDTTFALRNISfrVPGrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFA 84
Cdd:PRK10762 252 APGEVRLKVDNLS--GPG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 85 RKVAYLpqqlppAE---------GMTVRE---LVAIgRYPWHGALGRFGAADREKVEEAISLVGLK-PLAHRLVDSLSGG 151
Cdd:PRK10762 327 NGIVYI------SEdrkrdglvlGMSVKEnmsLTAL-RYFSRAGGSLKHADEQQAVSDFIRLFNIKtPSMEQAIGLLSGG 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829409 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAV 204
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILV 451
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-180 |
3.52e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 28 HPL----SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdAQPLeswsskafarKVAYLPQQLPPAEGMTVR 103
Cdd:PRK11147 16 APLldnaELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDL----------IVARLQQDPPRNVEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELVAIG---------RYpwHGALGRFGAADREK-----------------------VEEAISLVGLKPlaHRLVDSLSGG 151
Cdd:PRK11147 85 DFVAEGieeqaeylkRY--HDISHLVETDPSEKnlnelaklqeqldhhnlwqlenrINEVLAQLGLDP--DAALSSLSGG 160
|
170 180
....*....|....*....|....*....
gi 15829409 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-197 |
5.68e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLP 95
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 96 PAEGMTVRELVAIGRYPWHGALGrfgaadrekVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVG---------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180
....*....|....*....|..
gi 15829409 176 SALDiahQVDVLALVHRLSQER 197
Cdd:PRK13540 156 VALD---ELSLLTIITKIQEHR 174
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-248 |
1.01e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLESwssKAFARKVAYLPQQLPPAEGMTVR 103
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLaGRKTGGYiEGDIRISGFPKKQ---ETFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 ELV---AIGRYPWHgalgrfgAADREK---VEEAISLVGLKPLAHRLV-----DSLSGGERQRAWIAM-LVAQDSrCLLL 171
Cdd:PLN03140 972 ESLiysAFLRLPKE-------VSKEEKmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVeLVANPS-IIFM 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 172 DEPTSALDIAHQVDVLALVhRLSQERGLTVIAVLH--DINMAARYCDYLVALRGGEMIAQGT----PAEIMrgETLEMIY 245
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTV-RNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGPlgrnSHKII--EYFEAIP 1120
|
...
gi 15829409 246 GIP 248
Cdd:PLN03140 1121 GVP 1123
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-190 |
1.71e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQ-PPSEGEILLDAQPLESWSSKAFARKVAYL 90
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLaGREDyEVTGGTVEFKGKDLLELSPEDRAGEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 91 PQQLP-PAEGMTVR-----ELVAIGRYPWHGALGRFGAADRekVEEAISLVGLKP-LAHRLVD-SLSGGERQRAWIAMLV 162
Cdd:PRK09580 83 AFQYPvEIPGVSNQfflqtALNAVRSYRGQEPLDRFDFQDL--MEEKIALLKMPEdLLTRSVNvGFSGGEKKRNDILQMA 160
|
170 180
....*....|....*....|....*...
gi 15829409 163 AQDSRCLLLDEPTSALDIahqvDVLALV 190
Cdd:PRK09580 161 VLEPELCILDESDSGLDI----DALKIV 184
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-180 |
2.33e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdaqpleswsskAFARKVAYLPQ-QLP--PAEGM 100
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIKLGYFAQhQLEflRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVAIG----RYPWHGALGRFGAADrEKVEEAislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
Cdd:PRK10636 394 PLQHLARLApqelEQKLRDYLGGFGFQG-DKVTEE-------------TRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
....
gi 15829409 177 ALDI 180
Cdd:PRK10636 460 HLDL 463
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
147-232 |
2.83e-10 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.17 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 147 SLSGGERQRAWIAMLVAQDS--RCL-LLDEPTSAL---DIAHQVDVLalvHRLSqERGLTVIAVLHDINMAaRYCDYLVA 220
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRStgKTLyILDEPTTGLhfhDVKKLLEVL---QRLV-DKGNTVVVIEHNLDVI-KCADWIID 243
|
90
....*....|....*...
gi 15829409 221 L------RGGEMIAQGTP 232
Cdd:cd03271 244 LgpeggdGGGQVVASGTP 261
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-236 |
8.62e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILLDAqpleswsskafarKVAYLPQqLPPAEGMTV 102
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TVAYVPQ-VSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 103 RELVAigrypwhgalgrFGAA-DREKVEEAISLVGLK------------PLAHRLVDsLSGGERQRAWIAMLVAQDSRCL 169
Cdd:PLN03130 696 RDNIL------------FGSPfDPERYERAIDVTALQhdldllpggdltEIGERGVN-ISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829409 170 LLDEPTSALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINmaarYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PLN03130 763 IFDDPLSALDahVGRQVFDKCIKDELRGKTRVLVTNQLHFLS----QVDRIILVHEGMIKEEGTYEELS 827
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-208 |
9.91e-10 |
|
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: 57.56 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRhQPPSEGEILLD-----AQPLESWsSKAFarkvAYLPQQlppa 97
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGDIQIDgvswnSVPLQKW-RKAF----GVIPQK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 98 egmtvrelVAIGRYPWHGALGRFGAADREKVEEAISLVGLK--------PLAHRLVDS---LSGGERQRAWIAMLVAQDS 166
Cdd:cd03289 86 --------VFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKsvieqfpgQLDFVLVDGgcvLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15829409 167 RCLLLDEPTSALD-IAHQVDVLALVHRLSqerGLTVIAVLHDI 208
Cdd:cd03289 158 KILLLDEPSAHLDpITYQVIRKTLKQAFA---DCTVILSEHRI 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-237 |
1.19e-09 |
|
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: 58.49 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLL--LDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDIN 209
Cdd:TIGR00630 475 VGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDNRRLINTLKRLRDLgnTLIVVEHDED 551
|
90 100 110
....*....|....*....|....*....|....
gi 15829409 210 MAaRYCDYLVAL------RGGEMIAQGTPAEIMR 237
Cdd:TIGR00630 552 TI-RAADYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-236 |
1.32e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGE--------ILLDAQPLESWSSKAFAR 85
Cdd:PRK10938 6 ISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 86 KVAYLpqqLPPAE---GMTVRELVaigrypwhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA-ML 161
Cdd:PRK10938 86 NNTDM---LSPGEddtGRTTAEII------------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCqAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 162 VAQDSrCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK10938 151 MSEPD-LLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
148-237 |
1.38e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 58.11 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 148 LSGGERQRAWIAM-LVAQDS-RCL-LLDEPTSAL---DIAHQVDVLalvHRLSqERGLTVIAVLHD---INMAarycDYL 218
Cdd:COG0178 827 LSGGEAQRVKLASeLSKRSTgKTLyILDEPTTGLhfhDIRKLLEVL---HRLV-DKGNTVVVIEHNldvIKTA----DWI 898
|
90 100
....*....|....*....|....*
gi 15829409 219 VAL------RGGEMIAQGTPAEIMR 237
Cdd:COG0178 899 IDLgpeggdGGGEIVAEGTPEEVAK 923
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-206 |
1.40e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLeswsSKAFARKVAYLPQQLPPAEGMT 101
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKP----TKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 102 VRE---LVAIGRYPwhGALGRfgaadREKV---EEAISLVGLKP-----LAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PLN03211 157 VREtlvFCSLLRLP--KSLTK-----QEKIlvaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190
....*....|....*....|....*....|....*.
gi 15829409 171 LDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLH 206
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-241 |
2.04e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRhQPPSEGeilldaqpleswSSKAFARKVAYLPQqLPPAEGMTVREL 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGE-LSHAET------------SSVVIRGSVAYVPQ-VSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 106 VAIGRYPWHGALGRfgAADREKVEEAISLVG---LKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--I 180
Cdd:PLN03232 699 ILFGSDFESERYWR--AIDVTALQHDLDLLPgrdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829409 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAarycDYLVALRGGEMIAQGTPAEIMRGETL 241
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-235 |
8.53e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPgrtllhplsltfPAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
Cdd:PTZ00243 1326 LRGVSFRIA------------PREKV-GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQD 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 94 LPPAEGmTVRELVaigrypwhgalGRFGAADREKVEEAISLVGLKplaHRL------VDS--LSGGER----QRAWIAM- 160
Cdd:PTZ00243 1393 PVLFDG-TVRQNV-----------DPFLEASSAEVWAALELVGLR---ERVasesegIDSrvLEGGSNysvgQRQLMCMa 1457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829409 161 --LVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEI 235
Cdd:PTZ00243 1458 raLLKKGSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-237 |
8.94e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 55.80 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 135 VGLKPLA-HRLVDSLSGGERQRAWIA----------MLVaqdsrcllLDEPTSALdiaHQVD---VLALVHRLsQERGLT 200
Cdd:COG0178 472 VGLDYLTlDRSAGTLSGGEAQRIRLAtqigsglvgvLYV--------LDEPSIGL---HQRDndrLIETLKRL-RDLGNT 539
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15829409 201 VIAVLHD--INMAArycDYLVAL------RGGEMIAQGTPAEIMR 237
Cdd:COG0178 540 VIVVEHDedTIRAA---DYIIDIgpgageHGGEVVAQGTPEEILK 581
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-236 |
9.97e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPPAEGMTVRELV 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 107 AigrypwhgalgrFGAADREK----VEEAISLVG---LKPLAHRLVD-----SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
Cdd:TIGR00957 720 L------------FGKALNEKyyqqVLEACALLPdleILPSGDRTEIgekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 175 TSALDiAHqVDVLALVHRLSQE---RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIM 236
Cdd:TIGR00957 788 LSAVD-AH-VGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
135-237 |
1.02e-08 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 55.46 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 135 VGLKPLA-HRLVDSLSGGERQRAWIA----------MLVaqdsrcllLDEPTSALdiaHQVDVLALVHRLSQERGL--TV 201
Cdd:PRK00349 476 VGLDYLTlSRSAGTLSGGEAQRIRLAtqigsgltgvLYV--------LDEPSIGL---HQRDNDRLIETLKHLRDLgnTL 544
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15829409 202 IAVLHD---InMAArycDYLVAL------RGGEMIAQGTPAEIMR 237
Cdd:PRK00349 545 IVVEHDedtI-RAA---DYIVDIgpgagvHGGEVVASGTPEEIMK 585
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-235 |
1.05e-08 |
|
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: 55.79 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 147 SLSGGERQRAWIAM-LVAQDS-RCL-LLDEPTSAL---DIAHQVDVLalvHRLSqERGLTVIAVLH--DINMAArycDYL 218
Cdd:TIGR00630 829 TLSGGEAQRIKLAKeLSKRSTgRTLyILDEPTTGLhfdDIKKLLEVL---QRLV-DKGNTVVVIEHnlDVIKTA---DYI 901
|
90 100
....*....|....*....|...
gi 15829409 219 VAL------RGGEMIAQGTPAEI 235
Cdd:TIGR00630 902 IDLgpeggdGGGTVVASGTPEEV 924
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-206 |
1.21e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.14 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafaRKVAYLPQ 92
Cdd:TIGR00954 454 FENIPLVTPnGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QlPPAEGMTVRELVAigrYPwHGALGRFGAADREKVEEAI-SLVGLKPLAHRLV---------DSLSGGERQRAWIAMLV 162
Cdd:TIGR00954 523 R-PYMTLGTLRDQII---YP-DSSEDMKRRGLSDKDLEQIlDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15829409 163 AQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
Cdd:TIGR00954 598 YHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-209 |
1.69e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKMLGRH-QPPSEGEILLDAqpleswsskafarkvaylpqqlppaegmtvrelvaigrypwhg 115
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 116 algrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH---- 191
Cdd:smart00382 39 ----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170
....*....|....*....
gi 15829409 192 -RLSQERGLTVIAVLHDIN 209
Cdd:smart00382 109 lLLKSEKNLTVILTTNDEK 127
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-226 |
1.77e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA-FARKVAYLP---QQ----LPPAEGMT 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSsglyLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 102 VRELVaigrypwHGALGRF--GAADREKVEEAISLVGLKpLAH--RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
Cdd:PRK15439 362 VCALT-------HNRRGFWikPARENAVLERYRRALNIK-FNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829409 178 LDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-179 |
1.89e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFarkVAYLPQ 92
Cdd:PRK13541 3 SLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-IAKPY---CTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLPPAEGMTVRELVAIGRYPWHGAlgrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
Cdd:PRK13541 78 NLGLKLEMTVFENLKFWSEIYNSA---------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
....*..
gi 15829409 173 EPTSALD 179
Cdd:PRK13541 149 EVETNLS 155
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-236 |
3.98e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqplESWSSKAFARKVAYLPQQLPPAEGMTVRELV 106
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------DRNGEVSVIAISAGLSGQLTGIENIEFKMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 107 aigrypwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
Cdd:PRK13546 113 ----------MGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829409 187 LALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIM 236
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-236 |
6.01e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 5 TNHSDTTFALRNISFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR---------------------- 59
Cdd:PTZ00265 1159 KNDIKGKIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtn 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 60 ---HQPPSE-----------------------------GEILLDAQPLESWSSKAFaRKVAYLPQQLPPAEGMTVRELVA 107
Cdd:PTZ00265 1239 eqdYQGDEEqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLFNMSIYENIK 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 108 IGRYPwhgalgrfgaADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
Cdd:PTZ00265 1318 FGKED----------ATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829409 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVAL----RGGEMI-AQGTPAEIM 236
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVqAHGTHEELL 1451
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-225 |
1.12e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL-DAQPLES-----WSSK--- 81
Cdd:PTZ00265 385 FKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDinlkwWRSKigv 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 82 ----------AFARKVAYLPQQLPPAEGMTvRELVAIGRYPWHGALGRFG-----AADREKVEEAISLVGL--------- 137
Cdd:PTZ00265 465 vsqdpllfsnSIKNNIKYSLYSLKDLEALS-NYYNEDGNDSQENKNKRNScrakcAGDLNDMSNTTDSNELiemrknyqt 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 138 -----------KPLAHRLVDS---------------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH 191
Cdd:PTZ00265 544 ikdsevvdvskKVLIHDFVSAlpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
250 260 270
....*....|....*....|....*....|....
gi 15829409 192 RLSQERGLTVIAVLHDINmAARYCDYLVALRGGE 225
Cdd:PTZ00265 624 NLKGNENRITIIIAHRLS-TIRYANTIFVLSNRE 656
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-240 |
1.22e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 126 EKVEEAISLvGLK--PLAhRLVDSLSGGERQRAWIA--MLVAQDSRCL-LLDEPTSALdiaHQVDVLALVHRLSQ--ERG 198
Cdd:PRK00635 788 EKIHALCSL-GLDylPLG-RPLSSLSGGEIQRLKLAyeLLAPSKKPTLyVLDEPTTGL---HTHDIKALIYVLQSltHQG 862
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15829409 199 LTVIAVLHDINMaARYCDYLVAL------RGGEMIAQGTPAEIMRGET 240
Cdd:PRK00635 863 HTVVIIEHNMHV-VKVADYVLELgpeggnLGGYLLASCSPEELIHLHT 909
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
148-235 |
1.42e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 52.00 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 148 LSGGERQRAWIAMLVAQDS--RCL-LLDEPTSAL---DIAHQVDVLalvHRLSqERGLTVIAVLHDINMAaRYCDYLVAL 221
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLhfeDIRKLLEVL---HRLV-DKGNTVVVIEHNLDVI-KTADWIIDL 905
|
90 100
....*....|....*....|
gi 15829409 222 ------RGGEMIAQGTPAEI 235
Cdd:PRK00349 906 gpeggdGGGEIVATGTPEEV 925
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-239 |
1.46e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 27 LHPLSLT-FPAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPPAEGMTVRel 105
Cdd:PLN03130 1255 LHGLSFEiSPSEKV-GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-PVLFSGTVR-- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 106 VAIGRYPWHGALGRFGAADREKVEEAI--SLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahq 183
Cdd:PLN03130 1331 FNLDPFNEHNDADLWESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD---- 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829409 184 VDVLALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEIMRGE 239
Cdd:PLN03130 1407 VRTDALIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-231 |
1.98e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPPAEGMTVRELVAIgrypwHGA 116
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-QNMGYCPQFDAIDDLLTGREHLYL-----YAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 117 LGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
Cdd:TIGR01257 2039 LRGVPAEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170 180 190
....*....|....*....|....*....|....*.
gi 15829409 196 ErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
Cdd:TIGR01257 2119 E-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-193 |
2.20e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 13 ALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswSSKAFARKVAYLpQ 92
Cdd:PRK13543 13 AAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYL-G 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 93 QLP--PAEGMTVRELvaigrypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
Cdd:PRK13543 89 HLPglKADLSTLENL--------HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180
....*....|....*....|...
gi 15829409 171 LDEPTSALDIahqvDVLALVHRL 193
Cdd:PRK13543 161 LDEPYANLDL----EGITLVNRM 179
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-214 |
2.97e-07 |
|
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: 48.90 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGrhqppsegeilldaqpleswsskafarkvaylpqqlppaegmtvr 103
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 104 eLVAIGRYPwhgALGRFGAADREKVEEAISLVglkplAHRLVDSLSGGERQRAWIAMLVA----QDSRCLLLDEPTSALD 179
Cdd:cd03227 43 -LALGGAQS---ATRRRSGVKAGCIVAAVSAE-----LIFTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD 113
|
170 180 190
....*....|....*....|....*....|....*
gi 15829409 180 IAHQVDVLALVHRLSQErGLTVIAVLHDINMAARY 214
Cdd:cd03227 114 PRDGQALAEAILEHLVK-GAQVIVITHLPELAELA 147
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-235 |
4.05e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 12 FALRNISFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsSKAFARKVAYLP 91
Cdd:PRK13545 38 YALNNISFEVP-------------EGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 92 QQLPPAEGMTVRELVaigrypwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
Cdd:PRK13545 98 GQLTGIENIELKGLM----------MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 172 DEptsALDIAHQVDVLALVHRLSQ--ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEI 235
Cdd:PRK13545 168 DE---ALSVGDQTFTKKCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
30-230 |
6.07e-07 |
|
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: 48.47 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 30 LSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqppsEGEILLDAQPLESWSSKAFARKVAYLPQqlppaegmtVRELVAIG 109
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ---------LQFLIDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 110 rypwhgalgrfgaadrekveeaislVGLKPLAhRLVDSLSGGERQRAWIAMLVAQDSR--CLLLDEPTSALdiaHQVDVL 187
Cdd:cd03238 76 -------------------------LGYLTLG-QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL---HQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829409 188 ALvhrLSQERGL-----TVIAVLHDINMaARYCDYLVAL------RGGEMIAQG 230
Cdd:cd03238 127 QL---LEVIKGLidlgnTVILIEHNLDV-LSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
135-230 |
1.72e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQ--DSRCLLLDEPTSALdiaHQVDVLALVHRLSQER--GLTVIAVLHDIN 209
Cdd:cd03270 124 VGLGYLTlSRSAPTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGL---HPRDNDRLIETLKRLRdlGNTVLVVEHDED 200
|
90 100
....*....|....*....|....*..
gi 15829409 210 MaARYCDYLVAL------RGGEMIAQG 230
Cdd:cd03270 201 T-IRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-207 |
9.22e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 16 NISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP--------------------- 74
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErlgklrqdqfafeeftvldtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 75 ----LESWSSKAfARKVAYLPQQLPPAEGMTVREL-VAIGRYPWHGALGRFGaadrekveEAISLVGLKPLAHR-LVDSL 148
Cdd:PRK15064 86 imghTELWEVKQ-ERDRIYALPEMSEEDGMKVADLeVKFAEMDGYTAEARAG--------ELLLGVGIPEEQHYgLMSEV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829409 149 SGGERQRawiaMLVAQ----DSRCLLLDEPTSALDIaHQVDVLALVhrLSQeRGLTVIAVLHD 207
Cdd:PRK15064 157 APGWKLR----VLLAQalfsNPDILLLDEPTNNLDI-NTIRWLEDV--LNE-RNSTMIIISHD 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-180 |
1.20e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsEGEILLDAQPL---ESWSskafarkVAYLPQQlPPAEGM 100
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYtfpGNWQ-------LAWVNQE-TPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 101 TVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLK--------------PLAHRL----------VDSLSGGERQRA 156
Cdd:PRK10636 79 PALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKldaidawtirsraaSLLHGLgfsneqlerpVSDFSGGWRMRL 158
|
170 180
....*....|....*....|....
gi 15829409 157 WIAMLVAQDSRCLLLDEPTSALDI 180
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDL 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-184 |
2.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 14 LRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP---PSEGEILLDAQPLESWSSKAFA------ 84
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQILHVEQEVVGDDTTALQcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 85 -------RKVAYLPQQLPPAEGMTVRelvAIGRYPWHGALGRFGAADR----EKVEEAIS-----------LVGLK---P 139
Cdd:PLN03073 260 iertqllEEEAQLVAQQRELEFETET---GKGKGANKDGVDKDAVSQRleeiYKRLELIDaytaearaasiLAGLSftpE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15829409 140 LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQV 184
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAV 380
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-207 |
3.20e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 39 VTGLIGHNGSGKSTL---LKM-LGRHQPPSEGEILLDAQPLESWSSKAfarkVAYLPQQLPPAEGMTVRELVAIGRYpwh 114
Cdd:cd03240 24 LTLIVGQNGAGKTTIieaLKYaLTGELPPNSKGGAHDPKLIREGEVRA----QVKLAFENANGKKYTITRSLAILEN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 115 galgrfgaADREKVEEAislvgLKPLAhRLVDSLSGGERQ------RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
Cdd:cd03240 97 --------VIFCHQGES-----NWPLL-DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLA 162
|
170 180
....*....|....*....|
gi 15829409 189 -LVHRLSQERGLTVIAVLHD 207
Cdd:cd03240 163 eIIEERKSQKNFQLIVITHD 182
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-236 |
1.37e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 143 RLVDSLSGGERQRAWIAM-LVAQDSRCL-LLDEPTSALdiaHQVDVLALVHRLSQER--GLTVIAVLHDINMAArYCDYL 218
Cdd:PRK00635 472 RALATLSGGEQERTALAKhLGAELIGITyILDEPSIGL---HPQDTHKLINVIKKLRdqGNTVLLVEHDEQMIS-LADRI 547
|
90 100
....*....|....*....|....
gi 15829409 219 V------ALRGGEMIAQGTPAEIM 236
Cdd:PRK00635 548 IdigpgaGIFGGEVLFNGSPREFL 571
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-243 |
9.67e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829409 125 REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAV 204
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLT 200
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15829409 205 LHDINMAARYCDYLVALRGGEMIAQGTPAEI---MRGETLEM 243
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRGRVIADGKVDELktkVGGRTLQI 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-203 |
4.59e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 4.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829409 139 PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE-RGLTVIA 203
Cdd:PRK10982 383 PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIIS 448
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
10-54 |
5.55e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 5.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15829409 10 TTFALRNI-SFRvpgrtllhplSLTFPAGKVTGLIGHNGSGKSTLL 54
Cdd:COG4637 3 TRIRIKNFkSLR----------DLELPLGPLTVLIGANGSGKSNLL 38
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
27-54 |
9.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.67 E-value: 9.87e-03
10 20
....*....|....*....|....*...
gi 15829409 27 LHPLSLTFPagkVTGLIGHNGSGKSTLL 54
Cdd:COG3910 30 LEGLEFHPP---VTFFVGENGSGKSTLL 54
|
|
| |
