|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-255 |
7.60e-145 |
|
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: 405.97 E-value: 7.60e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQI 243
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|..
gi 983475024 244 VPCPVNCKPICL 255
Cdd:COG1120 242 IEDPVTGRPLVL 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-255 |
3.15e-117 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 336.22 E-value: 3.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAIL 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQ 242
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|...
gi 983475024 243 IVPCPVNCKPICL 255
Cdd:PRK11231 241 IHPEPVSGTPMCV 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-258 |
2.02e-111 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 321.26 E-value: 2.02e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQT 85
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 AEVPTGLTVFELVSYGRFPHQKGfgTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDE 165
Cdd:COG4604 84 NHINSRLTVRELVAFGRFPYSKG--RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 166 PTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQIvp 245
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV-- 239
|
250
....*....|...
gi 983475024 246 CPVNCKPICLTYD 258
Cdd:COG4604 240 EEIDGKRICVYFR 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
4.23e-91 |
|
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: 266.99 E-value: 4.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 5 AVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 taevptgltvfelvsygrfphqkgfgtlkeedyryihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 165 EPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-253 |
2.50e-89 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 265.70 E-value: 2.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:PRK10253 86 LAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEA 241
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRC 245
|
250
....*....|..
gi 983475024 242 QIVPCPVNCKPI 253
Cdd:PRK10253 246 MIIDDPVAGTPL 257
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
1.00e-80 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 243.07 E-value: 1.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeiaKKMA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTG--LTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGT 158
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALkAGKLMKQGTPDEVMTSETLRSVF 237
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAY 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-252 |
6.53e-80 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 241.56 E-value: 6.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYGRFPHqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQ------- 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSV 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250
....*....|....*.
gi 983475024 237 FEIEAQIVPCPVNCKP 252
Cdd:COG4559 237 YGADLRVLAHPEGGCP 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-257 |
3.55e-76 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 232.37 E-value: 3.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEA 241
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
250
....*....|....*.
gi 983475024 242 QIVPCPVNCKPICLTY 257
Cdd:PRK10575 250 GILPHPAGAAPVSFVY 265
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-247 |
2.28e-73 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 225.04 E-value: 2.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYGRFPHqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE-- 159
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 160 ----LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRS 235
Cdd:PRK13548 157 gpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
250
....*....|..
gi 983475024 236 VFEIEAQIVPCP 247
Cdd:PRK13548 237 VYGADVLVQPHP 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-219 |
2.77e-71 |
|
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: 218.17 E-value: 2.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeiaKKMAILPQT 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 AEVPTG--LTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03235 77 RSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLM 219
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-235 |
6.00e-68 |
|
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: 209.88 E-value: 6.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAIL 82
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAE---VptGLTVFELVSYGrfPHQKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:COG1122 81 FQNPDdqlF--APTVEEDVAFG--PENLGLP--REEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT-SETLRS 235
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSdYELLEE 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-252 |
1.98e-64 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 206.62 E-value: 1.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIE 240
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDAR 239
|
250
....*....|..
gi 983475024 241 AQIVPCPVNCKP 252
Cdd:PRK09536 240 TAVGTDPATGAP 251
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-237 |
2.51e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 196.05 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtKEIAKKMAILP 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYgrfpHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:COG1131 80 QEPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMtSETLRSVF 237
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-242 |
2.93e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.05 E-value: 2.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK---KM 79
Cdd:COG3638 3 LELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVSYGRFPH----QKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 156 QGTELLVLDEPTTYLD--MAHQleVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVmTSETL 233
Cdd:COG3638 163 QEPKLILADEPVASLDpkTARQ--VMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVL 239
|
....*....
gi 983475024 234 RSVFEIEAQ 242
Cdd:COG3638 240 REIYGGEAE 248
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
2.40e-61 |
|
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: 192.68 E-value: 2.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVP-TGLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:cd03225 82 QNPDDQfFGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-237 |
8.60e-58 |
|
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: 184.69 E-value: 8.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL-IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA---KKM 79
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVSYGRFPH----QKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVmTSETLRS 235
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDE 239
|
..
gi 983475024 236 VF 237
Cdd:cd03256 240 IY 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-230 |
7.45e-54 |
|
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: 182.03 E-value: 7.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG-----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQP---TKEI 75
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 AKKMAILPQTaevPTG-----LTVFELVSYGrfPHQKGFGTlKEEDYRYIHWALEVTGM-TEFANRPAEALSGGQRQRVW 149
Cdd:COG1123 341 RRRVQMVFQD---PYSslnprMTVGDIIAEP--LRLHGLLS-RAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
.
gi 983475024 230 S 230
Cdd:COG1123 495 N 495
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
1.27e-53 |
|
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: 173.78 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-MAIL 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVSYGRFPHQKGFGTL------KEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQ 156
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-235 |
8.21e-52 |
|
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: 169.92 E-value: 8.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG-KAIEKQPTKEIAKKMAIL 82
Cdd:TIGR04520 3 VENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAE---VptGLTVFELVSYGrfPHQKGFGTlkEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:TIGR04520 83 FQNPDnqfV--GATVEDDVAFG--LENLGVPR--EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMT-SETLRS 235
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSqVELLKE 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-244 |
1.49e-51 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 168.87 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 21 GLTVEIPEGKITTIIGPNGCGKSTLLktaSRI--LKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGLTVFELV 98
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLL---ARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYgrfpHQKGfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQ-------GTELLVLDEPTTYLD 171
Cdd:COG4138 91 AL----HQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 172 MAHQLEVLNLLKKLNEEeGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQIV 244
Cdd:COG4138 166 VAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRL 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-231 |
7.55e-51 |
|
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: 166.52 E-value: 7.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE---IAKKMAIL 82
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVSYGRFPHqkgfGTLKEEDYRYI--HWaLEVTGMTEFAN-RPAEaLSGGQRQRVWIAMALAQGTE 159
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREH----TRLSEEEIREIvlEK-LEAVGLRGAEDlYPAE-LSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-236 |
7.70e-51 |
|
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: 167.63 E-value: 7.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEG-----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI---EKQPTKEIAK 77
Cdd:TIGR04521 3 LKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 78 KMAILPQTAEvpTGL---TVFELVSYGrfPhqKGFGTLKEEDYRYIHWALEVTGMTE-FANRPAEALSGGQRQRVWIAMA 153
Cdd:TIGR04521 83 KVGLVFQFPE--HQLfeeTVYKDIAFG--P--KNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 154 LAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV-MTSET 232
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVfSDVDE 236
|
....
gi 983475024 233 LRSV 236
Cdd:TIGR04521 237 LEKI 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-213 |
1.54e-50 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 164.33 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 12 GYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVyldgkaiekqpTKEIAKKMAILPQTAEVPTG 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 L--TVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:NF040873 70 LplTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 983475024 170 LDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRfSDHMIAL 213
Cdd:NF040873 150 LDAESRERIIALLAEEH-ARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-237 |
3.20e-50 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 165.16 E-value: 3.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK---KM 79
Cdd:TIGR02315 2 LEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVSYGRFPH----QKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYkptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVmTSETLRS 235
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVLRH 240
|
..
gi 983475024 236 VF 237
Cdd:TIGR02315 241 IY 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-238 |
4.29e-50 |
|
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: 164.98 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL----IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKM 79
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQ--TAEVPTGLTVFELVS-----YGRFPHQkgfgtlkeedyRYIHWALEVTGMT-EFANR-PAEaLSGGQRQRVWI 150
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAeplriHGLPDRE-----------ERIAELLEQVGLPpSFLDRyPHQ-LSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLmkqgtpDEVMTS 230
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI------VEELTV 223
|
....*...
gi 983475024 231 ETLRSVFE 238
Cdd:COG1124 224 ADLLAGPK 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-218 |
8.61e-50 |
|
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: 163.43 E-value: 8.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA--- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 -KKMAILPQTAEVPTGLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFsDHMIALKAGKL 218
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-222 |
1.74e-49 |
|
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: 162.68 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL----IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEK---QPTKEIA 76
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 KKMAILPQ--TAEVPTGLTVFELVSYGRFPHQKGFGtlKEEDYRYIHWALEVTGMTE-FANR-PAEaLSGGQRQRVWIAM 152
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSK--KEARKEAVLLLLVGVGLPEeVLNRyPHE-LSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 153 ALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-237 |
4.18e-49 |
|
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: 162.33 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtKEIAKKMAILPQTAEVPTGL 92
Cdd:COG4555 11 YGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 93 TVFELVSYgrfphqkgFGTLKEEDYRYIHWA----LEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTT 168
Cdd:COG4555 90 TVRENIRY--------FAELYGLFDEELKKRieelIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 169 YLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM---TSETLRSVF 237
Cdd:COG4555 162 GLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeiGEENLEDAF 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-231 |
6.62e-49 |
|
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: 161.69 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE---IAKKMAIL 82
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVSygrFPHQKgFGTLKEEDYRYI-HWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTEL 160
Cdd:COG1127 88 FQGGALFDSLTVFENVA---FPLRE-HTDLSEAEIRELvLEKLELVGLPGAADKmPSE-LSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 161 LVLDEPTTYLD--MAhqLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:COG1127 163 LLYDEPTAGLDpiTS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-234 |
7.03e-49 |
|
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: 161.30 E-value: 7.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-M 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFE---LVSYGRfphqkgfgtlkeEDYRYIHWALE-VTGM----TEFANRPAEALSGGQRQRVWIA 151
Cdd:COG0410 81 GYVPEGRRIFPSLTVEEnllLGAYAR------------RDRAEVRADLErVYELfprlKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 152 MALAQGTELLVLDEPTtyLDMAHQL--EVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:COG0410 149 RALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
....*
gi 983475024 230 SETLR 234
Cdd:COG0410 226 DPEVR 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-218 |
2.19e-48 |
|
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: 157.94 E-value: 2.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtKEIAKKMAILP 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYgrfphqkgfgtlkeedyryihwalevtgmtefanrpaealSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03230 80 EEPSLYENLTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
2.46e-48 |
|
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: 167.39 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MAT-LAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAK---KGTVYLDGKAIEKQPTKE 74
Cdd:COG1123 1 MTPlLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 75 IAKKMAILPQTAEVP-TGLTVFELVSYGRfphqKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMA 153
Cdd:COG1123 81 RGRRIGMVFQDPMTQlNPVTVGDQIAEAL----ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 154 LAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
5.07e-48 |
|
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: 159.82 E-value: 5.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSV--GyneGL-IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK 77
Cdd:COG0411 2 DPLLEVRGLTKrfG---GLvAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 78 K-MAILPQTAEVPTGLTVFELVSYGRFPHQKG---------FGTLKEED--YRYIHWALEVTGMTEFANRPAEALSGGQR 145
Cdd:COG0411 79 LgIARTFQNPRLFPELTVLENVLVAAHARLGRgllaallrlPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 146 QRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPD 225
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
....*.
gi 983475024 226 EVMTSE 231
Cdd:COG0411 239 EVRADP 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-228 |
1.47e-47 |
|
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: 157.60 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-MAIL 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFE---LVSYGRFPHQkgfgtlkeedyryIHWALE-VTGM----TEFANRPAEALSGGQRQRVWIAMAL 154
Cdd:cd03224 81 PEGRRIFPELTVEEnllLGAYARRRAK-------------RKARLErVYELfprlKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 155 AQGTELLVLDEPTTYLdmAHQL--EVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:cd03224 148 MSRPKLLLLDEPSEGL--APKIveEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-227 |
2.17e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 157.34 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKK-----GTVYLDGKAIEKQPTKEIA-- 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 KKMAILPQTAeVPTGLTVFELVSYGRFPHqkGFGTLKEEDYRyIHWALEVTGMTEFANRPAEA--LSGGQRQRVWIAMAL 154
Cdd:cd03260 81 RRVGMVFQKP-NPFPGSIYDNVAYGLRLH--GIKLKEELDER-VEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 155 AQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-217 |
1.64e-46 |
|
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: 152.78 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQtaev 88
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 ptgltvfelvsygrfphqkgfgtlkeedyryihwalevtgmtefanrpaeaLSGGQRQRVWIAMALAQGTELLVLDEPTT 168
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 983475024 169 YLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:cd00267 110 GLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
4.37e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 4.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MAT-LAVDAVSVGYNEGL----IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEI 75
Cdd:COG1136 1 MSPlLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 AK----KMAILPQTAE-VPTgLTVFELVsygRFPHQKGfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWI 150
Cdd:COG1136 81 ARlrrrHIGFVFQFFNlLPE-LTALENV---ALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFsDHMIALKAGKL 218
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRI 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
7.08e-46 |
|
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: 153.06 E-value: 7.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAILP 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-244 |
1.32e-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: 151.01 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASR-ILKAKKGTVYLDGKAIEKQPTKEIAKKMAIL 82
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 -PQTAE-VPTGLTVFELV------SYGRFPHqkgfgtLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMAL 154
Cdd:COG1119 84 sPALQLrFPRDETVLDVVlsgffdSIGLYRE------PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 155 AQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLR 234
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLS 237
|
250
....*....|
gi 983475024 235 SVFEIEAQIV 244
Cdd:COG1119 238 EAFGLPVEVE 247
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
1.91e-44 |
|
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: 148.10 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqptkeiakkMAILP 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD---------LEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLtVFElvSYGRFPHqkgfgtlkeedyryihwalevtgMTEFANRpAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03229 72 PPLRRRIGM-VFQ--DFALFPH-----------------------LTVLENI-ALGLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-253 |
2.71e-44 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 150.75 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAK--------KGTVYLDGKAIEKQPTKEI 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 AKKMAILPQTAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 156 Q---------GTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260
....*....|....*....|....*..
gi 983475024 227 VMTSETLRSVFEIEAQIVPCPVNCKPI 253
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGVPPV 268
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-227 |
6.46e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.17 E-value: 6.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeiakkma 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ilPQtaEVPTG-----------LTVFELVSYGrfPHQKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVW 149
Cdd:COG3842 74 --PE--KRNVGmvfqdyalfphLTVAENVAFG--LRMRGVP--KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-226 |
1.63e-42 |
|
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: 144.57 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 17 LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtKEIAKKMAILPQTAEVPTGLTVFE 96
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 -LVSYGRFphqKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:cd03263 95 hLRFYARL---KGLP--KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 983475024 176 LEVLNLLKKlnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:cd03263 170 RAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-230 |
1.78e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 145.14 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQtae 87
Cdd:cd03295 6 VTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 vptgltvfelvSYGRFPH---QKGFGT----LKEEDYRYIHWALEVTGM-----TEFANR-PAEaLSGGQRQRVWIAMAL 154
Cdd:cd03295 83 -----------QIGLFPHmtvEENIALvpklLKWPKEKIRERADELLALvgldpAEFADRyPHE-LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 155 AQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
2.13e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.80 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGlTVFELVSYGRFPHQKGFGTLKEEDyryihwALEVTGMTE-FANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALE------LLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-245 |
4.81e-42 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 144.31 E-value: 4.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKkGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGLTVFELVSYg 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 rfpHQkGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQ-------GTELLVLDEPTTYLDMAH 174
Cdd:PRK03695 93 ---HQ-PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 175 QLEVLNLLKKLNEEeGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQIVP 245
Cdd:PRK03695 169 QAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-199 |
1.95e-41 |
|
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: 141.46 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTkEIAKKMAI 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYgrfpHQKGFGTLKEEDyrYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHD 199
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHL-ARGGAVLLTTHQ 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-222 |
3.32e-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: 140.79 E-value: 3.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGkITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKeIAKKMAILP 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYgrfphqkgFGTLKE----EDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:cd03264 79 QEFGVYPNFTVREFLDY--------IAWLKGipskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
3.69e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.83 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE--IAkk 78
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrnIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 M-----AILPQtaevptgLTVFELVSYG----RFPhqkgfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVW 149
Cdd:COG3839 79 MvfqsyALYPH-------MTVYENIAFPlklrKVP--------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMA--HQLEVlnLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKlrVEMRA--EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
1.70e-40 |
|
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: 139.53 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGkaiekQPTKEIAKKM 79
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVSYGRfphqKGFGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGT 158
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAyPHQ-LSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKA 215
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-227 |
2.25e-40 |
|
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: 139.29 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI-----EKQPTKEIAKK 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlppHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAILPQtaevptgLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGT 158
Cdd:cd03300 81 YALFPH-------LTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
3.16e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEkQPTKEIA 76
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-GPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 kkM-----AILPQtaevptgLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWI 150
Cdd:COG1116 84 --VvfqepALLPW-------LTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAyPHQ-LSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 151 AMALAQGTELLVLDEPTTYLD--MAHQLEvlNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAG 216
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDalTRERLQ--DELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
7-231 |
3.57e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 139.89 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 7 DAVSVGYN--EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQ 84
Cdd:PRK13648 11 KNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVP-TGLTVFELVSYG----RFPHqkgfgtlkEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:PRK13648 91 NPDNQfVGSIVKYDVAFGlenhAVPY--------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
3.90e-40 |
|
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: 146.06 E-value: 3.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:COG4988 335 PSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTGlTVFELVSYGRfPHqkgfgtLKEEDyryIHWALEVTGMTEFANR-P----------AEALSGGQRQRVW 149
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGR-PD------ASDEE---LEAALEAAGLDEFVAAlPdgldtplgegGRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLnHASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 983475024 230 SE 231
Cdd:COG4988 561 KN 562
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-226 |
4.55e-40 |
|
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: 138.27 E-value: 4.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTkEIAKKMAILPQTAEVPTGL 92
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 93 TVFE-LVSYGRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:cd03265 89 TGWEnLYIHARL-----YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 172 MAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
7.53e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 7.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:PRK13632 10 VENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTaevP----TGLTVFELVSYG----RFPhqkgfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK13632 90 QN---PdnqfIGATVEDDIAFGlenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-228 |
8.00e-39 |
|
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: 143.44 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGlTVFELVSYGRfphqkgfGTLKEEDyryIHWALEVTGMTEFANR-P----------AEALSGGQRQRVWI 150
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGD-------PDATDEE---IIEAARLAGLHDFIEAlPmgydtvvgegGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNHAsRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-244 |
8.34e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.79 E-value: 8.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTA--EVPTGlTVFE 96
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSS-TVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 LVSYGrfPHQKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQL 176
Cdd:PRK13647 100 DVAFG--PVNMGLD--KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 177 EVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPdEVMTSETLRSVFEIEAQIV 244
Cdd:PRK13647 176 TLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRLPLV 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-227 |
8.92e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.68 E-value: 8.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTaevP----TGLTVFELVSYGRFPHqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQG 157
Cdd:PRK13635 86 VFQN---PdnqfVGATVQDDVAFGLENI----GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 158 TELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
1.50e-38 |
|
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: 137.11 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLI--IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAK---KGTVYLDGKAIEKQPTKEI- 75
Cdd:COG0444 2 LEVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 ---AKKMAILPQ---TAEVPTgLTVFELVSYGRFPHQKGfgtLKEEDYRYIHWALEVTGMT---EFANR-PAEaLSGGQR 145
Cdd:COG0444 82 kirGREIQMIFQdpmTSLNPV-MTVGDQIAEPLRIHGGL---SKAEARERAIELLERVGLPdpeRRLDRyPHE-LSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 146 QRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPD 225
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
..
gi 983475024 226 EV 227
Cdd:COG0444 237 EL 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
2.07e-38 |
|
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: 132.51 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAevptglTVFElvsygrfphqkgfGTLKEEdyryIhwalevtgmtefanrpaeaLSGGQRQRVWIAMALAQGTELL 161
Cdd:cd03228 81 VPQDP------FLFS-------------GTIREN----I-------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLneEEGRTIVMVIHDLNHASRFsDHMIALKAGK 217
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-231 |
2.09e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.50 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 23 TVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeIAK-KMAILPQTAEVPTGLTVFELVSYG 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP---PAErPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 RFPHQKgfgtLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNL 181
Cdd:COG3840 96 LRPGLK----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 983475024 182 LKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
3.76e-38 |
|
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: 140.67 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKM 79
Cdd:COG4987 332 PSLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGlTVFELVSYGRfphqkgfGTLKEEDyryIHWALEVTGMTEFANRP-----------AEALSGGQRQRV 148
Cdd:COG4987 412 AVVPQRPHLFDT-TLRENLRLAR-------PDATDEE---LWAALERVGLGDWLAALpdgldtwlgegGRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLD--MAHQLevLNLLKKLneEEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQGTPDE 226
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDaaTEQAL--LADLLEA--LAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
..
gi 983475024 227 VM 228
Cdd:COG4987 556 LL 557
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-235 |
5.48e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.43 E-value: 5.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI--EKQPTKEIAKKMAILPQTAE-- 87
Cdd:PRK13639 11 YPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPDdq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 --VPTgltVFELVSYGrfPHQKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDE 165
Cdd:PRK13639 91 lfAPT---VEEDVAFG--PLNLGLS--KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 166 PTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT-SETLRS 235
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdIETIRK 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-229 |
6.87e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 133.50 E-value: 6.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRIL----KAK-KGTVYLDGKAIEKQPTKEI 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypEARvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 AKKMAILPQTAEVPTGLTVFELVSYGrfPHQKGFGTLKEEDYRYIHWALEVTGM-TEFANR---PAEALSGGQRQRVWIA 151
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 152 MALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-218 |
2.13e-37 |
|
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: 130.84 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIekqPTKEIAKKMAILPQ 84
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVP-TGLTVFELVSYGRfphqkgfgTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03226 79 DVDYQlFTDSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
2.63e-37 |
|
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: 128.92 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGLTVFELV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 99 SYGRfphqKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEA----LSGGQRQRVWIAMALAQGTELLVLDEPTT 168
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-218 |
9.28e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 9.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK---KMAILPQ 84
Cdd:COG2884 7 VSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVPTGLTVFELVSygrFPhQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:COG2884 87 DFRLLPDRTVYENVA---LP-LRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 165 EPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-227 |
9.80e-37 |
|
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: 130.15 E-value: 9.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEgLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAILP 83
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYGrFPHQKgfgTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03299 78 QNYALFPHMTVYKNIAYG-LKKRK---VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-228 |
1.56e-36 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 133.05 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 25 EIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA----KKMAILPQTAEVPTGLTVFELVSY 100
Cdd:TIGR01186 15 AIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELRevrrKKIGMVFQQFALFPHMTILQNTSL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 101 GrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLN 180
Cdd:TIGR01186 95 G----PELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 983475024 181 LLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:TIGR01186 171 ELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEIL 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-236 |
1.58e-36 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 129.57 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-MAIL 82
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVsygrfphQKGFGTLKEEDYRYIHWALE---VtgMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:TIGR03410 81 PQGREIFPRLTVEENL-------LTGLAALPRRSRKIPDEIYElfpV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSV 236
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-203 |
3.07e-36 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 127.54 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE--KQPTKEIAKKMAILPQTAEVPT- 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysRKGLLERRQRVGLVFQDPDDQLf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 GLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL 170
Cdd:TIGR01166 83 AADVDQDVAFG----PLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|...
gi 983475024 171 DMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHA 203
Cdd:TIGR01166 159 DPAGREQMLAILRRLR-AEGMTVVISTHDVDLA 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-230 |
4.03e-36 |
|
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: 129.30 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 25 EIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEI----AKKM-------AILPQtaevptgLT 93
Cdd:cd03294 46 DVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKIsmvfqsfALLPH-------RT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVSYG---RfphqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL 170
Cdd:cd03294 119 VLENVAFGlevQ-------GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 171 DMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-227 |
8.47e-36 |
|
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: 127.84 E-value: 8.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAILPQTAEVPTGLTVFELV 98
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEV 178
Cdd:cd03296 96 AFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 983475024 179 LNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:cd03296 176 RRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
1.33e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.43 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE--KQPTKEIAKKMAILPQTAEVPT-GLTVF 95
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVGMVFQDPDNQLfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFphqkGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:PRK13636 102 QDVSFGAV----NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 176 LEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS-ETLRSV 236
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEkEMLRKV 239
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-240 |
4.86e-35 |
|
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: 125.35 E-value: 4.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 24 VEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqPTKEIAKKMAILPQTAEV----PtgLTVFELVS 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRHEFawdfP--ISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 100 YGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVL 179
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 180 NLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKaGKLMKQGTPDEVMTSETLRSVFEIE 240
Cdd:TIGR03771 154 ELFIEL-AGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-227 |
6.13e-35 |
|
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: 125.39 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 12 GYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE---IAKKMAILPQTAEV 88
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkARRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 PTGLTVFELVSYgrfPHQKGfGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:cd03258 94 LSSRTVFENVAL---PLEIA-GVPKAEIEERVLELLELVGLEDKADAyPAQ-LSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 168 TYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:cd03258 169 SALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
1.09e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.29 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 15 EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI--EKQPT--KEIAKKMAILPQTAEvpT 90
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItaGKKNKklKPLRKKVGIVFQFPE--H 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 GL---TVFELVSYGrfPhqKGFGTLKEEDYRYIHWALEVTGMTE--FANRPAEaLSGGQRQRVWIAMALAQGTELLVLDE 165
Cdd:PRK13634 97 QLfeeTVEKDICFG--P--MNFGVSEEDAKQKAREMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 166 PTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-237 |
2.33e-34 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 125.00 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVyldgkAIEKQPTKEIAKK-- 78
Cdd:PRK15056 5 AGIVVNDVTVTWRNGhTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAILPQTAEVPTGLTVF--ELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQ 156
Cdd:PRK15056 80 VAYVPQSEEVDWSFPVLveDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKaGKLMKQGTPDEVMTSETLRSV 236
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELA 237
|
.
gi 983475024 237 F 237
Cdd:PRK15056 238 F 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-233 |
2.03e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.60 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRIL---KAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:PRK13640 8 FKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVP-TGLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:PRK13640 88 IVFQNPDNQfVGATVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-230 |
3.68e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 120.87 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEkQPTKEIAK---KMA 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKlrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 IlpqtaevptgltVFElvSYGRFPH-----------QKGFGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRV 148
Cdd:COG1126 81 M------------VFQ--QFNLFPHltvlenvtlapIKVKKMSKAEAEERAMELLERVGLADKADAyPAQ-LSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLD--MAHqlEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDpeLVG--EVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
....
gi 983475024 227 VMTS 230
Cdd:COG1126 223 FFEN 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-222 |
1.11e-32 |
|
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: 118.75 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAILPQTAEVPTGLTVFELVSYG 101
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 RFPHQKgfgtLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNL 181
Cdd:cd03298 95 LSPGLK----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 983475024 182 LKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-230 |
1.75e-32 |
|
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: 121.76 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 25 EIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG-------KAIEKQPTKeiaKKMAILPQTAEVPTGLTVFEL 97
Cdd:TIGR02142 19 TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRfphqkgfgTLKEEDYRYIHWA--LEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:TIGR02142 96 LRYGM--------KRARPSERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 176 LEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-218 |
2.15e-32 |
|
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: 118.02 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTK--EIAKKMAIlpqta 86
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 87 evptgltVFElvSYGRFPH-----------QKGFGTLKEEDYRYIHWALEVTGMTEFAN-RPAEaLSGGQRQRVWIAMAL 154
Cdd:cd03262 81 -------VFQ--QFNLFPHltvlenitlapIKVKGMSKAEAEERALELLEKVGLADKADaYPAQ-LSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 155 AQGTELLVLDEPTTYLD--MAHqlEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03262 151 AMNPKVMLFDEPTSALDpeLVG--EVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-227 |
2.34e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.81 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG-KAIEKQPTKEIAKKMAILPQTAE---VP 89
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKAGMVFQNPDnqiVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 90 TglTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:PRK13633 101 T--IVEEDVAFG----PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 170 LDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-227 |
6.31e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.25 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGK-AIEKQPTKEiaKKMAILPQT-AEVPTgLTVFEL 97
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPPRE--RRVGFVFQHyALFPH-MTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGrFPHQKGFGTLKEEdyRYIHWaLEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDmAH-- 174
Cdd:COG1118 96 IAFG-LRVRPPSKAEIRA--RVEEL-LELVQLEGLADRyPSQ-LSGGQRQRVALARALAVEPEVLLLDEPFGALD-AKvr 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 175 -QLEVlnLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG1118 170 kELRR--WLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-230 |
7.05e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.83 E-value: 7.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRIL----KAK-KGTVYLDGKAI--EKQPTKEIA 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipGARvEGEILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 KKMAILPQTaevPTGL--TVFELVSYGrfPHQKGFGTLKEEDYRyIHWAL-------EVtgmtefANR---PAEALSGGQ 144
Cdd:COG1117 92 RRVGMVFQK---PNPFpkSIYDNVAYG--LRLHGIKSKSELDEI-VEESLrkaalwdEV------KDRlkkSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 145 RQRVWIAMALAQGTELLVLDEPTTYLD--MAHQLEvlNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
....*...
gi 983475024 223 TPDEVMTS 230
Cdd:COG1117 236 PTEQIFTN 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-236 |
7.68e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.61 E-value: 7.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEGL-----IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTK--EIAKKMAILPQT 85
Cdd:PRK13637 12 YMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 AEVPT-GLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMT--EFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:PRK13637 92 PEYQLfEETIEKDIAFG----PINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS-ETLRSV 236
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESI 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-222 |
1.07e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 116.20 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAILPQTAEVPTGL 92
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 93 TVFELVSYG----RFPhqkgfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTT 168
Cdd:cd03301 88 TVYDNIAFGlklrKVP--------KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 169 YLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-227 |
1.20e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 -QTAEVPTGLTVFE--LVSYGRfpHQK-GF--GTLKEEDYRY---------IHWaLEVTGMTEFANRPAEALSGGQRQRV 148
Cdd:PRK11300 86 fQHVRLFREMTVIEnlLVAQHQ--QLKtGLfsGLLKTPAFRRaesealdraATW-LERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-227 |
2.81e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.28 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 8 AVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeiakkmailPQTAE 87
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-----------AENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTgltVFElvSYGRFPHQK-----GFG-----TLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQG 157
Cdd:PRK09452 88 VNT---VFQ--SYALFPHMTvfenvAFGlrmqkTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 158 TELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-230 |
4.68e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.53 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA---KKMAIL---PQT-------- 85
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVfqdPYAslnprmtv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 ----AEvptGLTVFELVSygrfphqkgfgtlKEEDYRYIHWALEVTGM-TEFANR-PAEaLSGGQRQRVWIAMALAQGTE 159
Cdd:COG4608 115 gdiiAE---PLRIHGLAS-------------KAERRERVAELLELVGLrPEHADRyPHE-FSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-235 |
6.09e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG------KAIEKQPTKE---IAKKM 79
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpKVDERLIRQEagmVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQtaevptgLTVFELVSYGrfPHQKGfGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGT 158
Cdd:PRK09493 87 YLFPH-------LTALENVMFG--PLRVR-GASKEEAEKQARELLAKVGLAERAHHyPSE-LSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT---SETLRS 235
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKnppSQRLQE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-222 |
7.73e-31 |
|
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: 113.85 E-value: 7.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqpTKEIAKKMAILP 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYgrfpHQKGFGTLKEEdyryIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03268 79 EAPGFYPNLTARENLRL----LARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-228 |
2.83e-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: 113.09 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAE 87
Cdd:cd03254 8 VNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGlTVFELVSYGRfphqkgfGTLKEEDyryIHWALEVTGMTEFANR-----------PAEALSGGQRQRVWIAMALAQ 156
Cdd:cd03254 88 LFSG-TIMENIRLGR-------PNATDEE---VIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-248 |
4.38e-30 |
|
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: 115.58 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 25 EIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGK-----------AIEKQPtkeiakkMAILPQTAEVPTGLT 93
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflPPHRRR-------IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVSYGRFPHQKGFGTLKEEDyryihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMA 173
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISFDE------VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 174 HQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQ--IVPCPV 248
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAgsVLEATV 244
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-222 |
4.66e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 111.99 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIekqpTKEIAKKMAILP 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYgrFPHQKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03269 77 EERGLYPKMKVIDQLVY--LAQLKGLK--KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-218 |
7.93e-30 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 111.35 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK---KMAILPQTAEVPTGLTVF 95
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPHQKGfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:cd03292 97 ENVAFALEVTGVP----PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 983475024 176 LEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03292 173 WEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-227 |
8.29e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.30 E-value: 8.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 15 EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPT----KEIAKKMAILPQTAEVPT 90
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 -GLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTE--FANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:PRK13649 99 fEETVLKDVAFG----PQNFGVSQEEAEALAREKLALVGISEslFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 168 TYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-228 |
8.97e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.19 E-value: 8.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:COG1132 339 EIEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGlTVFELVSYGRfPHQkgfgTLKEedyryIHWALEVTGMTEFANRPAE-----------ALSGGQRQRVWI 150
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYGR-PDA----TDEE-----VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNHAsRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEELL 562
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-245 |
1.28e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.26 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTV---YLDGKAIEKQPTKEIAKKMAILPQT--------AE 87
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVLEKLVIQKTrfkkikkiKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGL-TVFELVSYGRFPHQ---------KGFGTLKEEDYRYIHWALEVTGMTE-FANRPAEALSGGQRQRVWIAMALAQ 156
Cdd:PRK13651 103 IRRRVgVVFQFAEYQLFEQTiekdiifgpVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETlrsv 236
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK---- 257
|
....*....
gi 983475024 237 FEIEAQIVP 245
Cdd:PRK13651 258 FLIENNMEP 266
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-222 |
1.32e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 110.92 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtKEIAKKMAILPQTAEVPTGLTVFELV 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SY-GRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLD-MAHQ- 175
Cdd:cd03266 100 EYfAGL-----YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRa 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 983475024 176 -LEVLNLLKklneEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03266 175 lREFIRQLR----ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-217 |
1.62e-29 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 110.80 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK---KMAILPQ 84
Cdd:TIGR02673 7 VSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrrRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVPTGLTVFELVSygrFP-HQKGfgtLKEEDY-RYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:TIGR02673 87 DFRLLPDRTVYENVA---LPlEVRG---KKEREIqRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-240 |
2.06e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.41 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYN-----EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEK-----QPTKEI 75
Cdd:PRK13645 9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 AKKMAILPQTAEVPT-GLTVFELVSYGRFphqkGFGTLKEEDYRYIHWALEVTGM-TEFANRPAEALSGGQRQRVWIAMA 153
Cdd:PRK13645 89 RKEIGLVFQFPEYQLfQETIEKDIAFGPV----NLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 154 LAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
....*..
gi 983475024 234 RSVFEIE 240
Cdd:PRK13645 245 LTKIEID 251
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-229 |
2.17e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPT----KEIAKKMAILPQTAEVPT-GLT 93
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQFPEAQLfENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVSYGrfPHQKGFgTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMA 173
Cdd:PRK13641 103 VLKDVEFG--PKNFGF-SEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 174 HQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:PRK13641 180 GRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
2.31e-29 |
|
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: 115.92 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEGLII-DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVpTGLTVFELVSYGRfphqkgfGTLKEEDyryIHWALEVTGMTEF-ANRP----------AEALSGGQRQRVW 149
Cdd:TIGR02868 413 VCAQDAHL-FDTTVRENLRLAR-------PDATDEE---LWAALERVGLADWlRALPdgldtvlgegGARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLkkLNEEEGRTIVMVIHDL 200
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-227 |
2.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 15 EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVP-TGLT 93
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVSYGRfpHQKGFgTLKEEDYRyIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMA 173
Cdd:PRK13650 99 VEDDVAFGL--ENKGI-PHEEMKER-VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 174 HQLEVLNLLKKLNEEEGRTIVMVIHDLNHASrFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-222 |
3.21e-29 |
|
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: 110.08 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 28 EGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG-------KAIEKQPTKeiaKKMAILPQTAEVPTGLTVFELVSY 100
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 101 GRFPHQKGFGTLKEEDyryihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLN 180
Cdd:cd03297 99 GLKRKRNREDRISVDE------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 983475024 181 LLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-227 |
3.35e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.74 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA------ 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 ---KKMailpqtaevptglTVFELVSYgrfphqkgFGTLK-----EEDYRYIHWaLEVTGMTEFANRPAEALSGGQRQRV 148
Cdd:COG4152 81 glyPKM-------------KVGEQLVY--------LARLKglskaEAKRRADEW-LERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-227 |
3.77e-29 |
|
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: 112.59 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 34 IIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI-----EKQPTKEIAKKMAILPQtaevptgLTVFELVSYGRfphqKG 108
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnvppHLRHINMVFQSYALFPH-------MTVEENVAFGL----KM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 109 FGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEE 188
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 983475024 189 EGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-240 |
3.92e-29 |
|
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: 115.17 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKkGTVYLDGKAIEKQPTKEIA---KKMAILPQTaevPTG----- 91
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRplrRRMQVVFQD---PFGslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 LTVFELVSYGRFPHQKGFGtlKEEDYRYIHWALEVTGMT-EFANR-PAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:COG4172 379 MTVGQIIAEGLRVHGPGLS--AAERRARVAEALEEVGLDpAARHRyPHE-FSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 170 LDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM-------TSETLRSVFEIE 240
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFdapqhpyTRALLAAAPLLE 533
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-206 |
5.84e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 108.86 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK----KMAILPQ 84
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrreKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVPTGLTVFELVSYGrFPHQKGFGTLKEEDYRYihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:TIGR03608 84 NFALIENETVEENLDLG-LKYKKLSKKEKREKKKE---ALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 983475024 165 EPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRF 206
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDPEVAKQA 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-230 |
1.47e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.29 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI-------------EKQ 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 71 PTKEIAKKMAILPQTAEVPTGLTVFELVSYGrfPHQKgFGTLKEEDYRYIHWALEVTGMTEFANR--PAEaLSGGQRQRV 148
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEA--PIQV-LGLSKQEARERAVKYLAKVGIDERAQGkyPVH-LSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
..
gi 983475024 229 TS 230
Cdd:PRK10619 241 GN 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-234 |
2.03e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMailpqtaevptgltVFElv 98
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINM--------------MFQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYGRFPHQK-----GFGtLKE------EDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:PRK11607 99 SYALFPHMTveqniAFG-LKQdklpkaEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 168 TYLDMA----HQLEVLNLLKKLneeeGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLR 234
Cdd:PRK11607 178 GALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-222 |
2.12e-28 |
|
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: 106.63 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAI 81
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVptgltvFElvsygrfphqkgfgtlkeedyryihwalevtgmTEFANRPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:cd03247 80 LNQRPYL------FD---------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLkkLNEEEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQG 222
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-227 |
6.60e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.17 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE--KQPTKEIAKKMAI 81
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLT------VFELvsygrfphqKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK13638 82 VFQDPEQQIFYTdidsdiAFSL---------RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-227 |
8.29e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.24 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 11 VGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAK-----KGTVYLDGKAI--EKQPTKEIAKKMAILP 83
Cdd:PRK14267 12 VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYGRfpHQKGFGTLKEEDYRYIHWALEVTGM-TEFANR----PAEaLSGGQRQRVWIAMALAQGT 158
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGV--KLNGLVKSKKELDERVEWALKKAALwDEVKDRlndyPSN-LSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
1.03e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 104.43 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAIL 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQtaevptgltvfelvsygrfphqkgfgtlkeedyryihwalevtgmtefanrpaeaLSGGQRQRVWIAMALAQGTELLV 162
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-226 |
1.05e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.04 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAIlpqtaevptgltVFEl 97
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICM------------VFQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 vSYGRFPHQ----------KGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:PRK11432 86 -SYALFPHMslgenvgyglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 168 TYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-217 |
1.49e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQ-----TAEv 88
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQdpmmgTAP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 ptGLTVFE--LVSYGRfpHQK---GFGTLKEEDYRYIHwALEVTGMtEFANR---PAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:COG1101 96 --SMTIEEnlALAYRR--GKRrglRRGLTKKRRELFRE-LLATLGL-GLENRldtKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 161 LVLDEPTTYLD--MAHQleVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:COG1101 170 LLLDEHTAALDpkTAAL--VLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-245 |
3.33e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.04 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPT-GLTVFEL 97
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIfSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGrfPHQKGfgtLKEEDYRY-IHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQL 176
Cdd:PRK13652 100 IAFG--PINLG---LDEETVAHrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 177 EVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEIEAQIVP 245
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSLP 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-233 |
3.35e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVP-TGLTVFEL 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLE 177
Cdd:PRK13642 103 VAFG----MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 178 VLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVM-TSETL 233
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFaTSEDM 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
4.12e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.96 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-M 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVSYGrfphqkGFGTLKEEDYRYIHWALEV-TGMTEFANRPAEALSGGQRQRVWIAMALAQGT 158
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVF 237
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-230 |
4.30e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKA------IEKQPTKEIAKKMAILPQTAE 87
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGLTVFELVSYGRFPH----QKGFGTLKEEDYRYIHWALEVTgmtEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHgikeKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-227 |
7.82e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 7.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI----EKQPTKEIAKKMAILPQTAEVPT-GLTVFE 96
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVGVVFQFPESQLfEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 LVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMT-EFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:PRK13643 105 DVAFG----PQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 176 LEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13643 181 IEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-229 |
8.02e-27 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 109.19 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 7 DAVSVGYNE--GLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQ 84
Cdd:TIGR03375 467 RNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAevptglTVFelvsygrfphqkgFGTLKE---------EDYRYIHwALEVTGMTEFANR-PA----------EALSGGQ 144
Cdd:TIGR03375 547 DP------RLF-------------YGTLRDnialgapyaDDEEILR-AAELAGVTEFVRRhPDgldmqigergRSLSGGQ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 145 RQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLnHASRFSDHMIALKAGKLMKQGTP 224
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPK 683
|
....*
gi 983475024 225 DEVMT 229
Cdd:TIGR03375 684 DQVLE 688
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-230 |
8.56e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 23 TVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA----KKMAILPQTAEVPTGLTVFELV 98
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEV 178
Cdd:PRK10070 128 AFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 179 LNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-222 |
8.83e-27 |
|
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: 103.40 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEipEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAILPQTAEVPTGLTVFELVSYG 101
Cdd:TIGR01277 19 LNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 RFPHQKgfgtLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNL 181
Cdd:TIGR01277 95 LHPGLK----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 983475024 182 LKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
1.16e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.56 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqPTKE-- 74
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 75 -IAKKMAILPQtaevptgLTVFELVSYG-RFphqKGFGtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAM 152
Cdd:COG4525 80 vVFQKDALLPW-------LNVLDNVAFGlRL---RGVP--KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 983475024 153 ALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHA 203
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-237 |
1.30e-26 |
|
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: 103.39 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-MAILPQTAEVPTG 91
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 LTVFE-LVSYGRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL 170
Cdd:cd03218 90 LTVEEnILAVLEI-----RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 171 DMAHQLEVLNLLKKLNEeegRTIVMVIHDlnHASR----FSDHMIALKAGKLMKQGTPDEVMTSETLRSVF 237
Cdd:cd03218 165 DPIAVQDIQKIIKILKD---RGIGVLITD--HNVRetlsITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-245 |
1.63e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA---KKMAILPQTAEVPTGLTVFE 96
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLSSRTVAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 LVSygrFP--HQkgfGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMA 173
Cdd:COG1135 102 NVA---LPleIA---GVPKAEIRKRVAELLELVGLSDKADAyPSQ-LSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 174 HQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT---SETLRS-VFEIEAQIVP 245
Cdd:COG1135 175 TTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAnpqSELTRRfLPTVLNDELP 250
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-213 |
2.25e-26 |
|
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: 107.37 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGY-NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGlTVFELVSYGRfphqkgfgtlKEEDYRYIHWALEVTGMTEFAN-RPA----------EALSGGQRQRVWI 150
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR----------PDASDAEIREALERAGLDEFVAaLPQgldtpigeggAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLneEEGRTIVMVIHDLNHASRfSDHMIAL 213
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-228 |
4.02e-26 |
|
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: 102.23 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTaevPT--GLTVF 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE---PVlfDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPhqkgfGTLKEED--------YRYIHwALEVTGMTEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:cd03249 95 ENIRYGKPD-----ATDEEVEeaakkaniHDFIM-SLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 168 TYLDMAHQLEVLNLLKKLneEEGRTIVMVIHDLnHASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:cd03249 168 SALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-230 |
4.11e-26 |
|
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: 106.69 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTllkTASRILK-------AKKGTVYLDGKAIEK 69
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSV---TALSILRllpdpaaHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 70 QPTKEIAK----KMAIL---PQTAEVPTgLTVFELVSYGRFPHQKGFGtlKEEDYRYIHWaLEVTGMTEFANR----PAE 138
Cdd:COG4172 81 LSERELRRirgnRIAMIfqePMTSLNPL-HTIGKQIAEVLRLHRGLSG--AAARARALEL-LERVGIPDPERRldayPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 139 aLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:COG4172 157 -LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250
....*....|..
gi 983475024 219 MKQGTPDEVMTS 230
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-216 |
4.73e-26 |
|
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: 102.16 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI-EKQPTKEIA-KKMAILP-QTAEVPTGLTVF 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDRMVVfQNYSLLPwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVsygrfPHQKgfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:TIGR01184 81 RVL-----PDLS-----KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 983475024 176 LEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAG 216
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-222 |
6.57e-26 |
|
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: 101.58 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRIL---KAKKGTVYLDGKAIEKQPTKEIakkMAILPQTAEVPT 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQKC---VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 GLTVFELVSYG---RFPHQKGFGTLKEEDyryihwalEVTGMTEFANRPA-----EALSGGQRQRVWIAMALAQGTELLV 162
Cdd:cd03234 95 GLTVRETLTYTailRLPRKSSDAIRKKRV--------EDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIH----DLnhaSRFSDHMIALKAGKLMKQG 222
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQL-ARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-245 |
6.98e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.11 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK---KMAILPQTAEVPTGLTVFE 96
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 LVSygrFPHQKGfGTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:PRK11153 102 NVA---LPLELA-GTPKAEIKARVTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 176 LEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT---SETLRS-VFEIEAQIVP 245
Cdd:PRK11153 177 RSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFShpkHPLTREfIQSTLHLDLP 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
8.72e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLdGKAIekqptkeiakKMAILP 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 Q-TAEVPTGLTVFELVSYGRfphqkgfgtlkEEDYRyihwaLEVTGMTE---F----ANRPAEALSGGQRQRVWIAMALA 155
Cdd:COG0488 385 QhQEELDPDKTVLDELRDGA-----------PGGTE-----QEVRGYLGrflFsgddAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 156 QGTELLVLDEPTTYLDMAhQLEVLNLLkkLNEEEGrTIVMVIHD---LNhasRFSDHMIALKAGKL 218
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIE-TLEALEEA--LDDFPG-TVLLVSHDryfLD---RVATRILEFEDGGV 507
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-218 |
1.01e-25 |
|
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: 100.89 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK----KMAILPQ 84
Cdd:TIGR02211 11 YQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVPTGLTVFELVSYGRFPHQKGFGTLKEEDYRYihwaLEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:TIGR02211 91 FHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEM----LEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 165 EPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFsDHMIALKAGKL 218
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-203 |
1.03e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.63 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLK----TASRILKAkKGTVYLDGKAIEKQPTKeiAKK 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaiagTLSPAFSA-SGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAILPQTAEVPTGLTVFELVSYGrFPHQKGfgtlKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQG 157
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFA-LPPTIG----RAQRRARVEQALEEAGLAGFADRdPAT-LSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 983475024 158 TELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHA 203
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-228 |
1.07e-25 |
|
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: 101.15 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL-IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAIL 82
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTaevpTGL---TVFELVSYGRFphqkgfGTLKEEDYR-----YIHwaLEVTGMTE-FANRPAE---ALSGGQRQRVWI 150
Cdd:cd03253 81 PQD----TVLfndTIGYNIRYGRP------DATDEEVIEaakaaQIH--DKIMRFPDgYDTIVGErglKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVM 228
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-230 |
1.09e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.04 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRiLKAKKGTVYLDGKA-------IEKQPTKEIA 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRVeffnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 KKMA--ILPQTAEVPtgLTVFELVSYGrfphqkgfgtlkeedYRYIHW--ALEVTGMTEFANRPAE-------------- 138
Cdd:PRK14258 87 RRQVsmVHPKPNLFP--MSVYDNVAYG---------------VKIVGWrpKLEIDDIVESALKDADlwdeikhkihksal 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 139 ALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKA--- 215
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnen 229
|
250
....*....|....*..
gi 983475024 216 --GKLMKQGTPDEVMTS 230
Cdd:PRK14258 230 riGQLVEFGLTKKIFNS 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-233 |
1.24e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.01 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYL------DGKAIEKQPTKEIAKKMAILPQTAE 87
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKKIKNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTglTVFELVSYGRFPH--QK-------GFGTLKEEDYRYIHWALEVTGMTE-FANRPAEALSGGQRQRVWIAMALAQG 157
Cdd:PRK13631 117 RVS--MVFQFPEYQLFKDtiEKdimfgpvALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 158 TELLVLDEPTTYLDMAHQLEVLNLLKKlNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-239 |
1.92e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAI 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFE-LVSYGRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:PRK13537 85 VPQFDNLDPDFTVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFEI 239
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEI 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-208 |
2.01e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASR----ILKAK-KGTVYLDGKAIEKQPTK--EIA 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndlIPGFRvEGKVTFHGKNLYAPDVDpvEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 KKMAILPQTAEvPTGLTVFELVSYGrfPHQKGF-GTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYG--ARINGYkGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSD 208
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-222 |
2.18e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.97 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYN--EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAevptglTVFelvsygrfphqkgFGTLKE---------EDYRyIHWALEVTGMTEFANR-PA----------EALS 141
Cdd:cd03245 83 VPQDV------TLF-------------YGTLRDnitlgaplaDDER-ILRAAELAGVTDFVNKhPNgldlqigergRGLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 142 GGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLneEEGRTIVMVIHD---LNHASRfsdhMIALKAGKL 218
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRpslLDLVDR----IIVMDSGRI 216
|
....
gi 983475024 219 MKQG 222
Cdd:cd03245 217 VADG 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-234 |
2.39e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.99 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGK---AIEKQPTKEIAKKMAIL 82
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVSYGRFPHQKgfgtLKEEDYR-YIHWALEVTGMTEFAN-RPAEaLSGGQRQRVWIAMALAQGTEL 160
Cdd:PRK11831 90 FQSGALFTDMNVFDNVAYPLREHTQ----LPAPLLHsTVMMKLEAVGLRGAAKlMPSE-LSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLR 234
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
2.42e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.91 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVyLDGKAiekqPTKEIAKKMAILP 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA----PLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSYGrfphQKGfgtlkeedyryiHW------ALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQG 157
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLG----LKG------------QWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 158 TELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-223 |
2.95e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.86 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRIL---KAKKGTVYLDGKAIEKQP--TKEIAKKMA 80
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ---ILPQTAEVPTGLTVFELV---SYGRFPHQKG-FGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMA 153
Cdd:PRK09984 87 ntgYIFQQFNLVNRLSVLENVligALGSTPFWRTcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 154 LAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGT 223
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-198 |
7.03e-25 |
|
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: 97.29 E-value: 7.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVptgltvfelvsygrFPhqkgfGTLKEedyryihwalevtgmtefanrpaEALSGGQRQRVWIAMALAQGTELL 161
Cdd:cd03246 81 LPQDDEL--------------FS-----GSIAE-----------------------NILSGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIH 198
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAH 154
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-222 |
7.63e-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: 97.62 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLK--TASRILKAKKGTVYLDGKAIEKQptkEIAKKMAILPQTAEVPTGLTVF 95
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNalAGRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYgrfphqkgfgtlkeedyryihwALEVTGmtefanrpaeaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:cd03213 101 ETLMF----------------------AAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 983475024 176 LEVLNLLKKLnEEEGRTIVMVIHDLNhASRFS--DHMIALKAGKLMKQG 222
Cdd:cd03213 148 LQVMSLLRRL-ADTGRTIICSIHQPS-SEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-222 |
9.22e-25 |
|
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: 98.56 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGLTVFElv 98
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVID-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 sygrfphqkGFGTLKE----EDYRYIHWALEVTGM---TEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:cd03267 115 ---------SFYLLAAiydlPPARFKKRLDELSELldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 983475024 172 MAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
1.42e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 98.72 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSV-------GYNEglIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTK 73
Cdd:COG4598 1 MTDTAPPALEVrdlhksfGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 74 EIAKKMAILPQTAEVPTGLT-VFElvSYGRFPHQkgfgT------------LKEEDYRYIHWA---LEVTGMTEFANR-P 136
Cdd:COG4598 79 DGELVPADRRQLQRIRTRLGmVFQ--SFNLWSHM----TvlenvieapvhvLGRPKAEAIERAealLAKVGLADKRDAyP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 137 AEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAG 216
Cdd:COG4598 153 AH-LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
250 260
....*....|....*....|.
gi 983475024 217 KLMKQGTPDEVMT---SETLR 234
Cdd:COG4598 231 RIEEQGPPAEVFGnpkSERLR 251
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-228 |
1.64e-24 |
|
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: 102.13 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKM 79
Cdd:COG4618 329 GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGlTVFELVSygRFPhqkgfgtlkEEDYRYIHWALEVTGMTEFANRPAE-----------ALSGGQRQRV 148
Cdd:COG4618 409 GYLPQDVELFDG-TIAENIA--RFG---------DADPEKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLD---MAHQLEVLNLLKklneEEGRTIVMVIHD---LNHAsrfsDHMIALKAGKLMKQG 222
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDdegEAALAAAIRALK----ARGATVVVITHRpslLAAV----DKLLVLRDGRVQAFG 548
|
....*.
gi 983475024 223 TPDEVM 228
Cdd:COG4618 549 PRDEVL 554
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-226 |
1.70e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.49 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKM- 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 ----AILPQtaevptgLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK11000 81 fqsyALYPH-------LSVAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-232 |
2.04e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGL-----IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKE--- 74
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK-TKDkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 75 --IAKKMAILPQTAEvpTGL---TVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTE--FANRPAEaLSGGQRQR 147
Cdd:PRK13646 81 rpVRKRIGMVFQFPE--SQLfedTVEREIIFG----PKNFKMNLDEVKNYAHRLLMDLGFSRdvMSQSPFQ-MSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 148 VWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
....*
gi 983475024 228 MTSET 232
Cdd:PRK13646 234 FKDKK 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-218 |
2.52e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEG-KITtIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAiekqptkeiakKMAILPQ 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRIG-LVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVPTGLTVFELVSYGRFP------------HQKGFGTLKEEDYRYIH--------WALE------VTGM---TEFANR 135
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAElraleaeleeleAKLAEPDEDLERLAELQeefealggWEAEaraeeiLSGLgfpEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 136 PAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDmahqLEVLNLLKK-LNEEEGrTIVMVIHD---LNHAsrfSDHMI 211
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSHDryfLDRV---ATRIL 220
|
....*..
gi 983475024 212 ALKAGKL 218
Cdd:COG0488 221 ELDRGKL 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-231 |
2.66e-24 |
|
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: 97.30 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYN--EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGlTVFELVSYGRFphqkgfgtlkEEDYRYIHWALEVTGMTEFANRPAEA-----------LSGGQRQRVWI 150
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRP----------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLneEEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQ 226
|
.
gi 983475024 231 E 231
Cdd:cd03251 227 G 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-236 |
5.00e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGL-IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG-KAIEKQPTKEIAKKMAILP 83
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVP-TGLTVFELVSYGrfPHQKGFGTLkeEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:PRK13644 84 QNPETQfVGRTVEEDLAFG--PENLCLPPI--EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHAsRFSDHMIALKAGKLMKQGTPDEVMTSETLRSV 236
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
7.80e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.36 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSV--GYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKK 78
Cdd:PRK13536 37 MSTVAIDLAGVskSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAILPQTAEVPTGLTVFE-LVSYGRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQG 157
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 158 TELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVF 237
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVI 269
|
..
gi 983475024 238 EI 239
Cdd:PRK13536 270 EI 271
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-233 |
3.05e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQtaevptgltvfEL 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ-----------EP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGR-FPHQKGFGTLKEEDYRYIHWALE------VTGMTEFAN----RPAEALSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:TIGR00958 565 VLFSGsVRENIAYGLTDTPDEEIMAAAKAanahdfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 167 TTYLDMahqlEVLNLLKKLNEEEGRTIVMVIHDLnHASRFSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:TIGR00958 645 TSALDA----ECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-221 |
3.08e-23 |
|
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: 95.26 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL---------IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIekqpTKE 74
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL----YQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 75 IAKKMAILPQTAEVptgltVFElVSYGRFPHQKGFGTLKEEDYRY------------IHWALEVTGM-TEFANRPAEALS 141
Cdd:TIGR02769 79 DRKQRRAFRRDVQL-----VFQ-DSPSAVNPRMTVRQIIGEPLRHltsldeseqkarIAELLDMVGLrSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 142 GGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQ 221
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-227 |
3.93e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE-IAKKMAILPQtaE---VPTgLTVF 95
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQ--ElnlVPN-LSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPHQKGFgtlkeedyryIHW---------ALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:COG1129 98 ENIFLGREPRRGGL----------IDWramrrrareLLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 167 TTYLDMAhqlEVLNLLKKLNE--EEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG1129 168 TASLTER---EVERLFRIIRRlkAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-232 |
4.36e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 23 TVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeIAKK-MAILPQTAEVPTGLTVFELVSYG 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP---PSRRpVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 RFPHQKgfgtLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLN 180
Cdd:PRK10771 96 LNPGLK----LNAAQREKLHAIARQMGIEDLLARlPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 181 LLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSET 232
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-238 |
5.90e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEiaKKMAIL 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGLTVFELVSYGR--FPHQK--GFGTLKEEDYRYihwaLEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGT 158
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLtvLPRRErpNAAAIKAKVTQL----LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVFE 238
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLE 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
6.69e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.05 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDgkAIEKQPTKEIAKKMA 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEvPTGLtVFElvSYGRFPHQKGF-----------GTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVW 149
Cdd:PRK11264 79 LIRQLRQ-HVGF-VFQ--NFNLFPHRTVLeniiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEgRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-173 |
8.32e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 92.42 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAILP 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFE-LVSYGRF--PHQkgfgtlkeedyRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:TIGR01189 80 HLPGLKPELSALEnLHFWAAIhgGAQ-----------RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170
....*....|...
gi 983475024 161 LVLDEPTTYLDMA 173
Cdd:TIGR01189 149 WILDEPTTALDKA 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-222 |
1.41e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRI--LKAK---KGTVYLDGKAI--EKQPTKEIA 76
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 KKMAILPQTAEvPTGLTVFELVSYG-RFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK14239 86 KEIGMVFQQPN-PFPMSIYENVVYGlRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 156 QGTELLVLDEPTTYLD--MAHQLE--VLNLLKKLneeegrTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:PRK14239 165 TSPKIILLDEPTSALDpiSAGKIEetLLGLKDDY------TMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-224 |
1.65e-22 |
|
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: 97.01 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAILPQTAEVPTGLTVFE-L 97
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN-LDAVRQSLGMCPQHNILFHHLTVAEhI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRFPhqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLE 177
Cdd:TIGR01257 1025 LFYAQLK-----GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 983475024 178 VLNLLkkLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTP 224
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-237 |
2.24e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.35 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLktaSRILKAKK---GTVY-LDGkaiekqptkEIAKKM-- 79
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL---SLIAGARKiqqGRVEvLGG---------DMADARhr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 -AILPQTAEVPTGL--------TVFELVSY-GRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVW 149
Cdd:NF033858 72 rAVCPRIAYMPQGLgknlyptlSVFENLDFfGRL-----FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMV-IHDLNHASRFsDHMIALKAGKLMKQGTPDEVM 228
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
250
....*....|..
gi 983475024 229 T---SETLRSVF 237
Cdd:NF033858 226 ArtgADTLEAAF 237
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-231 |
2.93e-22 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 95.79 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLktasRIL----KAKKGTVYLDGKAIEKQPTKEIAK 77
Cdd:TIGR03797 452 IEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 78 KMAILPQTAEVPTGlTVFE-LVSYGRFPHQKGFGTLK----EEDYRyihwALEVtGMTEFANRPAEALSGGQRQRVWIAM 152
Cdd:TIGR03797 528 QLGVVLQNGRLMSG-SIFEnIAGGAPLTLDEAWEAARmaglAEDIR----AMPM-GMHTVISEGGGTLSGGQRQRLLIAR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 153 ALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEeegrTIVMVIHDLN---HASRfsdhMIALKAGKLMKQGTPDEVMT 229
Cdd:TIGR03797 602 ALVRKPRILLFDEATSALDNRTQAIVSESLERLKV----TRIVIAHRLStirNADR----IYVLDAGRVVQQGTYDELMA 673
|
..
gi 983475024 230 SE 231
Cdd:TIGR03797 674 RE 675
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-219 |
4.22e-22 |
|
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: 91.34 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAV--SVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI----EKQPTKEI 75
Cdd:COG4181 9 IELRGLtkTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 76 AKKMAILPQTAE-VPTgLTVFELVSygrFPhqkgfgtlkeedyryihwaLEVTGMTEFANRPAEAL-------------- 140
Cdd:COG4181 89 ARHVGFVFQSFQlLPT-LTALENVM---LP-------------------LELAGRRDARARARALLervglghrldhypa 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 141 --SGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKL 218
Cdd:COG4181 146 qlSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
.
gi 983475024 219 M 219
Cdd:COG4181 225 V 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-218 |
6.85e-22 |
|
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: 90.99 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 17 LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGlTVFE 96
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 LVSYGRfpHQKGFGTLKEEDYRYiHWALEVTGM-----TEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:cd03248 107 NIAYGL--QSCSFECVKEAAQKA-HAHSFISELasgydTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 983475024 172 MAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRfSDHMIALKAGKL 218
Cdd:cd03248 183 AESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-228 |
7.83e-22 |
|
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: 94.40 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGlTVFELV 98
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYGRfphqkgfgtLKEEDYRYIHWALEVTGMTEFANRPAEA-----------LSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:TIGR02203 427 AYGR---------TEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 168 TYLDMAHQLEVLNLLKKLneEEGRTIVMVIHDLN---HAsrfsDHMIALKAGKLMKQGTPDEVM 228
Cdd:TIGR02203 498 SALDNESERLVQAALERL--MQGRTTLVIAHRLStieKA----DRIVVMDDGRIVERGTHNELL 555
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-227 |
1.19e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.08 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTK---EIAKKMAILPQT--AEVPTGLT 93
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVS-----YgrFPHQKGfGTLKEedyRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTT 168
Cdd:PRK15079 117 IGEIIAeplrtY--HPKLSR-QEVKD---RVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 169 YLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-237 |
1.61e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.34 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-M 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVsYGRFPHQKGFGTLKEEDyrYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNL-MAVLQIRDDLSAEQRED--RANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVF 237
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-227 |
1.99e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAILPQtaE---VPTgLTVF 95
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALGIGMVHQ--HfmlVPN-LTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPHQKGFGTLKE---------EDYRyihwaLEVTgmtefANRPAEALSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:COG3845 99 ENIVLGLEPTKGGRLDRKAararirelsERYG-----LDVD-----PDAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 167 TTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG3845 169 TAVLTPQEADELFEILRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-227 |
2.00e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 91.71 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKST-------LLKTASRIlkakKGTVYLDGKAIEKQPTKEI----AKKMAIL---PQ 84
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRI----GGSATFNGREILNLPEKELnklrAEQISMIfqdPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVP---TGLTVFE-LVSYGRFPHQKGFgtlkEEDYRyihwALEVTGMTEFANR----PAEaLSGGQRQRVWIAMALAQ 156
Cdd:PRK09473 108 TSLNPymrVGEQLMEvLMLHKGMSKAEAF----EESVR----MLDAVKMPEARKRmkmyPHE-FSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-228 |
2.63e-21 |
|
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: 93.27 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 11 VGYNEGL---IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAE 87
Cdd:TIGR01193 479 VSYSYGYgsnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPY 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGlTVFELVSYGRFPhqkgfGTLKEEdyryIHWALEVTGM-TEFANRP----------AEALSGGQRQRVWIAMALAQ 156
Cdd:TIGR01193 559 IFSG-SILENLLLGAKE-----NVSQDE----IWAACEIAEIkDDIENMPlgyqtelseeGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 157 GTELLVLDEPTTYLDMAHQLEVLNLLKKLNEeegRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVM 228
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-237 |
2.82e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATL-AVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTvyldgkaIEKQPTKEIAkkm 79
Cdd:PRK09544 1 MTSLvSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRNGKLRIG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 aILPQTAEVPTGLTVfelvSYGRFPHQKGfGTLKEEdyryIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:PRK09544 71 -YVPQKLYLDTTLPL----TVNRFLRLRP-GTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKaGKLMKQGTPDEVMTSETLRSVF 237
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHPEFISMF 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-227 |
2.88e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.18 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA---KKMAILPQTaevPtgltvf 95
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQN---P------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 elvsYGRF-PHQKGFGTLKE-----------EDYRYIHWALEVTGM-TEFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:PRK11308 102 ----YGSLnPRKKVGQILEEpllintslsaaERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-217 |
5.55e-21 |
|
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: 85.96 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAiekqptkeiakKMAILP 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QtaevptgltvfelvsygrfphqkgfgtlkeedyryihwalevtgmtefanrpaeaLSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNeeegRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-218 |
6.63e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.51 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE-IAKKM 79
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAE-VPTgLTVFELVSYGRFPHQKGF---GTLKEEDYRYihwaLEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK11288 82 AIIYQELHlVPE-MTVAENLYLGQLPHKGGIvnrRLLNYEAREQ----LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 156 QGTELLVLDEPTTYLDmAHQLEVL-NLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK11288 157 RNARVIAFDEPTSSLS-AREIEQLfRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-253 |
1.28e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEG----LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKgTVYLDG----------KA 66
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPP-VVYPSGdirfhgesllHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 67 IEKQPTKEIAKKMAILPQTAEVPTG------LTVFELVSYGRfphqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAE-- 138
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEPMVSLNplhtleKQLYEVLSLHR-------GMRREAARGEILNCLDRVGIRQAAKRLTDyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 139 -ALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:PRK15134 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 983475024 218 LMKQ-------GTPDEVMTSETLRSvfEIEAQIVPCPVNCKPI 253
Cdd:PRK15134 235 CVEQnraatlfSAPTHPYTQKLLNS--EPSGDPVPLPEPASPL 275
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-203 |
1.32e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqPTKE---IAKKMA 80
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAErgvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQtaevptgLTVFELVSYGrfphQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:PRK11248 81 LLPW-------RNVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHA 203
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-218 |
2.19e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.82 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEG---------LIIDGLTVEIPEGKITTIIGPNGCGKSTLlktaSRIL----KAKKGTVYLDGKAI 67
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvgleSPSQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 68 EKQPTKEiakkMAILPQTAEVptgltVFElVSYGRFPHQKGFGTLKEEDYRYI---------HWALEVTGMTEFA----- 133
Cdd:PRK10419 77 AKLNRAQ----RKAFRRDIQM-----VFQ-DSISAVNPRKTVREIIREPLRHLlsldkaerlARASEMLRAVDLDdsvld 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 134 NRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIAL 213
Cdd:PRK10419 147 KRPPQ-LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM 225
|
....*
gi 983475024 214 KAGKL 218
Cdd:PRK10419 226 DNGQI 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-222 |
2.52e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.06 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKS----TLLKTASRILKAKKGTVYLDGKAIEkqPTKEIAKKMAIL---PQTAEVPt 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA--PCALRGRKIATImqnPRSAFNP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 gltVFELVSYGRfphQKGFGTLKEEDYRYIHWALEVTGMTEfANRPAEA----LSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:PRK10418 95 ---LHTMHTHAR---ETCLALGKPADDATLTAALEAVGLEN-AARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 167 TTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
9-231 |
3.08e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 90.00 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYN--EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQ-- 84
Cdd:TIGR03796 483 ITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQdi 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 ---TAEVPTGLTVFElvsygrfphqkgfGTLKEEDYRY------IHwaLEVTGMT-EFANRPAEA---LSGGQRQRVWIA 151
Cdd:TIGR03796 563 flfEGTVRDNLTLWD-------------PTIPDADLVRackdaaIH--DVITSRPgGYDAELAEGganLSGGQRQRLEIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 152 MALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKlneeEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-228 |
3.19e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeIAkkmAILpqtaEVPTG----LT 93
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VS---ALL----ELGAGfhpeLT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELV-SYGRFphqKGFgTLKEEDYRY--IhwaLEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL 170
Cdd:COG1134 105 GRENIyLNGRL---LGL-SRKEIDEKFdeI---VEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 171 DMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:COG1134 178 DAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
3.41e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.50 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKM 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTG------------------LTVFELVsygrfphqkGFGTLKEEDYRYIHWALEvtgmtefANRPaeaLS 141
Cdd:PRK11160 417 SVVSQRVHLFSAtlrdnlllaapnasdealIEVLQQV---------GLEKLLEDDKGLNAWLGE-------GGRQ---LS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 142 GGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQ 221
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
250
....*....|
gi 983475024 222 GTPDEVMTSE 231
Cdd:PRK11160 555 GTHQELLAQQ 564
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-233 |
4.78e-20 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 89.42 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGlTVFEL 97
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRfPHQkgfgtlkeEDYRYIHwALEVTGMTEFANRPAE-----------ALSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:TIGR01846 551 IALCN-PGA--------PFEHVIH-AAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 167 TTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:TIGR01846 621 TSALDYESEALIMRNMREIC--RGRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-182 |
5.50e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEkqpTKEIAKKMAIL 82
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 -PQTAEVPTgLTVFE-LVSYGRFphqkgFGTlkeeDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:PRK13539 79 gHRNAMKPA-LTVAEnLEFWAAF-----LGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180
....*....|....*....|..
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLL 182
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELI 170
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-229 |
7.63e-20 |
|
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: 88.56 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGkkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTGlTVFELVSygRFPhqkgfgtlKEEDYRYIHWALEVTGMTEF-ANRP----------AEALSGGQRQRVW 149
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIA--RFG--------ENADPEKIIEAAKLAGVHELiLRLPdgydtvigpgGATLSGGQRQRIA 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-225 |
1.26e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.07 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEiaKKMAILPQtaEVptGLtVFElvSY 100
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSD--KAIRELRR--NV--GM-VFQ--QY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 101 GRFPHQ-----------KGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:PRK11124 92 NLWPHLtvqqnlieapcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 170 LDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPD 225
Cdd:PRK11124 172 LDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-228 |
1.67e-19 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.88 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYL---DGKAIEKQPTKEIAKKM- 79
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 -----AILPQTA------EVPTGLTVFE-LVSYGrfphQKGFGTLKEEDYRyihWALEV-TGMTEFANRPAeALSGGQRQ 146
Cdd:TIGR02323 84 mrtewGFVHQNPrdglrmRVSAGANIGErLMAIG----ARHYGNIRATAQD---WLEEVeIDPTRIDDLPR-AFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 147 RVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
..
gi 983475024 227 VM 228
Cdd:TIGR02323 236 VL 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-219 |
3.38e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAIlpqtaevptgltVFelv 98
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-RKEFARRIGV------------VF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 syGrfphQKG-----------FGTLKE------EDYRY-IHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:COG4586 102 --G----QRSqlwwdlpaidsFRLLKAiyripdAEYKKrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLM 219
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-218 |
3.73e-19 |
|
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: 83.35 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqPTKEIAKKMAILPQtaevptgLTVFE- 96
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-----VSSLLGLGGGFNPE-------LTGREn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 LVSYGRFphqkgFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQL 176
Cdd:cd03220 105 IYLNGRL-----LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 983475024 177 EVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03220 180 KCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-224 |
3.77e-19 |
|
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: 83.31 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILP 83
Cdd:cd03244 5 FKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGlTVfelvsygRF---PhqkgFGTLKEEDyryIHWALEVTGMTEFANRPAEAL-----------SGGQRQRVW 149
Cdd:cd03244 85 QDPVLFSG-TI-------RSnldP----FGEYSDEE---LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKklNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTP 224
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-219 |
4.63e-19 |
|
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: 86.38 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVE---IPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeIAKKmailPQTAEVPTGLTVFELV 98
Cdd:COG1245 356 LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK---------ISYK----PQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 sygRFPHQKGFGT--LKEEdyryihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQL 176
Cdd:COG1245 423 ---RSANTDDFGSsyYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 983475024 177 EVLNLLKKLNEEEGRTIVMVIHDLnhasrfsdHMIALKAGKLM 219
Cdd:COG1245 493 AVAKAIRRFAENRGKTAMVVDHDI--------YLIDYISDRLM 527
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-224 |
9.37e-19 |
|
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: 82.07 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYGRFPHQKGFGtlkeedyryihwALEVTGmtefanrPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYG------------ALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKlnEEEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQGTP 224
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-236 |
9.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVY-----LDGKAI-EKQPTKEIAK 77
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIfNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 78 KMAILPQTAEvPTGLTVFELVSYGRFPHQkgfgTLKEEDYRYIHWA--LEVTGMTEFANRPAEA---LSGGQRQRVWIAM 152
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHK----LVPRKEFRGVAQArlTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 153 ALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS-- 230
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSpk 254
|
....*...
gi 983475024 231 --ETLRSV 236
Cdd:PRK14271 255 haETARYV 262
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-227 |
1.13e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.02 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGY-NEGL---IIDGLTVEIPEGKITTIIGPNGCGKST-------LLKTASRILKAKKGTVYLDGKAI-E 68
Cdd:PRK11022 1 MALLNVDKLSVHFgDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRVMAEKLEFNGQDLQRIsE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 69 KQPTKEIAKKMAIL---PQTAEVP---TGLTVFELVSYgrfpHQKGfgTLKEEDYRYIHwALEVTGMTEFANR----PAE 138
Cdd:PRK11022 81 KERRNLVGAEVAMIfqdPMTSLNPcytVGFQIMEAIKV----HQGG--NKKTRRQRAID-LLNQVGIPDPASRldvyPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 139 aLSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK11022 154 -LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
....*....
gi 983475024 219 MKQGTPDEV 227
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
1.77e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKK-M 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTV-------FELVSYGrfphqkgfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAM 152
Cdd:COG1137 81 GYLPQEASIFRKLTVednilavLELRKLS-----------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 153 ALAQGTELLVLDEPTTYLD-MAHQlEVLNLLKKLNEeegRTIVMVIHDlnHASR----FSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpIAVA-DIQKIIRHLKE---RGIGVLITD--HNVRetlgICDRAYIISEGKVLAEGTPEEI 223
|
250
....*....|
gi 983475024 228 MTSETLRSVF 237
Cdd:COG1137 224 LNNPLVRKVY 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-223 |
2.15e-18 |
|
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: 81.69 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVE---IPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIekqptkeiakkmAILPQTAEVPTGLTVFELV 98
Cdd:cd03237 15 LEVEggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SygrfPHQKGFGTLKeedyryiHWALEVT---GMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:cd03237 83 S----SITKDFYTHP-------YFKTEIAkplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 983475024 176 LEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKaGKLMKQGT 223
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGV 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-200 |
2.26e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.47 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVE---IPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeIAKKmailPQTAEVPTGLTVFELv 98
Cdd:PRK13409 355 LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK---------ISYK----PQYIKPDYDGTVEDL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 sygrfphqkgfgtLKE--EDYRYIHWALEVT---GMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMA 173
Cdd:PRK13409 421 -------------LRSitDDLGSSYYKSEIIkplQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*..
gi 983475024 174 HQLEVLNLLKKLNEEEGRTIVMVIHDL 200
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-233 |
2.54e-18 |
|
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: 81.38 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGlTVFELVSYGRfphqkgfgtlKEEDYRYIHWALEVTGMTEFANRPAE-----------ALSGGQRQRVWI 150
Cdd:cd03252 81 VLQENVLFNR-SIRDNIALAD----------PGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
...
gi 983475024 231 ETL 233
Cdd:cd03252 227 NGL 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-222 |
2.55e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 11 VGYNEGLiiDGLTVEIPEGKITTIIGPNGCGKST----LLKtasriLKAKKGTVYLDGKAIEKQPTKE---IAKKMAIL- 82
Cdd:PRK15134 296 VDHNVVV--KNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGEIWFDGQPLHNLNRRQllpVRHRIQVVf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 --PQTAEVPTgLTVFELVSYGRFPHQKGFgTLKEEDYRYIHWALEVTGMTEFANR-PAEaLSGGQRQRVWIAMALAQGTE 159
Cdd:PRK15134 369 qdPNSSLNPR-LNVLQIIEEGLRVHQPTL-SAAQREQQVIAVMEEVGLDPETRHRyPAE-FSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-237 |
2.85e-18 |
|
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: 84.61 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 10 SVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAE 87
Cdd:TIGR00957 1291 CLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGLTVFELvsygrfphqKGFGTLKEEDyryIHWALEVTGMTEF-ANRPA----------EALSGGQRQRVWIAMALAQ 156
Cdd:TIGR00957 1371 LFSGSLRMNL---------DPFSQYSDEE---VWWALELAHLKTFvSALPDkldhecaeggENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 157 GTELLVLDEPTTYLDmahqLEVLNLLKKL--NEEEGRTIVMVIHDLNHASRFSdHMIALKAGKLMKQGTPDEVMTSetlR 234
Cdd:TIGR00957 1439 KTKILVLDEATAAVD----LETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ---R 1510
|
...
gi 983475024 235 SVF 237
Cdd:TIGR00957 1511 GIF 1513
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-215 |
3.73e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 11 VGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTaev 88
Cdd:PRK10247 13 VGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 PT--GLTVFE-LVsygrFPHQ-KGfgtlKEEDYRYIHWALEVTGMTE-FANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:PRK10247 90 PTlfGDTVYDnLI----FPWQiRN----QQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHD---LNHAsrfsDHMIALKA 215
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDkdeINHA----DKVITLQP 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-201 |
7.80e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.46 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAILP 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVsygRFPHQKGFGTLKEEdyryihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:cd03231 80 HAPGIKTTLSVLENL---RFWHADHSDEQVEE-------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLN 201
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLG 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
8.23e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.81 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGL-IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE--IAk 77
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 78 kM-----AILPQtaevptgLTVFELVSYGrfphQKGFGTLKEE-DYRYIHWA--LEVTGMTEfaNRPAEaLSGGQRQRVw 149
Cdd:PRK11650 80 -MvfqnyALYPH-------MSVRENMAYG----LKIRGMPKAEiEERVAEAAriLELEPLLD--RKPRE-LSGGQRQRV- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 iAM--ALAQGTELLVLDEPTTYLD----MAHQLEvlnlLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGT 223
Cdd:PRK11650 144 -AMgrAIVREPAVFLFDEPLSNLDaklrVQMRLE----IQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
....
gi 983475024 224 PDEV 227
Cdd:PRK11650 219 PVEV 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-252 |
3.29e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-ASRILKAKK--GTVYLDGKAIEKqptKEIAKKMAILPQ-TAEVPTgLT 93
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNAlAFRSPKGVKgsGSVLLNGMPIDA---KEMRAISAYVQQdDLFIPT-LT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVSYG---RFPHQkgfgTLKEEDYRYIHWALEVTGMTEFAN------RPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:TIGR00955 116 VREHLMFQahlRMPRR----VTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 165 EPTTYLD--MAHQleVLNLLKKLnEEEGRTIVMVIHD-LNHASRFSDHMIALKAGKLMKQGTPDEvmtsetLRSVFeieA 241
Cdd:TIGR00955 192 EPTSGLDsfMAYS--VVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ------AVPFF---S 259
|
250
....*....|..
gi 983475024 242 QI-VPCPVNCKP 252
Cdd:TIGR00955 260 DLgHPCPENYNP 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-200 |
3.69e-17 |
|
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: 80.60 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 28 EGKITTIIGPNGCGKSTLLKTAS-----------------RILKAKKGTV---YLdgkaiEKQPTKEIakKMAILPQ--- 84
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgelkpnlgdydeepswdEVLKRFRGTElqdYF-----KKLANGEI--KVAHKPQyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 -TAEVPTGlTVFELvsygrfphqkgfgtLKEEDYRYIhwALEVT---GMTEFANRPAEALSGGQRQRVWIAMALAQGTEL 160
Cdd:COG1245 171 lIPKVFKG-TVREL--------------LEKVDERGK--LDELAeklGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 983475024 161 LVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDL 200
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDL 272
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
140-230 |
3.93e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.56 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 140 LSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLM 219
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
90
....*....|.
gi 983475024 220 KQGTPDEVMTS 230
Cdd:COG4170 239 ESGPTEQILKS 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-223 |
4.29e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 13 YNEGLI----IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK----KMAILPQ 84
Cdd:PRK11629 15 YQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVPTGLTVFELVSygrFPHQKGfGTLKEEDYRYIHWALEVTGMTEFAN-RPAEaLSGGQRQRVWIAMALAQGTELLVL 163
Cdd:PRK11629 95 FHHLLPDFTALENVA---MPLLIG-KKKPAEINSRALEMLAAVGLEHRANhRPSE-LSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSdHMIALKAGKLMKQGT 223
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-223 |
6.02e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqPTKEIAKKMAILPQTaevpTGLtVFElvSYG 101
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDF-SQKPSEKAIRLLRQK----VGM-VFQ--QYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 RFPHQ-----------KGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL 170
Cdd:COG4161 93 LWPHLtvmenlieapcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 983475024 171 DMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGT 223
Cdd:COG4161 173 DPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-219 |
6.09e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK-----------KMAILP--- 83
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfgfifqRYHLLShlt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 --QTAEVPTgltVFElvsygrfphqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:PRK10535 103 aaQNVEVPA---VYA-------------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRfSDHMIALKAGKLM 219
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-216 |
6.92e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 76.99 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEI-AKKMAILPQTAEVPTGL--TVF 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYSVAYAAQKPWLLnaTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRfPHQKgfgtlkeEDYRYIHWA---------LEVTGMTEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:cd03290 97 ENITFGS-PFNK-------QRYKAVTDAcslqpdidlLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 167 TTYLD--MAHQLEVLNLLKKLNEEEgRTIVMVIHDLNHASRfSDHMIALKAG 216
Cdd:cd03290 168 FSALDihLSDHLMQEGILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-234 |
8.30e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 8.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK-KMAILPQTAEVPTGLTVFEL 97
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRFPHQKGFGtLKEEDYRYIHWALEV----TGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL--- 170
Cdd:PRK09700 101 LYIGRHLTKKVCG-VNIIDWREMRVRAAMmllrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnk 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 171 DMAHQLEVLNLLKKlneeEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLR 234
Cdd:PRK09700 180 EVDYLFLIMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-200 |
8.76e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 28 EGKITTIIGPNGCGKSTLLK-----------------TASRILKAKKGTV---YLdgkaiEKQPTKEIakKMAILPQTAE 87
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKilsgelipnlgdyeeepSWDEVLKRFRGTElqnYF-----KKLYNGEI--KVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 -VPTGL--TVFELvsygrfphqkgfgtLKEEDYRYIHWAL-EVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:PRK13409 171 lIPKVFkgKVREL--------------LKKVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDL 200
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEHDL 271
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-227 |
9.51e-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: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEglIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTasrIL-----KAKKGTVYLDGKAIEKQPTKEIAKK-MAIL 82
Cdd:cd03217 8 VSVGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKT---IMghpkyEVTEGEILFKGEDITDLPPEERARLgIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQT-AEVPtGLTVFELVsygrfphqkgfgtlkeedyRYIHwalevtgmtefanrpaEALSGGQRQRVWIAMALAQGTELL 161
Cdd:cd03217 83 FQYpPEIP-GVKNADFL-------------------RYVN----------------EGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVihdlNHASRFSDHMIA-----LKAGKLMKQGTPDEV 227
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLII----THYQRLLDYIKPdrvhvLYDGRIVKSGDKELA 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-232 |
1.02e-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: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYL--------------DGKAIEKQptkeiakKMAILPQ 84
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpDGRGRAKR-------YIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 taevptgltvfelvSYGRFPHQKGFGTL---------KEEDYRYIHWALEVTGMTE-----FANRPAEALSGGQRQRVWI 150
Cdd:TIGR03269 373 --------------EYDLYPHRTVLDNLteaiglelpDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 151 AMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
..
gi 983475024 231 ET 232
Cdd:TIGR03269 519 LT 520
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-217 |
1.06e-16 |
|
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: 76.35 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTasrIL---KAKKGTVYLDGKaiekqptkeiakkMAILPQTAEVPTGlTV 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSA---LLgelEKLSGSVSVPGS-------------IAYVSQEPWIQNG-TI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 95 FELVSYGRfphqkgfgTLKEEDYRYihwALEVTG------------MTEFANRPAeALSGGQRQRVWIAMALAQGTELLV 162
Cdd:cd03250 83 RENILFGK--------PFDEERYEK---VIKACAlepdleilpdgdLTEIGEKGI-NLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 163 LDEPTTYLDM---AHQLE--VLNLLKKlneeeGRTIVMVIHDLNHASRFsDHMIALKAGK 217
Cdd:cd03250 151 LDDPLSAVDAhvgRHIFEncILGLLLN-----NKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-232 |
1.88e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.86 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTA 86
Cdd:PLN03232 1240 VHLRYRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 87 EVPTGLTVFELvsyGRFPHQKGFGTLKEEDYRYIHWALEVT--GMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:PLN03232 1320 VLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 165 EPTTYLDmahqLEVLNLLKKLNEEEGRTIVMVI--HDLNHASRfSDHMIALKAGKLMKQGTPDEVMTSET 232
Cdd:PLN03232 1397 EATASVD----VRTDSLIQRTIREEFKSCTMLViaHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-200 |
2.41e-16 |
|
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: 76.25 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 28 EGKITTIIGPNGCGKSTLLKTASRILKAKKGTV-----------YLDGKAIEKQPTKEIAKKM--AILPQTA-EVPTGL- 92
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVkvIVKPQYVdLIPKAVk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 93 -TVFELVSygrfphqkgfgtlKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:cd03236 105 gKVGELLK-------------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|....*....
gi 983475024 172 MAHQLEVLNLLKKLNeEEGRTIVMVIHDL 200
Cdd:cd03236 172 IKQRLNAARLIRELA-EDDNYVLVVEHDL 199
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-218 |
3.39e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA---KKMAILPQTAEVPTGLTVF 95
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPHqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ 175
Cdd:PRK10908 98 DNVAIPLIIA----GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 983475024 176 LEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK10908 174 EGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-212 |
3.68e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLdGKAIekqptkeiakKMAILPQT 85
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 AEVPTG-LTVFELVSYGrfphqkgfgtlkeEDYryihwaLEVtGMTEFANR---------------PAEALSGGQRQRVW 149
Cdd:TIGR03719 394 RDALDPnKTVWEEISGG-------------LDI------IKL-GKREIPSRayvgrfnfkgsdqqkKVGQLSGGERNRVH 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDmahqLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIA 212
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILA 512
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
21-227 |
4.36e-16 |
|
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: 77.75 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 21 GLTVEIPEGKITTIIGPNGCGKSTLL-----KTASRILKAKKGT----------------VYLDGKAIEKQP-------T 72
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLIndtlyPALANRLNGAKTVpgrytsieglehldkvIHIDQSPIGRTPrsnpatyT 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 73 K---EIAKKMAILPQTAEvpTGLTV--FEL-VSYGRFPHQKGFGTLKEEDY---------------RYIHWALEVT---- 127
Cdd:TIGR00630 706 GvfdEIRELFAETPEAKV--RGYTPgrFSFnVKGGRCEACQGDGVIKIEMHflpdvyvpcevckgkRYNRETLEVKykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 128 ------GMTE------FAN----------------------RPAEALSGGQRQRVWIAMAL---AQGTELLVLDEPTTYL 170
Cdd:TIGR00630 784 niadvlDMTVeeayefFEAvpsisrklqtlcdvglgyirlgQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 171 ---DMAHQLEVLNLLKklneEEGRTIVMVIHDLnHASRFSDHMIAL------KAGKLMKQGTPDEV 227
Cdd:TIGR00630 864 hfdDIKKLLEVLQRLV----DKGNTVVVIEHNL-DVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-216 |
4.50e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVG-YNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLdgkaiekqPTKEiakKMA 80
Cdd:COG4178 361 GALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGA---RVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTGlTVFELVSYgrfPHQKGfgTLKEEDYRYihwALEVTGMTEFANRPAEA------LSGGQRQRVWIAMAL 154
Cdd:COG4178 430 FLPQRPYLPLG-TLREALLY---PATAE--AFSDAELRE---ALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 155 AQGTELLVLDEPTTYLDMAHQLEVLNLLKKlnEEEGRTIVMVIHdlnHAS--RFSDHMIALKAG 216
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH---RSTlaAFHDRVLELTGD 559
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-204 |
5.55e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 20 DGLTVEIPEGKITTIIGPNGCGKSTLLktasRIL----KAKKGTVYLDGKAIEKQPTkEIAKKMAILPQTAEVPTGLTVF 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLL----RILaglaRPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 E-LVSYgrfphQKGFGTLKEEDyryIHWALEVTGMTEFANRPAEALSGGQRQRVwiamALA----QGTELLVLDEPTTYL 170
Cdd:PRK13538 93 EnLRFY-----QRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRV----ALArlwlTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 983475024 171 DMA--HQLEVLnLLKKLneEEGRTIVMVIH-DLNHAS 204
Cdd:PRK13538 161 DKQgvARLEAL-LAQHA--EQGGMVILTTHqDLPVAS 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-228 |
9.23e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 15 EGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-ASRILKAK-KGTVYLDGKaiekQPTKEIAKKMAILPQTAEVPTGL 92
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAlAGRIQGNNfTGTILANNR----KPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 93 TVFE---LVSYGRFPHQkgfgTLKEEDYRYIHWALEVTGMTE-----FANRPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:PLN03211 156 TVREtlvFCSLLRLPKS----LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 165 EPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHdlNHASR---FSDHMIALKAGKLMKQGTPDEVM 228
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH--QPSSRvyqMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-230 |
9.47e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.47 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVyldgKAIEKqptkeiaKKMAILP 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSEN-------ANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 Q--TAEVPTGLTVFELVSYGRFPH---QKGFGTLkeedyryihwalevtGMTEF----ANRPAEALSGGQRQRVWIAMAL 154
Cdd:PRK15064 389 QdhAYDFENDLTLFDWMSQWRQEGddeQAVRGTL---------------GRLLFsqddIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 155 AQGTELLVLDEPTTYLDMaHQLEVLNL-LKKLneeEGrTIVMVIHDLNHASRFSDHMIALKAGKLMK-QGTPDEVMTS 230
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDM-ESIESLNMaLEKY---EG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-225 |
9.96e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.33 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTasrIL-----KAKKGTVYLDGKAIEKQPTKEIAKK 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV---LMghpkyEVTSGSILLDGEDILELSPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 ---MAiLPQTAEVPtGLTVFELV--SYG--RFPHQKGFGTLKEedyryIHWALEVTGM-TEFANRPA-EALSGGQRQRVW 149
Cdd:COG0396 78 gifLA-FQYPVEIP-GVSVSNFLrtALNarRGEELSAREFLKL-----LKEKMKELGLdEDFLDRYVnEGFSGGEKKRNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMALAQGTELLVLDEPTTYLDmahqLEVLNLL-KKLNE--EEGRTIVMVIH-----DLNHAsrfsDHMIALKAGKLMKQ 221
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD----IDALRIVaEGVNKlrSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVKS 222
|
....
gi 983475024 222 GTPD 225
Cdd:COG0396 223 GGKE 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-234 |
1.24e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 24 VEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIekqptKEIAKKMAILPQTAEVptGLtVFE---Lvsy 100
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL-----FDAEKGICLPPEKRRI--GY-VFQdarL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 101 grFPHQKGFGTL----KEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQL 176
Cdd:PRK11144 88 --FPHYKVRGNLrygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 177 EVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLR 234
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-228 |
1.75e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.81 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAK-KMAIL 82
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEaERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTA--------------EVPTGLTVFE-LVSYGrfphQKGFGTLKEEDyryIHWALEVtgmtEFA-----NRPAeALSG 142
Cdd:PRK11701 87 LRTEwgfvhqhprdglrmQVSAGGNIGErLMAVG----ARHYGDIRATA---GDWLERV----EIDaaridDLPT-TFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 143 GQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQG 222
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
....*.
gi 983475024 223 TPDEVM 228
Cdd:PRK11701 235 LTDQVL 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-237 |
3.13e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGLTVFEL 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 vsygrfphqKGFGTLKEEDYryihW-ALEVTGMTEFANRPA-----------EALSGGQRQRVWIAMALAQGTELLVLDE 165
Cdd:PLN03130 1334 ---------DPFNEHNDADL----WeSLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 166 PTTYLDMAHQLevlnLLKKLNEEEGRTIVMVI--HDLNHASRfSDHMIALKAGKLMKQGTPDEVMTSEtlRSVF 237
Cdd:PLN03130 1401 ATAAVDVRTDA----LIQKTIREEFKSCTMLIiaHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE--GSAF 1467
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-198 |
3.15e-15 |
|
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: 71.42 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLdgkaiekqPTKEiakKMAIL 82
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGE---DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 PQTAEVPTGlTVFELVSYgrfPhqkgfgtlkeedyryihWalevtgmtefanrpAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:cd03223 70 PQRPYLPLG-TLREQLIY---P-----------------W--------------DDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 983475024 163 LDEPTTYLDMAHQLEVLNLLKklneEEGRTIVMVIH 198
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-227 |
6.24e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY-NEGLIIDG---LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIA--- 76
Cdd:PRK10261 13 LAVENLNIAFmQEQQKIAAvrnLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 77 -----------KKMAIL---PQTAEVPTgLTVFELVSYGRFPHQkGFGtlKEEDYRYIHWALEVTGMTE---FANRPAEA 139
Cdd:PRK10261 93 qsaaqmrhvrgADMAMIfqePMTSLNPV-FTVGEQIAESIRLHQ-GAS--REEAMVEAKRMLDQVRIPEaqtILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 140 LSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLM 219
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 983475024 220 KQGTPDEV 227
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-171 |
6.98e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.00 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 6 VDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLdGKAIekqptkeiakKMAILPQT 85
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 AEvptGL----TVFELVSYGrfphqkgfgtlkeEDYryihwaLEVtGMTEFANR---------------PAEALSGGQRQ 146
Cdd:PRK11819 396 RD---ALdpnkTVWEEISGG-------------LDI------IKV-GNREIPSRayvgrfnfkggdqqkKVGVLSGGERN 452
|
170 180
....*....|....*....|....*
gi 983475024 147 RVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-226 |
7.44e-15 |
|
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: 74.09 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 2 ATLAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:COG5265 356 GEVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTaevpTGL---TVFELVSYGRfPhqkgfGTLKEEdyryIHWALEVTGMTEFANRPAEA-----------LSGGQRQ 146
Cdd:COG5265 436 IVPQD----TVLfndTIAYNIAYGR-P-----DASEEE----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQ 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 147 RVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLneEEGRTIVMVIHDLN---HAsrfsDHMIALKAGKLMKQGT 223
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLStivDA----DEILVLEAGRIVERGT 575
|
...
gi 983475024 224 PDE 226
Cdd:COG5265 576 HAE 578
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-233 |
7.71e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKkGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGlTVFELVSYG 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHG-TLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 102 RfPHqkgfgtLKEEDyryIHWALEVTGMTEFANRPAE-----------ALSGGQRQRVWIAMALAQGTELLVLDEPTTYL 170
Cdd:PRK11174 447 N-PD------ASDEQ---LQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 171 DMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PRK11174 517 DAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-223 |
1.10e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.89 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKMAILPQTAEVPTGLTVFE-L 97
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-ISDVHQNMGYCPQFDAIDDLLTGREhL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRFPhqkgfGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLE 177
Cdd:TIGR01257 2034 YLYARLR-----GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 983475024 178 VLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGT 223
Cdd:TIGR01257 2109 LWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-238 |
1.54e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 29 GKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVP-TGLTVFELVSYGRFPHQK 107
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPyASLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 108 GFGTLK-EEDYRYIHWALEVTGMT-EFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKL 185
Cdd:PRK10261 430 VHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 983475024 186 NEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPdevmtsetlRSVFE 238
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR---------RAVFE 553
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-225 |
1.87e-14 |
|
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: 70.75 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-----ASRIlkaKKGTVYLDGKAIEKQPTKEIAKK-MAILPQT-AEVPt 90
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTiaghpSYEV---TSGTILFKGQDLLELEPDERARAgLFLAFQYpEEIP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 GLTVFELV--SYGRFPHQKGFGTLKEEDYR-YIHWALEVTGMTE-FANRPA-EALSGGQRQRVWIAMALAQGTELLVLDE 165
Cdd:TIGR01978 91 GVSNLEFLrsALNARRSARGEEPLDLLDFEkLLKEKLALLDMDEeFLNRSVnEGFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 166 PTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHD---LNHASrfSDHMIALKAGKLMKQGTPD 225
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRL-REPDRSFLIITHYqrlLNYIK--PDYVHVLLDGRIVKSGDVE 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-217 |
1.99e-14 |
|
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: 72.55 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILK--AKKGTVYLDGKAIEKQPTKEI-AKKMAILPQTAEVPTGLTVF 95
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFAN-RPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAH 174
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 983475024 175 QLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:TIGR02633 177 TEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
3.99e-14 |
|
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: 68.61 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGynegLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAIL 82
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 83 P----QTAEVPtGLTVFELVSYGRFphqkgfgtlkeedyryihwalevtgmtefanrpaeaLSGGQRQRVWIAMALAQGT 158
Cdd:cd03215 81 PedrkREGLVL-DLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 159 ELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-216 |
8.47e-14 |
|
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: 68.04 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLL------KTASRIlkakKGTVYLDGKAIEKQPTKEI--AKKMAILPQTaevp 89
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLdvlagrKTAGVI----TGEILINGRPLDKNFQRSTgyVEQQDVHSPN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 90 tgLTVFElvsygrfphqkgfgtlkeedyryihwALEVTGmtefANRpaeALSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:cd03232 94 --LTVRE--------------------------ALRFSA----LLR---GLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 983475024 170 LDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNhASRFS--DHMIALKAG 216
Cdd:cd03232 139 LDSQAAYNIVRFLKKL-ADSGQAILCTIHQPS-ASIFEkfDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-229 |
1.02e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILK--AKKGTVYLDGKAIEKQPTKEIAKK-MAILPQTAEVPTGLTVF 95
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 96 ELVSYGRFPHQKGfgtlkeedyrYIHWA---------LEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:PRK13549 101 ENIFLGNEITPGG----------IMDYDamylraqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 167 TTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGK-----LMKQGTPDEVMT 229
Cdd:PRK13549 171 TASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRhigtrPAAGMTEDDIIT 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
28-230 |
1.26e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 28 EGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDG---------------KAIEKQPTKEIAKKMAIlPQTAEVPTGL 92
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqriRMIFQDPSTSLNPRQRI-SQILDFPLRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 93 TVfELVSygrfphqkgfgtlkEEDYRYIHWALEVTGM-TEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:PRK15112 117 NT-DLEP--------------EQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 172 MAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTS 230
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-229 |
2.02e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeiAKKMAILPQTAEVPTGLTVFELv 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQLTGIENIEL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 sygrfphqKGF--GTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPttyLDMAHQL 176
Cdd:PRK13545 109 --------KGLmmGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 177 EVLNLLKKLNE--EEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:PRK13545 178 FTKKCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-237 |
2.36e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 5 AVDAVSVgynegliidgltvEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEkqptkeiAKKMAI--- 81
Cdd:NF033858 281 AVDHVSF-------------RIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-------AGDIATrrr 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 ---LPQTAEVPTGLTV---FELvsygrfpHQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:NF033858 341 vgyMSQAFSLYGELTVrqnLEL-------HARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMTS---ET 232
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAArgaAT 492
|
....*
gi 983475024 233 LRSVF 237
Cdd:NF033858 493 LEEAF 497
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
140-230 |
4.24e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 140 LSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLM 219
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|.
gi 983475024 220 KQGTPDEVMTS 230
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-217 |
4.54e-13 |
|
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: 65.81 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTasrILKAKKGTVYLDG-KAIEKQPTKEIAKKMAIlpqtaeVPTGLtvfel 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE---GLYASGKARLISFlPKFSRNKLIFIDQLQFL------IDVGL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 vsygrfphqkGFGTLkeedyryihwalevtgmtefaNRPAEALSGGQRQRVWIAMALAQGTE--LLVLDEPTTYLDMAHQ 175
Cdd:cd03238 77 ----------GYLTL---------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 983475024 176 LEVLNLLKKLNeEEGRTIVMVIHDLNhASRFSDHMIAL--KAGK 217
Cdd:cd03238 126 NQLLEVIKGLI-DLGNTVILIEHNLD-VLSSADWIIDFgpGSGK 167
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-218 |
5.58e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAI----EKQPTKEIAKKMAILPQ 84
Cdd:PRK10584 16 VGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 T-AEVPTgLTVFELVsygRFPhqkgfGTLKEEDYRYIHWA----LEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTE 159
Cdd:PRK10584 96 SfMLIPT-LNALENV---ELP-----ALLRGESSRQSRNGakalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 160 LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKL 218
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-199 |
7.64e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTV---------YLDGKAIEKQPTKEIAKKMAILPQTAEV 88
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFDQHRAELDPEKTVMDNLAEGKQEVMV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 PtgltvfelvsyGRFPHQKGFgtlkeedyryihwalevtgMTEF------ANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:PRK11147 414 N-----------GRPRHVLGY-------------------LQDFlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190
....*....|....*....|....*....|....*..
gi 983475024 163 LDEPTTYLDmahqLEVLNLLKKLNEEEGRTIVMVIHD 199
Cdd:PRK11147 464 LDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-227 |
8.13e-13 |
|
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: 67.91 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLK----------TASRILK-----AKKGTVYLDGKAIE 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHvlrgmdqyepTSGRIIYhvalcEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 69 KQP--------------------TKEIAKKMAILPQ-TAEVPTGLTVFELVSygRFPHQKGFGTlKEEDYRyihwALEVT 127
Cdd:TIGR03269 81 PCPvcggtlepeevdfwnlsdklRRRIRKRIAIMLQrTFALYGDDTVLDNVL--EALEEIGYEG-KEAVGR----AVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 128 GMTEFANRP---AEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHAS 204
Cdd:TIGR03269 154 EMVQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 983475024 205 RFSDHMIALKAGKLMKQGTPDEV 227
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-224 |
1.31e-12 |
|
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: 66.10 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLL-----KTASRILKAKKGT----------------VYLDGKAIEKQP-------TK 73
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQpgnhdrieglehidkvIVIDQSPIGRTPrsnpatyTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 74 ----------EIAKKMAILPQTAEVP---------TGLTVFELVSYgrFPHQKGFG----TLKEEDYRYIHWAlevtgmt 130
Cdd:cd03271 94 vfdeirelfcEVCKGKRYNRETLEVRykgksiadvLDMTVEEALEF--FENIPKIArklqTLCDVGLGYIKLG------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 131 efanRPAEALSGGQRQRVWIAMAL---AQGTELLVLDEPTTYL---DMAHQLEVLNLLKklneEEGRTIVMVIHDLnHAS 204
Cdd:cd03271 165 ----QPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDVKKLLEVLQRLV----DKGNTVVVIEHNL-DVI 235
|
250 260
....*....|....*....|....*.
gi 983475024 205 RFSDHMIAL------KAGKLMKQGTP 224
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-228 |
1.44e-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: 67.66 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGkaiekqptkeiakKMAILPQTAEVPTGlTVFELV 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQND-SLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYGRfphqkgfgTLKEEDYRYIHWA------LEVT---GMTEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:TIGR00957 720 LFGK--------ALNEKYYQQVLEAcallpdLEILpsgDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 170 LDM---AHQLEvlNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVM 228
Cdd:TIGR00957 791 VDAhvgKHIFE--HVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-233 |
1.74e-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: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSV-GYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEI-AKKMAI 81
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQ----TAEVPtGLTVFE---LVSYGRFPHQKGfGTLkeeDYRYIH-WALEVtgMTEF------ANRPAEALSGGQRQR 147
Cdd:COG3845 338 IPEdrlgRGLVP-DMSVAEnliLGRYRRPPFSRG-GFL---DRKAIRaFAEEL--IEEFdvrtpgPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 148 VWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEV 227
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
....*.
gi 983475024 228 mTSETL 233
Cdd:COG3845 490 -TREEI 494
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-226 |
2.06e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.52 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 7 DAVSVGY-NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQT 85
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 86 AevptGL---TVFELVSYGRfphqkgfGTLKEEDyryIHWALEVTGMTEFANRPAE-----------ALSGGQRQRVWIA 151
Cdd:PRK13657 418 A----GLfnrSIEDNIRVGR-------PDATDEE---MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 152 MALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDE 555
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-211 |
2.14e-12 |
|
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: 63.75 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 25 EIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPtkeiakkmailpqtaevptgltvfelvsygrfp 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP--------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 105 hqkgfgtlkeedyRYIhwalevtgmtefanrpaeALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKK 184
Cdd:cd03222 68 -------------QYI------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*..
gi 983475024 185 LNEEEGRTIVMVIHDLNHASRFSDHMI 211
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-198 |
9.27e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-ASRILKA--KKGTVYLDGKAIEKQPTKEIAkkmAILPQTAEVPTgLTV 94
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVlAERVTTGviTGGDRLVNGRPLDSSFQRSIG---YVQQQDLHLPT-STV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 95 FELVSYGRFPHQKGFGTLKEEDyRYIHWALEVTGMTEFANR----PAEALSGGQRQRVWIAMALAQGTELLV-LDEPTTY 169
Cdd:TIGR00956 854 RESLRFSAYLRQPKSVSKSEKM-EYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180
....*....|....*....|....*....
gi 983475024 170 LDMAHQLEVLNLLKKLnEEEGRTIVMVIH 198
Cdd:TIGR00956 933 LDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-195 |
1.57e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 12 GYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-ASRILKAKK--GTVYLDGkaIEKQPTKEIAKKMAILPQTAEV 88
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlANRTEGNVSveGDIHYNG--IPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 --PTgLTVFELVSYgrfphqkgfgtlkeedyryihwALEVTGmtefaNRPAEALSGGQRQRVWIAMALAQGTELLVLDEP 166
Cdd:cd03233 94 hfPT-LTVRETLDF----------------------ALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180
....*....|....*....|....*....
gi 983475024 167 TTYLDMAHQLEVLNLLKKLNEEEGRTIVM 195
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-198 |
2.00e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqptkeiakkmailp 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 qtaevptgltvfELVSYGR----FPHQKGFG---TLKEEDYRYIHWALEVTGMTE---------FANRPAEALSGGQRQR 147
Cdd:PRK13540 68 ------------DLCTYQKqlcfVGHRSGINpylTLRENCLYDIHFSPGAVGITElcrlfslehLIDYPCGLLSSGQKRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 983475024 148 VWIAMALAQGTELLVLDEPTTYLDmahQLEVLNLLKKLNE--EEGRTIVMVIH 198
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALD---ELSLLTIITKIQEhrAKGGAVLLTSH 185
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-228 |
2.09e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.50 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGlTVFELVSYGRfphqkgfgtlkEEDY-RY-IHWALEVTGMTEFANRPAEA-----------LSGGQRQRV 148
Cdd:PRK11176 422 VSQNVHLFND-TIANNIAYAR-----------TEQYsREqIEEAARMAYAMDFINKMDNGldtvigengvlLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEegRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVM 228
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-229 |
2.70e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLtveIPEGKITTIIGPNGCGKSTLLKT-ASRI---LKAKKGTVYLDG---KAIEKQPTKEIakkmaILPQTAEVPTG 91
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCSTLLKTiASNTdgfHIGVEGVITYDGitpEEIKKHYRGDV-----VYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 -LTVFELVSYG---RFPHQKGFGTLKEE------DYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELL 161
Cdd:TIGR00956 152 hLTVGETLDFAarcKTPQNRPDGVSREEyakhiaDVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 162 VLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNH-ASRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-231 |
8.89e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 29 GKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEK-QPTKeiAKKMAI--LPQTAEVPTGLTVFELVSYGRFPH 105
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAK--AHQLGIylVPQEPLLFPNLSVKENILFGLPKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 106 QkgfgtlkeEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAhqlEVLNLLKKL 185
Cdd:PRK15439 115 Q--------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA---ETERLFSRI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 983475024 186 NE--EEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:PRK15439 184 REllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-198 |
9.96e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-----ASRILkakKGTVYLDGKAIEKQPTKEIAKK 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKViaghpAYKIL---EGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAIL----PqtAEVPtGLTVFELVSYGRFPHQKgFGTLKEED----YRYIHWALEVTGMTE-FANRPA-EALSGGQRQRV 148
Cdd:CHL00131 85 GIFLafqyP--IEIP-GVSNADFLRLAYNSKRK-FQGLPELDplefLEIINEKLKLVGMDPsFLSRNVnEGFSGGEKKRN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 149 WI-AMALAQgTELLVLDEPTTYLDM-AHQL--EVLNLLKKLNeeegRTIVMVIH 198
Cdd:CHL00131 161 EIlQMALLD-SELAILDETDSGLDIdALKIiaEGINKLMTSE----NSIILITH 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-185 |
1.03e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEkqpTKEIAKKMAILP 83
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 84 QTAEVPTGLTVFELVSY-----GRFPHQKGFGtlkeedyryihwALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGT 158
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcglhGRRAKQMPGS------------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPA 156
|
170 180
....*....|....*....|....*..
gi 983475024 159 ELLVLDEPTTYLDmahqLEVLNLLKKL 185
Cdd:PRK13543 157 PLWLLDEPYANLD----LEGITLVNRM 179
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-217 |
1.89e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEipEGKITTIIGPNGCGKSTLLKTASRILKAK--KGTVYLDGKAIEKQPTKE--------IAKKMAILPQtaevptg 91
Cdd:NF040905 22 LSVR--EGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDsealgiviIHQELALIPY------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 LTVFELVSYGRFPHQKGFgtlkeedyryIHWA---------LEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLV 162
Cdd:NF040905 93 LSIAENIFLGNERAKRGV----------IDWNetnrrarelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 163 LDEPTTYL---DMAHqleVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:NF040905 163 LDEPTAALneeDSAA---LLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-198 |
2.11e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 8 AVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKgtvyldGKAIEKQPTKEIAKKMAILPQTAE 87
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP------VAGCVDVPDNQFGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGLTVFELVsygrfpHQKGFGtlkeEDYRYIhwalevtgmtefanRPAEALSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:COG2401 109 KGDFKDAVELL------NAVGLS----DAVLWL--------------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|.
gi 983475024 168 TYLDMAHQLEVLNLLKKLNEEEGRTIVMVIH 198
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-199 |
3.09e-10 |
|
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: 58.39 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 31 ITTIIGPNGCGKSTLLKTASRIL--------------------KAKKGTVYLDGKAIEKQPTKeIAKKMAILPQTAevpt 90
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYALtgelppnskggahdpklireGEVRAQVKLAFENANGKKYT-ITRSLAILENVI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 91 gltvfelvsygrFPHQkgfgtlkEEdyryIHWALEvtgmtefanRPAEALSGGQRQ------RVWIAMALAQGTELLVLD 164
Cdd:cd03240 99 ------------FCHQ-------GE----SNWPLL---------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALD 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 983475024 165 EPTTYLDMAHQLEVL-NLLKKLNEEEGRTIVMVIHD 199
Cdd:cd03240 147 EPTTNLDEENIEESLaEIIEERKSQKNFQLIVITHD 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-218 |
4.44e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 29 GKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAILPQ--TAE--VPtGLTVFELVSYGRF 103
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEdrKAEgiIP-VHSVADNINISAR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 104 PHQKGFGTL----KEEDY--RYIHwALEVTgmTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLE 177
Cdd:PRK11288 358 RHHLRAGCLinnrWEAENadRFIR-SLNIK--TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 983475024 178 VLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK11288 435 IYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-233 |
4.80e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 28 EGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAILPQTAEvPTGL----TVFELVSYGR 102
Cdd:PRK09700 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESRR-DNGFfpnfSIAQNMAISR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 103 FPHQKGFGTL-----KEEDYRYIHWALEVTGMT-EFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQL 176
Cdd:PRK09700 367 SLKDGGYKGAmglfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKA 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 983475024 177 EVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PRK09700 447 EIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-231 |
6.21e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 58.38 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 26 IPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMAILPQTAEVPTGLTVFELVSYGRFPH 105
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 106 QKGFGTLKEEDYRYIHWALEvTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQlevlNLLKK- 184
Cdd:cd03288 124 DRLWEALEIAQLKNMVKSLP-GGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKv 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 983475024 185 -LNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMTSE 231
Cdd:cd03288 199 vMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-233 |
6.94e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 39 GCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAILP----QTAEVPtGLTVFE---LVSYGRFPHqKGFG 110
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVPedrkGEGLVL-DLSIREnitLASLDRLSR-GGLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 111 TLKEED---YRYIHwALEVTgmTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDM-AHQlEVLNLLKKLN 186
Cdd:COG1129 366 DRRRERalaEEYIK-RLRIK--TPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgAKA-EIYRLIRELA 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 983475024 187 eEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEvMTSETL 233
Cdd:COG1129 442 -AEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREE-ATEEAI 486
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
141-216 |
7.90e-10 |
|
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: 57.44 E-value: 7.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 141 SGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAG 216
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-199 |
1.13e-09 |
|
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: 58.41 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 27 PEGKITtIIGPNGCGKSTLLKTASRILKAkkgtvyLDGKAIekqPTKEIakKMAILPQTAEVPTGLTVFELVSYGrFPHQ 106
Cdd:TIGR03719 30 PGAKIG-VLGLNGAGKSTLLRIMAGVDKD------FNGEAR---PQPGI--KVGYLPQEPQLDPTKTVRENVEEG-VAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 107 KGfgTLKEEDYRYIHWALEVTGMTEFANR----------------------------------PAEALSGGQRQRVWIAM 152
Cdd:TIGR03719 97 KD--ALDRFNEISAKYAEPDADFDKLAAEqaelqeiidaadawdldsqleiamdalrcppwdaDVTKLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 983475024 153 ALAQGTELLVLDEPTTYLDMAhqlEVLNLLKKLNEEEGrTIVMVIHD 199
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPG-TVVAVTHD 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-218 |
2.13e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 34 IIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAiekqptkeiakKMAILPQTAEVPTGLTVFELVSYGR-FPhqkgfgTL 112
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAVFSQHHVDGLDLSSNPLLYMMRcFP------GV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 113 KEEDYRYIHWALEVTGmtEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAhqlEVLNLLKKLNEEEGrT 192
Cdd:PLN03073 603 PEQKLRAHLGSFGVTG--NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGLVLFQG-G 676
|
170 180
....*....|....*....|....*.
gi 983475024 193 IVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-218 |
2.80e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAK-KGTVYLDGKAIE-KQPTKEIAKKMAILPQTAE--------- 87
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKrhgivpilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGLTVFELVSY---GRFPHQKGFGTLKEEDYRyihwaLEVTGMTEFAnrPAEALSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:TIGR02633 356 VGKNITLSVLKSFcfkMRIDAAAELQIIGSAIQR-----LKVKTASPFL--PIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 165 EPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-233 |
3.13e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTA-SRILKAKKGTVYLDGKaiekqptkeiakkMAILPQTAEVPTGlTVFELVSY 100
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMlGELSHAETSSVVIRGS-------------VAYVPQVSWIFNA-TVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 101 GRfphqkgfgtlKEEDYRYihW-ALEVTGM------------TEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:PLN03232 702 GS----------DFESERY--WrAIDVTALqhdldllpgrdlTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 168 TYLD--MAHQleVLNLLKKlNEEEGRTIVMVIHDLnHASRFSDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PLN03232 769 SALDahVAHQ--VFDSCMK-DELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-223 |
3.52e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEG-LIIDGLTVEIPEGKITTIIGPNGCGKSTLlktASRIL---KAKKGTVYLDGKAIEKQPTKEIAKK 78
Cdd:PRK10790 340 RIDIDNVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAILPQTAEVPTGlTVFELVSYGRfphqkgfgTLKEEDYryihW-ALEVTGMTEFANRPAEA-----------LSGGQRQ 146
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTLGR--------DISEEQV----WqALETVQLAELARSLPDGlytplgeqgnnLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 147 RVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEeegRTIVMVIhdlnhASRFS-----DHMIALKAGKLMKQ 221
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE---HTTLVVI-----AHRLStiveaDTILVLHRGQAVEQ 555
|
..
gi 983475024 222 GT 223
Cdd:PRK10790 556 GT 557
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-235 |
3.84e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYldgkaiekqptkeIAKKMAILPQ-----TAEVPTGLTVFE 96
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQqawimNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 97 lvsygrfphqkgfgtlkEEDYRYIHWALEVT-----------GM-TEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLD 164
Cdd:PTZ00243 746 -----------------EEDAARLADAVRVSqleadlaqlggGLeTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983475024 165 EPTTYLDmAH--QLEVLNLLkkLNEEEGRTIVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEVMTS---ETLRS 235
Cdd:PTZ00243 808 DPLSALD-AHvgERVVEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTslyATLAA 879
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-246 |
4.30e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE-IAKKMAILPQTAEV-------PTGLT 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQSsglyldaPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 94 VFELVSygrfpHQKGFGTLKEEDY----RYiHWALEVTgmTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTY 169
Cdd:PRK15439 362 VCALTH-----NRRGFWIKPARENavleRY-RRALNIK--FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 170 LDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVMTSETLRSVF-EIEAQIVPC 246
Cdd:PRK15439 434 VDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFgEHQAQEASC 510
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-217 |
5.42e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKE-IAKKMAILPQTAEVPTGLTVFEL 97
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRFPhQKGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYL---DMAH 174
Cdd:PRK10982 94 MWLGRYP-TKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 983475024 175 QLEVLNLLKklneEEGRTIVMVIHDLNHASRFSDHMIALKAGK 217
Cdd:PRK10982 173 LFTIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-214 |
6.10e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.53 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 29 GKITTIIGPNGCGKSTLLKTASRILKAKKGTV-YLDGKAIEKQPTKEIAKkmailpqtaevptgltvfelvsygrfphqk 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 108 gfgtlkeedyryihwalevtgmtEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQ-----LEVLNLL 182
Cdd:smart00382 52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLL 108
|
170 180 190
....*....|....*....|....*....|....*...
gi 983475024 183 KKLNEEEGRTIVMVIHDLNH------ASRFSDHMIALK 214
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDlgpallRRRFDRRIVLLL 146
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
124-229 |
1.16e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 124 LEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHA 203
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEA 207
|
90 100
....*....|....*....|....*.
gi 983475024 204 SRFSDHMIALKAGKLMKQGTPDEVMT 229
Cdd:NF000106 208 EQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-245 |
1.78e-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: 55.02 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 134 NRPAEALSGGQRQRvwIAMALAQGTELL----VLDEPTTYLdmaHQ------LEVLNLLKKLneeeGRTIVMVIHDlNHA 203
Cdd:TIGR00630 483 SRAAGTLSGGEAQR--IRLATQIGSGLTgvlyVLDEPSIGL---HQrdnrrlINTLKRLRDL----GNTLIVVEHD-EDT 552
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 204 SRFSDHMIAL--KAGK----LMKQGTPDEVM------TSETLRSVFEIEaqiVP 245
Cdd:TIGR00630 553 IRAADYVIDIgpGAGEhggeVVASGTPEEILanpdslTGQYLSGRKKIE---VP 603
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
136-232 |
1.79e-08 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 55.08 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 136 PAEALSGGQRQRVWIAMAL---AQGTELLVLDEPTTYL---DMAHQLEVLNLLKklneEEGRTIVMVIHDLNhASRFSDH 209
Cdd:PRK00349 827 PATTLSGGEAQRVKLAKELskrSTGKTLYILDEPTTGLhfeDIRKLLEVLHRLV----DKGNTVVVIEHNLD-VIKTADW 901
|
90 100
....*....|....*....|....*....
gi 983475024 210 MIAL------KAGKLMKQGTPDEVMTSET 232
Cdd:PRK00349 902 IIDLgpeggdGGGEIVATGTPEEVAKVEA 930
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-251 |
2.77e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 135 RPAEALSGGQRQRVWIAMALAQGTE---LLVLDEPTTYL---DMAHQLEVLNLLKklneEEGRTIVMVIHDLnHASRFSD 208
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLhthDIKALIYVLQSLT----HQGHTVVIIEHNM-HVVKVAD 879
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 983475024 209 HMIAL------KAGKLMKQGTPDEVM-----TSETLRSVFEIEAQIVPCPVNCK 251
Cdd:PRK00635 880 YVLELgpeggnLGGYLLASCSPEELIhlhtpTAKALRPYLSSPQELPYLPDPSP 933
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-199 |
2.79e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLdGKAI---------------E 68
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIklgyfaqhqleflraD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 69 KQPTKEIAKkmaILPQTAEVptgltvfELVSYgrfphQKGFGTLKEEdyryihwalevtgMTEfanrPAEALSGGQRQRV 148
Cdd:PRK10636 392 ESPLQHLAR---LAPQELEQ-------KLRDY-----LGGFGFQGDK-------------VTE----ETRRFSGGEKARL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLDMAHQLEvlnLLKKLNEEEGrTIVMVIHD 199
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQA---LTEALIDFEG-ALVVVSHD 486
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-214 |
2.97e-08 |
|
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: 51.98 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 14 NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRIL--KAKKGTVYLDGKAiekqptkeiakkmailpqTAEVPtg 91
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALggAQSATRRRSGVKA------------------GCIVA-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 ltvfelvsygrfphqkgfgtlkeedYRYIHWALEVTGmtefanrpaeaLSGGQRQRVWIAMALA----QGTELLVLDEPT 167
Cdd:cd03227 66 -------------------------AVSAELIFTRLQ-----------LSGGEKELSALALILAlaslKPRPLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 983475024 168 TYLDMAHQLEVLNLLKKLNEEEGRTIVmVIHDLNHAsRFSDHMIALK 214
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELA-ELADKLIHIK 154
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-231 |
3.04e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 54.26 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 136 PAEALSGGQRQRVWIAMALA---QGTELLVLDEPTTYL---DMAHQLEVLNLLKklneEEGRTIVMVIHDL----Nhasr 205
Cdd:COG0178 823 PATTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIRKLLEVLHRLV----DKGNTVVVIEHNLdvikT---- 894
|
90 100 110
....*....|....*....|....*....|..
gi 983475024 206 fSDHMIAL------KAGKLMKQGTPDEVMTSE 231
Cdd:COG0178 895 -ADWIIDLgpeggdGGGEIVAEGTPEEVAKVK 925
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-226 |
3.17e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.95 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGY--NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:PRK10789 313 ELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTGlTVFELVSYGR-------FPHQKGFGTLKEEDYRyihwaLEVTGMTEFANRpAEALSGGQRQRVWIAMA 153
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNIALGRpdatqqeIEHVARLASVHDDILR-----LPQGYDTEVGER-GVMLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 154 LAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeeEGRTIVMVIHDLNhASRFSDHMIALKAGKLMKQGTPDE 226
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWG--EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQ 535
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-171 |
3.67e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKkGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:cd03289 3 MTVKDLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYGRFPHQK--------GFGTLKEEDYRYIHWALEVTGMTefanrpaeaLSGGQRQRVWIAMA 153
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEiwkvaeevGLKSVIEQFPGQLDFVLVDGGCV---------LSHGHKQLMCLARS 152
|
170
....*....|....*...
gi 983475024 154 LAQGTELLVLDEPTTYLD 171
Cdd:cd03289 153 VLSKAKILLLDEPSAHLD 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-199 |
1.15e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 27 PEGKITtIIGPNGCGKSTLLktasRILkAKKGTVYlDGKAIekqPTKEIakKMAILPQTAEVPTGLTVFELVsygrfphQ 106
Cdd:PRK11819 32 PGAKIG-VLGLNGAGKSTLL----RIM-AGVDKEF-EGEAR---PAPGI--KVGYLPQEPQLDPEKTVRENV-------E 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 107 KGFG----TLKEEDYRYIHWALEVTGMTEFANR------------------------------PAEA----LSGGQRQRV 148
Cdd:PRK11819 93 EGVAevkaALDRFNEIYAAYAEPDADFDALAAEqgelqeiidaadawdldsqleiamdalrcpPWDAkvtkLSGGERRRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 149 WIAMALAQGTELLVLDEPTTYLDMahqlE-VLNLLKKLNEEEGrTIVMVIHD 199
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDA----EsVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-231 |
1.24e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 138 EALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHDLNHASRfSDHMIAL---- 213
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpd 1435
|
90
....*....|....*....
gi 983475024 214 KAGKLMK-QGTPDEVMTSE 231
Cdd:PTZ00265 1436 RTGSFVQaHGTHEELLSVQ 1454
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-231 |
1.35e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.34 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 134 NRPAEALSGGQRQRVWIAMALaqGTELL----VLDEPTTYL---DMAHQLEVLNLLKKLneeeGRTIVMVIHDLNhASRF 206
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQI--GSGLVgvlyVLDEPSIGLhqrDNDRLIETLKRLRDL----GNTVIVVEHDED-TIRA 552
|
90 100 110
....*....|....*....|....*....|.
gi 983475024 207 SDHMIAL--KA----GKLMKQGTPDEVMTSE 231
Cdd:COG0178 553 ADYIIDIgpGAgehgGEVVAQGTPEEILKNP 583
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-218 |
1.79e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGY-NEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEkqptkeIAKKMAI 81
Cdd:PRK10522 322 TLELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------AEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFElvsygRFPHQKGFGTLKEedyRYIHWaLEVTGMTE--------FANRpaeALSGGQRQRVWIAMA 153
Cdd:PRK10522 396 RKLFSAVFTDFHLFD-----QLLGPEGKPANPA---LVEKW-LERLKMAHkleledgrISNL---KLSKGQKKRLALLLA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 154 LAQGTELLVLDEPTtyldmAHQ---------LEVLNLLKklneEEGRTIVMVIHDlNHASRFSDHMIALKAGKL 218
Cdd:PRK10522 464 LAEERDILLLDEWA-----ADQdphfrrefyQVLLPLLQ----EMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-233 |
1.98e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 24 VEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKgtvylDGKAIekqptkeIAKKMAILPQTAEVPTGlTVFELVSYGrf 103
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-----DASVV-------IRGTVAYVPQVSWIFNA-TVRDNILFG-- 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 104 phqkgfgtLKEEDYRYiHWALEVTGM------------TEFANRPAEaLSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:PLN03130 703 --------SPFDPERY-ERAIDVTALqhdldllpggdlTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983475024 172 MAHQLEVLNLLKKlNEEEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQGTPDEVMTSETL 233
Cdd:PLN03130 773 AHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGPL 832
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-201 |
2.49e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYL-DGKAIEKQPTKEIAKKMAILPQ-----TAEVPTG 91
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQdpllfSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 92 L-----TVFELVSYGRFPHQKGFGTLKEEDYRYIHWALEVTGMTEFANRP------------------------------ 136
Cdd:PTZ00265 480 IkyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTdsneliemrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 137 -----------------AEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHD 199
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
..
gi 983475024 200 LN 201
Cdd:PTZ00265 640 LS 641
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-171 |
7.24e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEG--LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILkAKKGTVYLDGKAIEKQPTKEIAKKMAI 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 82 LPQTAEVPTGLTVFELVSYGRFPHQK--------GFGTLKEEDYRYIHWALEVTGMTefanrpaeaLSGGQRQRVWIAMA 153
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQWSDEEiwkvaeevGLKSVIEQFPDKLDFVLVDGGYV---------LSNGHKQLMCLARS 1367
|
170
....*....|....*...
gi 983475024 154 LAQGTELLVLDEPTTYLD 171
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD 1385
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-222 |
8.06e-07 |
|
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: 48.79 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 22 LTVEIPEGKITTIIGPNGCGKSTL----------------LKTASRILKAKKGTVYLDgkAIEK-QPTKEIAKKmailpQ 84
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARQFLGQMDKPDVD--SIEGlSPAIAIDQK-----T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 85 TAEVP--TGLTVFELVSYGRFPHQK-GfgtLKEEDYRYIHWALEVTGMtefaNRPAEALSGGQRQRVWIAMALAQG-TEL 160
Cdd:cd03270 87 TSRNPrsTVGTVTEIYDYLRLLFARvG---IRERLGFLVDVGLGYLTL----SRSAPTLSGGEAQRIRLATQIGSGlTGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983475024 161 L-VLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNhASRFSDHMIAL------KAGKLMKQG 222
Cdd:cd03270 160 LyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDED-TIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-248 |
8.48e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 134 NRPAEALSGGQRQRVWIAMALaqGTELL----VLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASrFSDH 209
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMIS-LADR 546
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 983475024 210 MI------ALKAGKLMKQGTPDE-VMTSETLRSVFEIEAQIVPCPV 248
Cdd:PRK00635 547 IIdigpgaGIFGGEVLFNGSPREfLAKSDSLTAKYLRQELTIPIPE 592
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-218 |
9.02e-07 |
|
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: 49.41 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 25 EIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQpTKEIAKKM--AIL---------------PQTAE 87
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD-NREAYRQLfsAVFsdfhlfdrllgldgeADPAR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 88 VPTGLTVFELvsygrfpHQKgfgtLKEEDYRyihwalevtgmteFANRpaeALSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:COG4615 433 ARELLERLEL-------DHK----VSVEDGR-------------FSTT---DLSQGQRKRLALLVALLEDRPILVFDEWA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 168 tyldmAHQ---------LEVLNLLKKlneeEGRTIVMVIHD---LNHAsrfsDHMIALKAGKL 218
Cdd:COG4615 486 -----ADQdpefrrvfyTELLPELKA----RGKTVIAISHDdryFDLA----DRVLKMDYGKL 535
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-199 |
9.38e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 17 LIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGK---AIEKQPT---------------KEIAKK 78
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETpalpqpaleyvidgdREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 79 MAILPQTAEVPTGLTVFELvsYGRFPHQKGFgTLKEEDYRYIHwalevtGM---TEFANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK10636 95 EAQLHDANERNDGHAIATI--HGKLDAIDAW-TIRSRAASLLH------GLgfsNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 983475024 156 QGTELLVLDEPTTYLDMAhqlEVLNLLKKLNEEEGrTIVMVIHD 199
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHD 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-218 |
1.25e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIE-KQPTKEIAKKMAILPQTAE---VPTGLTV 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 95 FELVSYGRFPH-QKGFGTLKEEDyryihwalEVTGMTEF----------ANRPAEALSGGQRQRVWIAMALAQGTELLVL 163
Cdd:PRK10762 348 KENMSLTALRYfSRAGGSLKHAD--------EQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 983475024 164 DEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-168 |
1.50e-06 |
|
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: 48.98 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAiekqptkeiakKMAILPQTAEVPTGlTVFEL 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFYVPQRPYMTLG-TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGRFPHQ---KGFG------TLKEEDYRYIhwaLEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTT 168
Cdd:TIGR00954 535 IIYPDSSEDmkrRGLSdkdleqILDNVQLTHI---LEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-227 |
2.08e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeiakkMAILPQTAEVPTGlTVFEL 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGrfphqkgfgtLKEEDYRY---IHWALEVTGMTEFANRPAE-------ALSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:TIGR01271 507 IIFG----------LSYDEYRYtsvIKACQLEEDIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 168 TYLDMAHQLEVL-NLLKKLNEEEGRtiVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEV 227
Cdd:TIGR01271 577 THLDVVTEKEIFeSCLCKLMSNKTR--ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-233 |
2.53e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 3 TLAVDAVSVGYNEGL--IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEIAKKMA 80
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQTAEVPTGlTVFELVSygrfphqkgfgTLKEEDYRYIHWALEVTGMTEFANRPAEAL-----------SGGQRQRVW 149
Cdd:PTZ00243 1388 MIPQDPVLFDG-TVRQNVD-----------PFLEASSAEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMC 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 150 IAMA-LAQGTELLVLDEPTTYLDMAHQLEVLNLLkkLNEEEGRTIVMVIHDLNHASRFsDHMIALKAGKLMKQGTPDE-V 227
Cdd:PTZ00243 1456 MARAlLKKGSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRElV 1532
|
....*.
gi 983475024 228 MTSETL 233
Cdd:PTZ00243 1533 MNRQSI 1538
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-228 |
2.68e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 19 IDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeiakkMAILPQTAEVPTGLTVFELV 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 99 SYGRFphqkGFGTLKEEDYRYIHWALEVTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPttyLDMAHQLEV 178
Cdd:PRK13546 107 EFKML----CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA---LSVGDQTFA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 179 LNLLKKLNE--EEGRTIVMVIHDLNHASRFSDHMIALKAGKLMKQGTPDEVM 228
Cdd:PRK13546 180 QKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-227 |
2.93e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.54 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKaiekqptkeiakkMAILPQTAEVPTGlTVFEL 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 98 VSYGrfphqkgfgtLKEEDYRY------IHWALEVTGMTEFANRP-AEA---LSGGQRQRVWIAMALAQGTELLVLDEPT 167
Cdd:cd03291 118 IIFG----------VSYDEYRYksvvkaCQLEEDITKFPEKDNTVlGEGgitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983475024 168 TYLDMAHQLEVL-NLLKKLNEEEGRtiVMVIHDLNHASRfSDHMIALKAGKLMKQGTPDEV 227
Cdd:cd03291 188 GYLDVFTEKEIFeSCVCKLMANKTR--ILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-236 |
3.59e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 128 GMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLNeEEGRTIVMVIHDLNHASRFS 207
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFV 202
|
90 100 110
....*....|....*....|....*....|....*...
gi 983475024 208 DHMIALKAGKLMKQGTPDEVMT---------SETLRSV 236
Cdd:PRK10938 203 QFAGVLADCTLAETGEREEILQqalvaqlahSEQLEGV 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-218 |
6.40e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 18 IIDGLTVEIPEGKITTIIGPNGCGKSTLlktASRILKA----KKGTVYLDGKAIE-KQPTKEIAKKMAILPQTAE----V 88
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTEL---VQCLFGAypgrWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDRKrdgiV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 PTgLTVFE---LVSYGRFphqKGFGTLKEedyryihwALEVTGMTEFANR----------PAEALSGGQRQRVWIAMALA 155
Cdd:PRK13549 354 PV-MGVGKnitLAALDRF---TGGSRIDD--------AAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMVIHDLNHASRFSDHMIALKAGKL 218
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-198 |
6.55e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 29 GKITTIIGPNGCGKSTLLKtasrILKAKKGTVYLDGKA-IEKQPTKE--IAKKMAILPQTAEVPTGLTVFELVSYG---R 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMD----VLAGRKTGGYIEGDIrISGFPKKQetFARISGYCEQNDIHSPQVTVRESLIYSaflR 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 103 FPHQKGfgtlKEEDYRYIHWALEVTGMTEFANR----PA-EALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLE 177
Cdd:PLN03140 982 LPKEVS----KEEKMMFVDEVMELVELDNLKDAivglPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180
....*....|....*....|.
gi 983475024 178 VLNLLKKlNEEEGRTIVMVIH 198
Cdd:PLN03140 1058 VMRTVRN-TVDTGRTVVCTIH 1077
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
134-231 |
7.91e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 134 NRPAEALSGGQRQRVWIAmalaqgTE--------LLVLDEPTTYLdmaHQ---LEVLNLLKKLnEEEGRTIVMVIHDLNh 202
Cdd:PRK00349 484 SRSAGTLSGGEAQRIRLA------TQigsgltgvLYVLDEPSIGL---HQrdnDRLIETLKHL-RDLGNTLIVVEHDED- 552
|
90 100 110
....*....|....*....|....*....|....*
gi 983475024 203 ASRFSDHMIAL--KA----GKLMKQGTPDEVMTSE 231
Cdd:PRK00349 553 TIRAADYIVDIgpGAgvhgGEVVASGTPEEIMKNP 587
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-233 |
8.93e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 35 IGPNGCGKSTLLKTASRILKAKKGTVYLDgkaiekqPTKeiakKMAILPQTAEVPTGLTVFELVSYGrfpHQKGFGTLKE 114
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNE----RLGKLRQDQFAFEEFTVLDTVIMG---HTELWEVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 115 EDYRYihwAL-EVT---GM------TEFA--------NRPAEALSG-----------------GQRQRVWIAMALAQGTE 159
Cdd:PRK15064 99 RDRIY---ALpEMSeedGMkvadleVKFAemdgytaeARAGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 160 LLVLDEPTTYLDMA--HQLE-VLNllkklneeeGRTIVMVI--HDLNHASRFSDHMIALKAGKL-MKQGTPDEVMTSETL 233
Cdd:PRK15064 176 ILLLDEPTNNLDINtiRWLEdVLN---------ERNSTMIIisHDRHFLNSVCTHMADLDYGELrVYPGNYDEYMTAATQ 246
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-171 |
1.45e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLktaSRIlkakkgtvyldgkaiekqptkeiakkmailpqTAEV 88
Cdd:PRK10938 266 GVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL---SLI--------------------------------TGDH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 89 PTG----LTVFelvsyGRfphQKGFGT----LKEE----------DYRY-----------------IHWA---------- 123
Cdd:PRK10938 311 PQGysndLTLF-----GR---RRGSGEtiwdIKKHigyvssslhlDYRVstsvrnvilsgffdsigIYQAvsdrqqklaq 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 983475024 124 --LEVTGMTE-FANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLD 171
Cdd:PRK10938 383 qwLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-218 |
1.62e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 1 MATLAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKTASrilkakkGTVYLD-GKAIEKQPTKeiakkM 79
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEQDLI-----V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 80 AILPQTAEVPTGLTVFELVS------------YGRFPHQ----------KGFGTLKEE---------DYRyIHWALEVTG 128
Cdd:PRK11147 69 ARLQQDPPRNVEGTVYDFVAegieeqaeylkrYHDISHLvetdpseknlNELAKLQEQldhhnlwqlENR-INEVLAQLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 129 MTefANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDmahqLEVLNLLKKLNEEEGRTIVMVIHDLNHASRFSD 208
Cdd:PRK11147 148 LD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMAT 221
|
250
....*....|
gi 983475024 209 HMIALKAGKL 218
Cdd:PRK11147 222 RIVDLDRGKL 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-222 |
7.92e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 4 LAVDAVSVGYNEGLIIDGLTVEIPEGKITTIIGPNGCGKSTLLKT-ASR-ILKAKKGTVYLDGKAI-EKQPTKEIAKKMA 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATlAGReDYEVTGGTVEFKGKDLlELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 81 ILPQ-TAEVPTGLTVFEL-VSYGRFPHQKGFGTLKEEDYR-YIHWALEVTGMTE--FANRPAEALSGGQRQRVWIAMALA 155
Cdd:PRK09580 82 MAFQyPVEIPGVSNQFFLqTALNAVRSYRGQEPLDRFDFQdLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 156 QGTELLVLDEPTTYLDMAHQLEVLNLLKKLNEEEgRTIVMVIHD---LNHASrfSDHMIALKAGKLMKQG 222
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSG 228
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-46 |
9.63e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 9.63e-05
10 20 30
....*....|....*....|....*....|....
gi 983475024 13 YNEGLIiDGLTVEIPEGKITTIIGPNGCGKSTLL 46
Cdd:pfam13555 7 INWGTF-DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-182 |
1.19e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 31 ITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKqptkeIAKK-MAILPQTAEVPTGLTVFE-LVSYGRFPHQkg 108
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----IAKPyCTYIGHNLGLKLEMTVFEnLKFWSEIYNS-- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 109 fgtlKEEDYRYIHWalevTGMTEFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLL 182
Cdd:PRK13541 101 ----AETLYAAIHY----FKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-47 |
4.20e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.14 E-value: 4.20e-04
10 20
....*....|....*....|....*....
gi 983475024 19 IDGLTVEIPEGkITTIIGPNGCGKSTLLK 47
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILE 41
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-199 |
5.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 5.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983475024 138 EALSGGQRQ------RVWIAMALAQGTE------LLVLDEPTTYLDMAHQLEVLNLLKKLNEEEGRTIVMVIHD 199
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEGIEgdaplpPLILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHD 853
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
23-43 |
5.70e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.70e-04
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-196 |
6.93e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 6.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 983475024 139 ALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDMAHQLEVLNLLKKLnEEEGRTIVMV 196
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIII 447
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-172 |
7.55e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 9 VSVGYNEgLIIDGlTVEIPEGKITTIIGPNGCGKSTLLK-----------TASRILKAKKGTVYLDGKAIE------KQP 71
Cdd:PLN03073 185 ISVGGRD-LIVDA-SVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipKNCQILHVEQEVVGDDTTALQcvlntdIER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983475024 72 TKEIAKKMAILPQTAEVPtgltvfelvsygrFPHQKGFGTLKEED----------YRYIHWALE--------------VT 127
Cdd:PLN03073 263 TQLLEEEAQLVAQQRELE-------------FETETGKGKGANKDgvdkdavsqrLEEIYKRLElidaytaearaasiLA 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 983475024 128 GMT---EFANRPAEALSGGQRQRVWIAMALAQGTELLVLDEPTTYLDM 172
Cdd:PLN03073 330 GLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
23-43 |
7.74e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 7.74e-04
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-53 |
1.03e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....*.
gi 983475024 19 IDGLTVEIPEG-KITTIIGPNGCGKSTLLKTASRIL 53
Cdd:COG3950 14 FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIALAL 49
|
|
| PTZ00202 |
PTZ00202 |
tuzin; Provisional |
30-81 |
1.91e-03 |
|
tuzin; Provisional
Pssm-ID: 240312 Cd Length: 550 Bit Score: 39.38 E-value: 1.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 983475024 30 KITTIIGPNGCGKSTLLKTAsrILKAKKGTVYLDGKAIEkQPTKEIAKKMAI 81
Cdd:PTZ00202 287 RIVVFTGFRGCGKSSLCRSA--VRKEGMPAVFVDVRGTE-DTLRSVVKALGV 335
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
29-63 |
3.49e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 36.80 E-value: 3.49e-03
10 20 30
....*....|....*....|....*....|....*
gi 983475024 29 GKITTIIGPNGCGKSTLLKTASRILKAKKGTVYLD 63
Cdd:pfam13173 2 RKILVITGPRQVGKTTLLLQLIKELLPPENILYIN 36
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
24-46 |
3.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 3.51e-03
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
29-63 |
4.66e-03 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 37.33 E-value: 4.66e-03
10 20 30
....*....|....*....|....*....|....*.
gi 983475024 29 GKITTIIGPNGCGKSTL-LKTASRILKAKKGTVYLD 63
Cdd:cd01393 1 GKITEIYGPPGSGKTQLaLQLAANALLLGGGVVWID 36
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-75 |
8.05e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.98 E-value: 8.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 983475024 31 ITTIIGPNGCGKSTLLKTASRILKAKKGTVYLDGKAIEKQPTKEI 75
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGI 45
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
28-66 |
9.18e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 35.99 E-value: 9.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 983475024 28 EGKITTIIGPNGCGKSTLLKTASRILKAKKGTVYL---DGKA 66
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLaapTGKA 52
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
19-46 |
9.48e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.32 E-value: 9.48e-03
10 20
....*....|....*....|....*...
gi 983475024 19 IDGLTVEIPEGkITTIIGPNGCGKSTLL 46
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTIL 35
|
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