|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-261 |
1.64e-123 |
|
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: 352.81 E-value: 1.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLP 89
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVEADI 248
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|...
gi 2543669097 249 LRAPVDGSPVVVP 261
Cdd:COG1120 242 IEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-260 |
4.93e-99 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 290.76 E-value: 4.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLP 89
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVEADIL 249
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIH 242
|
250
....*....|.
gi 2543669097 250 RAPVDGSPVVV 260
Cdd:PRK11231 243 PEPVSGTPMCV 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-261 |
2.46e-89 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 266.18 E-value: 2.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSgqRQAAHRIALL 88
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVatTPS--RELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPH-QGLLrqwSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYsKGRL---TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVEA 246
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDI 237
|
250
....*....|....*
gi 2543669097 247 DILRapVDGSPVVVP 261
Cdd:COG4604 238 EVEE--IDGKRICVY 250
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-266 |
2.65e-87 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 261.46 E-value: 2.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 6 SPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRI 85
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTP 165
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGV 244
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
250 260
....*....|....*....|..
gi 2543669097 245 EADILRAPVDGSPVVVPRARTA 266
Cdd:PRK10253 244 RCMIIDDPVAGTPLVVPLGRTA 265
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-227 |
6.88e-78 |
|
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: 234.25 E-value: 6.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQ 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 91 sprapeavtvaglvrygrhphqgllrqwsraderavreALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLD 170
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 171 EPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-263 |
6.81e-76 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 231.93 E-value: 6.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQRqaAHRIAL 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaaWSPWEL--ARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYGRHPHQGLlrqwSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQ----- 162
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGSS----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 163 --QTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRS 240
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250 260
....*....|....*....|...
gi 2543669097 241 LYGVEADILRAPVDGSPVVVPRA 263
Cdd:COG4559 236 VYGADLRVLAHPEGGCPQVLPRA 258
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-250 |
2.50e-74 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 227.66 E-value: 2.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgqRQAAH 83
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEA--VTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMkDGEVVGEGAPRDTVDAELVRSL 241
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRA 234
|
....*....
gi 2543669097 242 YGVEADILR 250
Cdd:COG1121 235 YGGPVALLA 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-262 |
5.16e-70 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 216.95 E-value: 5.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQRqAAHRiAL 87
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadWSPAEL-ARRR-AV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYGRHPHQGLLRQwsraDERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQ----- 162
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAE----DDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 163 -QTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRS 240
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
250 260
....*....|....*....|..
gi 2543669097 241 LYGVEADILRAPVDGSPVVVPR 262
Cdd:PRK13548 237 VYGADVLVQPHPETGAPLVLPR 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-258 |
4.22e-65 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 205.02 E-value: 4.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 2 KNMSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSgqR 79
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLesWSS--K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 80 QAAHRIALLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELV 238
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
250 260
....*....|....*....|
gi 2543669097 239 RSLYGVEADILRAPVDGSPV 258
Cdd:PRK10575 242 EQIYGIPMGILPHPAGAAPV 261
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-227 |
2.85e-64 |
|
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: 200.84 E-value: 2.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGqrqaaHRIALLPQ 90
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 91 SPRAPEA--VTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMkDGEVVGEG 227
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-272 |
2.16e-60 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 196.99 E-value: 2.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLP 89
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVEADIL 249
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVG 243
|
250 260
....*....|....*....|...
gi 2543669097 250 RAPVDGSPVVVPRARTADANLAD 272
Cdd:PRK09536 244 TDPATGAPTVTPLPDPDRTEAAA 266
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
10-247 |
2.37e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 192.19 E-value: 2.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ---RQAAHRI 85
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLV---RYGRHP-HQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVlagRLGRTStWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDtVDAELVRS 240
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAVLRE 241
|
....*..
gi 2543669097 241 LYGVEAD 247
Cdd:COG3638 242 IYGGEAE 248
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
9-260 |
2.93e-60 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 192.34 E-value: 2.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVEADI 248
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATV 240
|
250
....*....|..
gi 2543669097 249 LRAPVDGSPVVV 260
Cdd:TIGR03873 241 LTHPDTGRPIIA 252
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-240 |
2.47e-59 |
|
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: 188.70 E-value: 2.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPR----APeavTVA-----GLVRYGRhphqgllrqwSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAM 158
Cdd:COG1122 81 FQNPDdqlfAP---TVEedvafGPENLGL----------PREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTV-DAEL 237
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFsDYEL 227
|
...
gi 2543669097 238 VRS 240
Cdd:COG1122 228 LEE 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-242 |
1.46e-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: 187.39 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV---WKSGQRQAAHRI 85
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLV---RYGRHPH-QGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRSTwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDtVDAELVRS 240
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDE 239
|
..
gi 2543669097 241 LY 242
Cdd:cd03256 240 IY 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-231 |
3.16e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.03 E-value: 3.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGqRQAAHRIALLP 89
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYgrhphQGLLRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:COG1131 80 QEPALYPDLTVRENLRF-----FARLYGLPRKEaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-222 |
1.00e-54 |
|
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: 176.50 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPR----APeavTVA-----GLVRYGRHPHQgllrqwsraDERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:cd03225 81 FQNPDdqffGP---TVEeevafGLENLGLPEEE---------IEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGE 222
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-243 |
1.34e-53 |
|
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: 174.41 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ---RQAAHRI 85
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLV---RYGRHPH-QGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDtVDAELVRS 240
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLRH 240
|
...
gi 2543669097 241 LYG 243
Cdd:TIGR02315 241 IYG 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-240 |
3.91e-51 |
|
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: 168.11 E-value: 3.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGqRQAAHRIALLP 89
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYgrhpHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:COG4555 81 DERGLYDRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPrDTVDAELVRS 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL-DELREEIGEE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-231 |
5.55e-51 |
|
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: 175.09 E-value: 5.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA-----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ---RQA 81
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 AHRIALLPQSPRA--PEAVTVAGLVRYGRHphqgLLRQWSRADERA-VREALEAtstTELAGERLDR----LSGGQRQRC 154
Cdd:COG1123 341 RRRVQMVFQDPYSslNPRMTVGDIIAEPLR----LHGLLSRAERRErVAELLER---VGLPPDLADRypheLSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-227 |
3.49e-50 |
|
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: 165.37 E-value: 3.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA--- 82
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRA---PeAVTVAGLVRYGRHPHQGLLRQWSRadERAVREALEAtstTELAGERLDR----LSGGQRQRCW 155
Cdd:cd03257 82 KEIQMVFQDPMSslnP-RMTIGEQIAEPLRIHGKLSKKEAR--KEAVLLLLVG---VGLPEEVLNRypheLSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 156 LAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-218 |
4.33e-50 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 163.94 E-value: 4.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwksgQRQAAHRIALLPQSPRAPEA 97
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 --VTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSA 175
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2543669097 176 LDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARySDHVIAM 218
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-223 |
9.84e-49 |
|
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: 159.49 E-value: 9.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGqRQAAHRIALLP 89
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTvaglvrygrhphqgllrqwsraderaVREALeatsttelagerldRLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:cd03230 80 EEPSLYENLT--------------------------VRENL--------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-231 |
1.17e-48 |
|
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: 161.45 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWksgqRQAAHRIALLP 89
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT----GLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 -----QSPR------APEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAM 158
Cdd:cd03219 77 igrtfQIPRlfpeltVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-233 |
1.13e-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: 158.88 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLH-----RPSRGTVLADGADVWKSGQRQAAHR 84
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 --IALLPQSPrAPEAVTVAGLVRYGRHPHQgllRQWSRADERAVREALEATSTTELAGERLD--RLSGGQRQRCWLAMVL 160
Cdd:cd03260 81 rrVGMVFQKP-NPFPGSIYDNVAYGLRLHG---IKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREgRTVVMVQHDLAAAARYSDHVIAMKDGEVVgEGAPRDTV 233
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV-EFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-231 |
1.46e-47 |
|
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: 159.20 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP----GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRI 85
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRApeAVtvaglvrygrHPHQGLLRQWS--------RADERAVREALEAtstTELAGERLDR----LSGGQRQR 153
Cdd:COG1124 82 QMVFQDPYA--SL----------HPRHTVDRILAeplrihglPDREERIAELLEQ---VGLPPSFLDRyphqLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-222 |
5.55e-47 |
|
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: 154.71 E-value: 5.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQ 90
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 91 sprapeavtvaglvrygrhphqgllrqwsraderavrealeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVVLLD 170
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 171 EPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGE 222
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-231 |
2.14e-46 |
|
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: 163.78 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAH 83
Cdd:COG4988 332 AGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEAvTVAGLVRYGRHphqgllrqwsRADERAVREALEATSTTELA-----------GERLDRLSGGQRQ 152
Cdd:COG4988 412 QIAWVPQNPYLFAG-TIRENLRLGRP----------DASDEELEAALEAAGLDEFVaalpdgldtplGEGGRGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEGAPRD 231
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEE 557
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-259 |
7.12e-46 |
|
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: 161.22 E-value: 7.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA--VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPS---RGTVLADGADVWKSGQRQAAHR 84
Cdd:COG1123 5 LEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQSP-RAPEAVTVAGLVRYGrhphqGLLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQ 162
Cdd:COG1123 85 IGMVFQDPmTQLNPVTVGDQIAEA-----LENLGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDA----EL 237
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAApqalAA 239
|
250 260
....*....|....*....|..
gi 2543669097 238 VRSLYGVEADILRAPVDGSPVV 259
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPLL 261
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-224 |
1.16e-45 |
|
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: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHR--IAL 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERrnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYgrhphqGL-LRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTP 165
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF------GLkLRGVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-247 |
1.29e-44 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 151.73 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHRIALLP 89
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI----TGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 -----QSPRAP------EAVTVAGLVRYGRHPHQGLLRQWS-RADERAVR----EALEATSTTELAGERLDRLSGGQRQR 153
Cdd:COG0411 81 iartfQNPRLFpeltvlENVLVAAHARLGRGLLAALLRLPRaRREEREAReraeELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDT 232
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....*.
gi 2543669097 233 VDAELVRSLY-GVEAD 247
Cdd:COG0411 241 RADPRVIEAYlGEEAA 256
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-222 |
1.01e-43 |
|
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: 146.95 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR--IAL 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYGrhphqgllrqwsraderavrealeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTV-AREGRTVVMVQHDLAAAARYSDHVIAMKDGE 222
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-223 |
6.04e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.11 E-value: 6.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAH----RI 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMPPPewrrQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAvTVAGLVRYGRHPHQGllrqwsRADERAVREALEATS-TTELAGERLDRLSGGQRQRCWLAMVLAQQT 164
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRER------KFDRERALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRT-VAREGRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-226 |
1.13e-42 |
|
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: 145.69 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgqRQAAHRI 85
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLVRYGRhphqgLLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQT 164
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL-----ELQGVPKAEARErAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 165 PVVLLDEPTSALD------LGhvvdvLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAM--KDGEVVGE 226
Cdd:cd03293 151 DVLLLDEPFSALDaltreqLQ-----EELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-231 |
3.80e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 144.75 E-value: 3.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR--IAL 87
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRrkVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQS----PR--APEAVTVAgLVRygrhphqglLRQWSRADerAVREALEATSTTELAgERLD----RLSGGQRQRCWLA 157
Cdd:COG1126 82 VFQQfnlfPHltVLENVTLA-PIK---------VKKMSKAE--AEERAMELLERVGLA-DKADaypaQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-240 |
4.60e-42 |
|
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: 144.57 E-value: 4.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK---SGQRQAAHRIA 86
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRadeRAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIR---EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 167 VLLDEPTSALD--LGHVVDvlELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD--TVDAELVRS 240
Cdd:cd03261 158 LLYDEPTAGLDpiASGVID--DLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEElrASDDPLVRQ 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
4.76e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.03 E-value: 4.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 1 MKNMsspsgLEVRGLHVGYP----GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKS 76
Cdd:COG1136 1 MSPL-----LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQAA----HRIALLPQS----PR--APEAVTVAGLVRyGRHPhqgllrqwsRADERAVREALEATSTTELAGERLDRL 146
Cdd:COG1136 76 SERELArlrrRHIGFVFQFfnllPEltALENVALPLLLA-GVSR---------KERRERARELLERVGLGDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAArYSDHVIAMKDGEVVG 225
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
.
gi 2543669097 226 E 226
Cdd:COG1136 225 D 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-224 |
5.37e-42 |
|
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: 143.55 E-value: 5.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRQAahRIALLP 89
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRK--SIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSP-RAPEAVTVAGLVRYGrhphqglLRQWSRADERAvREALEatsTTELAGERlDR----LSGGQRQRCWLAMVLAQQT 164
Cdd:cd03226 78 QDVdYQLFTDSVREELLLG-------LKELDAGNEQA-ETVLK---DLDLYALK-ERhplsLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-220 |
1.61e-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: 142.23 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGqRQAAHRIALLP 89
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYgrhpHQGLLRQwsRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:COG4133 82 HADGLKPELTVRENLRF----WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAArySDHVIAMKD 220
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-231 |
5.69e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.86 E-value: 5.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSgLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAH 83
Cdd:COG3842 1 MAMPA-LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 R--IALLPQSPrapeAV----TVAGLVRYGrhphqglLRQ--WSRADERA-VREALEATSTTELAGERLDRLSGGQRQRC 154
Cdd:COG3842 76 KrnVGMVFQDY----ALfphlTVAENVAFG-------LRMrgVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-231 |
6.46e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.15 E-value: 6.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MS-SPSGLEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgq 78
Cdd:COG1116 1 MSaAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 79 RQAAHRIALLPQSPRAPEAVTVAGLVRYGRHphqglLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLA 157
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPWLTVLDNVALGLE-----LRGVPKAERRErARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 158 MVLAQQTPVVLLDEPTSALdlghvvDVL-------ELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKD--GEVVGE-- 226
Cdd:COG1116 151 RALANDPEVLLMDEPFGAL------DALtrerlqdELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEid 224
|
....*...
gi 2543669097 227 ---GAPRD 231
Cdd:COG1116 225 vdlPRPRD 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-223 |
3.64e-40 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 138.82 E-value: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR--IAL 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQS----PR--APEAVTVAGLVRYGRHPHQgllrqwsrADERAvREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:cd03262 81 VFQQfnlfPHltVLENITLAPIKVKGMSKAE--------AEERA-LELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-231 |
4.11e-40 |
|
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: 139.11 E-value: 4.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR-IALL 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEatsttelagERLDR----LSGGQRQRCWLAMVLAQQT 164
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK---------ERRKQlagtLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-222 |
1.94e-39 |
|
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: 135.59 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA--VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRapeavtvaglvrygrhphqgLLrqwsradERAVREALeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03228 81 VPQDPF--------------------LF-------SGTIRENI---------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTvAREGRTVVMVQHDLAAAARYsDHVIAMKDGE 222
Cdd:cd03228 119 ILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-242 |
4.59e-39 |
|
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: 136.65 E-value: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHR----- 84
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI----TGLPPHRiarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQsprapeavtvaglvryGRHPHQGL-----LR--QWSRADERAVREALEATSTT--ELAgERLDR----LSGGQR 151
Cdd:COG0410 80 IGYVPE----------------GRRIFPSLtveenLLlgAYARRDRAEVRADLERVYELfpRLK-ERRRQragtLSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 152 QRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
250
....*....|.
gi 2543669097 232 TVDAELVRSLY 242
Cdd:COG0410 223 LLADPEVREAY 233
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-247 |
4.21e-38 |
|
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: 133.82 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 30 FSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADvwksgQRQAAHRIALLPQspRAPEA----VTVAGLVR 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQ--RHEFAwdfpISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 106 YGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVL 185
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 186 ELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMkDGEVVGEGAPRDTVDAELVRSLYGVEAD 247
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGVSDS 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-239 |
4.87e-38 |
|
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: 134.34 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK---SGQRQAAHRIA 86
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlseKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPrapeAV----TVAGLVRYGrhphqglLRQWSRADERAVRealeatsttELAGERLDR-------------LSGG 149
Cdd:COG1127 86 MLFQGG----ALfdslTVFENVAFP-------LREHTDLSEAEIR---------ELVLEKLELvglpgaadkmpseLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 150 QRQRCWLAMVLAQQTPVVLLDEPTSALD--LGHVVDvlELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDpiTSAVID--ELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*
gi 2543669097 227 GAPRD--TVDAELVR 239
Cdd:COG1127 224 GTPEEllASDDPWVR 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-236 |
7.72e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.34 E-value: 7.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 30 FSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHRIALLPQSPRAPEAVTVAGLVRYGRH 109
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSMLFQENNLFPHLTVAQNIGLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 110 PHQGLlrqwSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVR 189
Cdd:COG3840 98 PGLKL----TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2543669097 190 TVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAE 236
Cdd:COG3840 174 ELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-236 |
8.37e-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: 140.29 E-value: 8.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA 82
Cdd:COG4987 329 PGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRAPEAvTVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTELA-----------GERLDRLSGGQR 151
Cdd:COG4987 409 RRIAVVPQRPHLFDT-TLRENLRLAR----------PDATDEELWAALERVGLGDWLaalpdgldtwlGEGGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 152 QRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEGAPRD 231
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
....*
gi 2543669097 232 TVDAE 236
Cdd:COG4987 556 LLAQN 560
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-218 |
8.62e-38 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 139.73 E-value: 8.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 6 SPSGLEVRGLHVGYPGR-AVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR 84
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQSPRAPEAvTVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTEL-----------AGERLDRLSGGQRQR 153
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLAR----------PDASDAEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAARYsDHVIAM 218
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-223 |
1.30e-37 |
|
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: 132.61 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK-SGQRQAAHR 84
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 ---IALLPQSPR------APEAVTVAGLVRYgrhphqgllRQWSRADERAvREALEATSTTELAGERLDRLSGGQRQRCW 155
Cdd:cd03255 81 rrhIGFVFQSFNllpdltALENVELPLLLAG---------VPKKERRERA-EELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 156 LAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLaAAARYSDHVIAMKDGEV 223
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-284 |
1.73e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.66 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVW---KSGQRqaahRI 85
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlPPRER----RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPrapeAV----TVAGLVRYG-RHphqgllRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:COG1118 78 GFVFQHY----ALfphmTVAENIAFGlRV------RPPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 160 LAQQTPVVLLDEPTSALDlGHVVDVLE--LVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDA-- 235
Cdd:COG1118 148 LAVEPEVLLLDEPFGALD-AKVRKELRrwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRpa 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2543669097 236 -ELVRSLYGvEADILRAPVDGSpvvvpRARTADANLADPYPADAGQVDAG 284
Cdd:COG1118 227 tPFVARFLG-CVNVLRGRVIGG-----QLEADGLTLPVAEPLPDGPAVAG 270
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-261 |
2.70e-37 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 133.41 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA-RLHRPS-------RGTVLADGADVWKSGQRQA 81
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 AHRIALLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTP---------VVLLDEPTSALDLGHVVDVLELVRTVAREGRT-VVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13547 162 QLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260 270
....*....|....*....|....*....|
gi 2543669097 232 TVDAELVRSLYGVEADILRAPVDGSPVVVP 261
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGVPPVIVP 271
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-231 |
9.62e-37 |
|
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: 131.80 E-value: 9.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 16 HVGY---PG----RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ---RQAAHRI 85
Cdd:TIGR04521 5 NVSYiyqPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklKDLRKKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPrapE----AVTVAGLVRYGrhPH-QGLLRQwsRADERaVREALEATSTTElagERLDR----LSGGQRQRCWL 156
Cdd:TIGR04521 85 GLVFQFP---EhqlfEETVYKDIAFG--PKnLGLSEE--EAEER-VKEALELVGLDE---EYLERspfeLSGGQMRRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-239 |
1.27e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.30 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRIALL 88
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAqAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPR-APEaVTVAGLVRYGRHPHQGLLRQWSRADERAvREALEATSTTELAGERLDRLSGGQRQrcwlaMV-----LAQ 162
Cdd:COG1129 85 HQELNlVPN-LSVAENIFLGREPRRGGLIDWRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQ-----LVeiaraLSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVR 239
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-224 |
9.73e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 128.62 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLH--RPS---RGTVLADGADVWKSGQR 79
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 80 QAAHR--IALLPQSPRaPEAVTVAGLVRYGrHPHQGLLRQwSRADERaVREALEAtsttelAG------ERLDR----LS 147
Cdd:COG1117 87 VVELRrrVGMVFQKPN-PFPKSIYDNVAYG-LRLHGIKSK-SELDEI-VEESLRK------AAlwdevkDRLKKsalgLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 148 GGQRQR-CwLAMVLAQQTPVVLLDEPTSALD---------LghvvdVLELvrtvaREGRTVVMVQHDLAAAARYSDHVIA 217
Cdd:COG1117 157 GGQQQRlC-IARALAVEPEVLLMDEPTSALDpistakieeL-----ILEL-----KKDYTIVIVTHNMQQAARVSDYTAF 225
|
....*..
gi 2543669097 218 MKDGEVV 224
Cdd:COG1117 226 FYLGELV 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-229 |
1.98e-35 |
|
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: 127.35 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGY-PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQsprapEAV----TVAGLVRYGRhphqgllrqWSRADErAVREALEATSTTEL-----------AGERLDRLSGGQRQR 153
Cdd:cd03253 81 PQ-----DTVlfndTIGYNIRYGR---------PDATDE-EVIEAAKAAQIHDKimrfpdgydtiVGERGLKLSGGEKQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAP 229
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-233 |
4.87e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 128.63 E-value: 4.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRP---SRGTVLADGADVWKSGQRQAA 82
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 H----RIALLPQSPRA---PeAVTVAGLVRYGRHPHQGLlrqwSRADERA-VREALEATSTTElAGERLDR----LSGGQ 150
Cdd:COG0444 82 KirgrEIQMIFQDPMTslnP-VMTVGDQIAEPLRIHGGL----SKAEARErAIELLERVGLPD-PERRLDRypheLSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 151 RQRCWLAMVLAQQTPVVLLDEPTSALDlghVV---DVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVgE 226
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALD---VTiqaQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIV-E 231
|
....*..
gi 2543669097 227 GAPRDTV 233
Cdd:COG0444 232 EGPVEEL 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-227 |
7.74e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 132.21 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPG-RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:COG1132 339 EIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQsprapEAV----TVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTELA-----------GERLDRLSGGQRQ 152
Cdd:COG1132 419 VPQ-----DTFlfsgTIRENIRYGR----------PDATDEEVEEAAKAAQAHEFIealpdgydtvvGERGVNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEG 227
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-231 |
1.04e-34 |
|
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: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVW---KSGQRQAA 82
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRAPEAVTVAGLVRYgrhPHQglLRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL---PLE--IAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-239 |
1.21e-34 |
|
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: 132.27 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA--VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAvTVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTELA-----------GERLDRLSGGQRQRCWL 156
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGD----------PDATDEEIIEAARLAGLHDFIealpmgydtvvGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDLG---HVVDVLELvrtvAREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGAP---- 229
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAEteaIILENLRR----LLKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHeell 697
|
250
....*....|.
gi 2543669097 230 -RDTVDAELVR 239
Cdd:COG2274 698 aRKGLYAELVQ 708
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-227 |
1.29e-34 |
|
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: 124.61 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGtVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHR-IALL 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYgrhphQGLLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03264 78 PQEFGVYPNFTVREFLDY-----IAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTVArEGRTVVMVQH---DLAAAArysDHVIAMKDGEVVGEG 227
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHiveDVESLC---NQVAVLNKGKLVFEG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-251 |
2.63e-34 |
|
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: 124.81 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLA------DGADVWKsgQRQaah 83
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWE--LRK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLpqSP----RAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:COG1119 79 RIGLV--SPalqlRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREG-RTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELV 238
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENL 236
|
250
....*....|...
gi 2543669097 239 RSLYGVEADILRA 251
Cdd:COG1119 237 SEAFGLPVEVERR 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-174 |
2.98e-34 |
|
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: 121.60 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPRAPEAVTVAGLV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 105 RYGRHPhQGLLRQWSRADeraVREALEATSTTELAGERLDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTS 174
Cdd:pfam00005 81 RLGLLL-KGLSKREKDAR---AEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-231 |
3.72e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.73 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 8 SGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksGQRQAAHR-IA 86
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPrapeAV----TVAGLVRYgrhphqGL-LRQWSRAD-ERAVREALEATSTTELagerLDR----LSGGQRQRCWL 156
Cdd:COG3839 79 MVFQSY----ALyphmTVYENIAF------PLkLRKVPKAEiDRRVREAAELLGLEDL----LDRkpkqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMrAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
10-262 |
1.12e-33 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 123.03 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGypGRavVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHrPSRGTVLADGADV--WkSGQRQAAHRiAL 87
Cdd:COG4138 1 LQLNDVAVA--GR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsdW-SAAELARHR-AY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYGRHPHQGllrqwSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:COG4138 74 LSQQQSPPFAMPVFQYLALHQPAGAS-----SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 168 -------LLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRS 240
Cdd:COG4138 149 npegqllLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSE 228
|
250 260
....*....|....*....|..
gi 2543669097 241 LYGVEADILRapVDGSPVVVPR 262
Cdd:COG4138 229 VFGVKFRRLE--VEGHRWLIPT 248
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-229 |
1.39e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADG-----ADVWksgqrQAA 82
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVW-----DVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRAP-EAVTVAGLVRYGRHpHQGLLRqwsraDE--RAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:PRK13635 81 RQVGMVFQNPDNQfVGATVQDDVAFGLE-NIGVPR-----EEmvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGR-TVVMVQHDLAAAARySDHVIAMKDGEVVGEGAP 229
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-229 |
1.85e-33 |
|
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: 121.84 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA--VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRQAAHRIAL 87
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYgrhphQGLLRQWSRADERAVREA-LEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:cd03263 80 CPQFDALFDELTVREHLRF-----YARLKGLPKSEIKEEVELlLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-244 |
2.79e-33 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 122.68 E-value: 2.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSGLEVRGLHVGY-PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAa 82
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 hrIALLPQSPRAPEA--VTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVL 160
Cdd:PRK15056 80 --VAYVPQSEEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKdGEVVGEGAPRDTVDAE-LVR 239
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAEnLEL 236
|
....*
gi 2543669097 240 SLYGV 244
Cdd:PRK15056 237 AFSGV 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
5.99e-33 |
|
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: 118.69 E-value: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRIALL 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDArRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQsprapeavtvaglvrygrhphqgllrqwsraderavrealeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-240 |
1.03e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVW--KSGQRQAAHRIA 86
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPR----APeavTVAGLVRYGrhP-HQGLLRQwsrADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLA 161
Cdd:PRK13639 82 IVFQNPDdqlfAP---TVEEDVAFG--PlNLGLSKE---EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTV-DAELVRS 240
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFsDIETIRK 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-227 |
1.25e-32 |
|
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: 119.31 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGadvwKSGQRQAAHRIALLP 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYgrhphQGLLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03269 77 EERGLYPKMKVIDQLVY-----LAQLKGLKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-233 |
1.16e-31 |
|
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: 122.87 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA-----------VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHrPSRGTVLADGADV--WKS 76
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdgLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQAA-HRIALLPQ------SPRapeaVTVAGLVRYGRHPHQgllRQWSRAD-ERAVREALEAtstTELAGERLDR--- 145
Cdd:COG4172 355 RALRPLrRRMQVVFQdpfgslSPR----MTVGQIIAEGLRVHG---PGLSAAErRARVAEALEE---VGLDPAARHRyph 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 -LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:COG4172 425 eFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
250
....*....|
gi 2543669097 224 VGEGaPRDTV 233
Cdd:COG4172 505 VEQG-PTEQV 513
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-231 |
1.36e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.71 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARL-----HRPSRGTVLADGADVWKSGQRQAAHR 84
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQSPRAPEAVTVAGLVRYGrhPHQGLLRQWSRADERAVREALEATSTTELAGERLD----RLSGGQRQRCWLAMVL 160
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREgRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-253 |
2.25e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPE-AVTVAGLVRYGrhP-HQGLlrqwsRADE--RAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQT 164
Cdd:PRK13647 85 FQDPDDQVfSSTVWDDVAFG--PvNMGL-----DKDEveRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELvrslygV 244
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI------V 231
|
....*....
gi 2543669097 245 EADILRAPV 253
Cdd:PRK13647 232 EQAGLRLPL 240
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-230 |
2.39e-31 |
|
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: 116.56 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGY-PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLP 89
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAvTVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTEL-----------AGERLDRLSGGQRQRCWLAM 158
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFimklpngydtvLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGAPR 230
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHD 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-231 |
5.28e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.22 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 6 SPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVW----KSGQRQA 81
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 AH---------RIALLPQSPRAPEAVTVagLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQ 152
Cdd:PRK10619 82 ADknqlrllrtRLTMVFQHFNLWSHMTV--LENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-231 |
7.16e-31 |
|
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: 115.41 E-value: 7.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADvwksgqrqaahrIALLP 89
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD------------ITNLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVtvagLVRYGRHPHQ--------GL-LRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:cd03300 69 PHKRPVNTV----FQNYALFPHLtvfeniafGLrLKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-231 |
8.86e-31 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 115.33 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPGRA---VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03249 2 EFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPrAPEAVTVAGLVRYGRHPHQgllrqwSRADERAVREAlEATSTTE--------LAGERLDRLSGGQRQRCWLAMV 159
Cdd:cd03249 82 VSQEP-VLFDGTIAENIRYGKPDAT------DEEVEEAAKKA-NIHDFIMslpdgydtLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 160 LAQQTPVVLLDEPTSALDL---GHVVDVLELvrtvAREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03249 154 LLRNPKILLLDEATSALDAeseKLVQEALDR----AMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-227 |
1.98e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 113.84 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQsprapEAVTVAGLVR----YGRhPHqgllrqwsrADERAVREALEATSTTELA-----------GERLDRLSGGQRQ 152
Cdd:cd03245 83 VPQ-----DVTLFYGTLRdnitLGA-PL---------ADDERILRAAELAGVTDFVnkhpngldlqiGERGRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAArYSDHVIAMKDGEVVGEG 227
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-239 |
2.16e-30 |
|
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: 119.47 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 7 PSG-LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAH 83
Cdd:COG4618 327 PKGrLSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSpraPE--AVTVA-GLVRYGrhphqgllrqwsRADERAVREALEATSTTEL-----------AGERLDRLSGG 149
Cdd:COG4618 407 HIGYLPQD---VElfDGTIAeNIARFG------------DADPEKVVAAAKLAGVHEMilrlpdgydtrIGEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 150 QRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGaP 229
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFG-P 549
|
250
....*....|
gi 2543669097 230 RDTVDAELVR 239
Cdd:COG4618 550 RDEVLARLAR 559
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-231 |
2.86e-30 |
|
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: 114.66 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA----AHRI-------ALLPQSpr 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKIsmvfqsfALLPHR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 94 apeavTVAGLVRYGRHPhQGLLRQWSRadERAvREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPT 173
Cdd:cd03294 118 -----TVLENVAFGLEV-QGVPRAERE--ERA-AEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 174 SALD---LGHVVDvlELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03294 189 SALDpliRREMQD--ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
10-237 |
3.38e-30 |
|
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: 119.59 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgqRQAA----- 82
Cdd:TIGR03375 464 IEFRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI-----RQIDpadlr 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRapeavTVAGLVR----YGRhPHqgllrqwsrADERAVREALEATSTTELA-----------GERLDRLS 147
Cdd:TIGR03375 539 RNIGYVPQDPR-----LFYGTLRdniaLGA-PY---------ADDEEILRAAELAGVTEFVrrhpdgldmqiGERGRSLS 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 148 GGQRQRCWLAMVLAQQTPVVLLDEPTSALDLG---HVVDVLELVrtvaREGRTVVMVQHDLAAAARySDHVIAMKDGEVV 224
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRseeRFKDRLKRW----LAGKTLVLVTHRTSLLDL-VDRIIVMDNGRIV 678
|
250
....*....|...
gi 2543669097 225 GEGaPRDTVDAEL 237
Cdd:TIGR03375 679 ADG-PKDQVLEAL 690
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-231 |
3.68e-30 |
|
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: 113.55 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSprapeavtv 100
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 101 AGLVrygrhPHQ------GL---LRQWSRADERA-VREALEATS--TTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03295 84 IGLF-----PHMtveeniALvpkLLKWPKEKIRErADELLALVGldPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-240 |
4.21e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.56 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGA--DVWKSGQRQAAHRIA 86
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSP-RAPEAVTVAGLVRYgrhphqGLLRQWSRADE--RAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQ 163
Cdd:PRK13636 86 MVFQDPdNQLFSASVYQDVSF------GAVNLKLPEDEvrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 164 TPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDT-VDAELVRS 240
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfAEKEMLRK 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-227 |
4.80e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK-SGQ--RQAA 82
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERelRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRAPEAVTVAGLVRYgrhPhqglLRQ--WSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVAL---P----LEIagVPKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-231 |
6.60e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 113.36 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 1 MKNMSSPSgLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV----WKS 76
Cdd:COG4598 1 MTDTAPPA-LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQAAH---------RIALLPQS-------------PRAPeaVTVAGLvrygrhphqgllrqwSRADERAVREALeats 134
Cdd:COG4598 80 GELVPADrrqlqrirtRLGMVFQSfnlwshmtvlenvIEAP--VHVLGR---------------PKAEAIERAEAL---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 135 tteLA----GERLD----RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLA 206
Cdd:COG4598 139 ---LAkvglADKRDaypaHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMG 215
|
250 260
....*....|....*....|....*
gi 2543669097 207 AAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:COG4598 216 FARDVSSHVVFLHQGRIEEQGPPAE 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-255 |
7.91e-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: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGaDVW---KSGQRQAAH--RIALLPQSPRAPEAVTVA 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLqdsARGIFLPPHrrRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 102 GLVRYGRHphqgllRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHV 181
Cdd:COG4148 96 GNLLYGRK------RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 182 VDVLELVRTVAREGRT-VVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDT-VDAELVRSLYGVEAD-ILRAPVDG 255
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVlSRPDLLPLAGGEEAGsVLEATVAA 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-272 |
3.64e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.66 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQaaHRIALLPQSprapeavtvagl 103
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQS------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 104 vrYGRHPHQ--------GLLRQWSRADERA--VREALEatsTTELAG--ER-LDRLSGGQRQRCWLAMVLAQQTPVVLLD 170
Cdd:PRK11432 87 --YALFPHMslgenvgyGLKMLGVPKEERKqrVKEALE---LVDLAGfeDRyVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 171 EPTSALDLGHVVDVLELVRTV-AREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD---TVDAELVRSLYGvEA 246
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQElyrQPASRFMASFMG-DA 240
|
250 260 270
....*....|....*....|....*....|.
gi 2543669097 247 DILRAPVDGSPVVV-----PRARTADANLAD 272
Cdd:PRK11432 241 NIFPATLSGDYVDIygyrlPRPAAFAFNLPD 271
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-235 |
3.90e-29 |
|
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: 115.97 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSprapeaV-----TVAGLVRYGRhphqglLRQWSRADeraVREALEATSTTELA-----------GERLDRLSGGQR 151
Cdd:TIGR02203 411 VSQD------VvlfndTIANNIAYGR------TEQADRAE---IERALAAAYAQDFVdklplgldtpiGENGVLLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 152 QRCWLAMVLAQQTPVVLLDEPTSALDLG---HVVDVLELVrtvaREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGA 228
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNEserLVQAALERL----MQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
....*..
gi 2543669097 229 PRDTVDA 235
Cdd:TIGR02203 551 HNELLAR 557
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-227 |
5.20e-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: 110.15 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGY----PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSgQRQAAHRI 85
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE-PAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLVRYGRHPHqGLLRQwsrADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTP 165
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLY-GLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-224 |
8.78e-29 |
|
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: 109.27 E-value: 8.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKsgqRQAAHR-IALL 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD---LPPKDRdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSprapeavtvaglvrYGRHPHQ--------GL-LRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAM 158
Cdd:cd03301 78 FQN--------------YALYPHMtvydniafGLkLRKVPKDEiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-275 |
1.06e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.62 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAhrIALLP 89
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRYGrhphqglLRQ--WSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFG-------LKQdkLPKAEIASrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 167 VLLDEPTSALDLG-------HVVDVLElvrtvaREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVD----- 234
Cdd:PRK11607 171 LLLDEPMGALDKKlrdrmqlEVVDILE------RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEhpttr 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2543669097 235 --AELVRSLYGVEADILRAPVDG----SPVVV-PRARTADANLADPYP 275
Cdd:PRK11607 245 ysAEFIGSVNVFEGVLKERQEDGlvidSPGLVhPLKVDADASVVDNVP 292
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-227 |
1.09e-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: 108.17 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA--VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRQAAHRIAL 87
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRapeavtvaglvrygrhphqgllrqwsraderavreaLEATSTTELAGERLdrlSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03247 80 LNQRPY------------------------------------LFDTTLRNNLGRRF---SGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTVAREgRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEG 227
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-208 |
1.28e-28 |
|
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: 108.28 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YPGRA-VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGA--DVWKSGQRQAAHRIALLPQSPRAP 95
Cdd:TIGR01166 1 YPGGPeVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 96 E-AVTVAGLVRYGRHpHQGLlrqwSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPT 173
Cdd:TIGR01166 81 LfAADVDQDVAFGPL-NLGL----SEAEvERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 174 SALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAA 208
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-227 |
1.40e-28 |
|
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: 108.73 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 33 PAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHRIALLPQSPRAPEAVTVAGLVRYGRHPHQ 112
Cdd:cd03298 22 AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 113 GLLRQwsraDERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVA 192
Cdd:cd03298 100 KLTAE----DRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2543669097 193 RE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03298 176 AEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-259 |
1.96e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.58 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AH 83
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERaVREALEATsttelaGERLD------RLSGGQRQRCWLA 157
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARAR-IRELSERY------GLDVDpdakveDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAEL 237
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEEL 233
|
250 260
....*....|....*....|....
gi 2543669097 238 VRSLYG--VEADILRAPVDGSPVV 259
Cdd:COG3845 234 AELMVGreVLLRVEKAPAEPGEVV 257
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-231 |
2.14e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 108.96 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYpGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHRIALLP 89
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSprapeavtvaglvrYGRHPHQ--------GL-LRQWSRA-DERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:cd03299 78 QN--------------YALFPHMtvykniayGLkKRKVDKKeIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-229 |
3.12e-28 |
|
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: 107.84 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSgQRQAAHRIALLP 89
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVT-VAGLVRYGRhpHQGLlrQWSRADERaVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03265 80 QDLSVDDELTgWENLYIHAR--LYGV--PGAERRER-IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRT-VAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-231 |
3.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPrapEAVTVAGLVRY 106
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNP---DNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 107 grHPHQGLLRQWSRADE--RAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDV 184
Cdd:PRK13648 104 --DVAFGLENHAVPYDEmhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2543669097 185 LELVRTVAREGR-TVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13648 182 LDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTE 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-257 |
4.80e-28 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 108.10 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 30 FSAPAGTVTSVVGPNGCGKSTLLRALARLhRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPRAPEAVTVAGLVRYgrh 109
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 110 pHQGLLRQwSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVV-------LLDEPTSALDLGHVV 182
Cdd:PRK03695 93 -HQPDKTR-TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 183 DVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVeaDILRAPVDGSP 257
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGV--NFRRLDVEGHP 243
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-244 |
5.31e-28 |
|
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: 107.61 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQRqAAHRIAL 87
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItkLPPHER-ARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLVRYGRHPHqgllrqwsRADERAVRE-------ALEatsttELAGERLDRLSGGQRQRCWLAMVL 160
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAAL--------PRRSRKIPDeiyelfpVLK-----EMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGR-TVVMVQHDLAAAARYSDHVIAMKDGEVVGEGaPRDTVDAELVR 239
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASG-AGDELDEDKVR 225
|
....*
gi 2543669097 240 SLYGV 244
Cdd:TIGR03410 226 RYLAV 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-236 |
6.60e-28 |
|
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: 107.70 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQsprapEAV----TVAGLVRYGRHphqgllrqwsRADERAVREALEATSTTEL-----------AGERLDRLSGGQRQ 152
Cdd:cd03251 81 VSQ-----DVFlfndTVAENIAYGRP----------GATREEVEEAARAANAHEFimelpegydtvIGERGVKLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDlghvvdvLELVRTVAR------EGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGE 226
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALD-------TESERLVQAalerlmKNRTTFVIAHRL-STIENADRIVVLEDGKIVER 217
|
250
....*....|
gi 2543669097 227 GAPRDTVDAE 236
Cdd:cd03251 218 GTHEELLAQG 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-223 |
8.51e-28 |
|
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: 105.38 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQsprapEAVTVAGlvrygrhphqgllrqwsraderAVREALeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03246 81 LPQ-----DDELFSG----------------------SIAENI---------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARySDHVIAMKDGEV 223
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-227 |
9.24e-28 |
|
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: 106.53 E-value: 9.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSgqRQAAHRIALLP 89
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPrapeavtvaGLVRY--GRHpHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03268 79 EAP---------GFYPNltARE-NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 168 LLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-224 |
1.00e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLH-VGYPG----RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQRqaA 82
Cdd:COG1101 2 LELKNLSkTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPR---APeAVTVAG--LVRYGRHPHQGLLRQWSRADERAVREALeatSTTELAGE-RLD----RLSGGQRQ 152
Cdd:COG1101 80 KYIGRVFQDPMmgtAP-SMTIEEnlALAYRRGKRRGLRRGLTKKRRELFRELL---ATLGLGLEnRLDtkvgLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGR-TVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-235 |
1.49e-27 |
|
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: 106.65 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQaaHRIALL 88
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 169 LDEPTSALDlghvVDVLELVRTVARE-----GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDA 235
Cdd:cd03296 160 LDEPFGALD----AKVRKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-227 |
1.70e-27 |
|
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: 105.33 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA-RLHRPS-RGTVLADGADVWKSGQRQaahRIALLPQsprapEAV 98
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGRPLDKRSFRK---IIGYVPQ-----DDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TvaglvrygrHPHQgllrqwsraderAVREALEATSttelageRLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDL 178
Cdd:cd03213 93 L---------HPTL------------TVRETLMFAA-------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 179 GHVVDVLELVRTVAREGRTVVMVQHdlaaAARYS-----DHVIAMKDGEVVGEG 227
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTIICSIH----QPSSEifelfDKLLLLSQGRVIYFG 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-245 |
5.45e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.73 E-value: 5.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHRIALLP 89
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTVAGLVRY-GRhphqglLRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:COG4152 78 EERGLYPKMKVGEQLVYlAR------LKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 168 LLDEPTSALDlgHV-VDVL-ELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG--------APRDTV---- 233
Cdd:COG4152 152 ILDEPFSGLD--PVnVELLkDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGsvdeirrqFGRNTLrlea 229
|
250
....*....|....
gi 2543669097 234 --DAELVRSLYGVE 245
Cdd:COG4152 230 dgDAGWLRALPGVT 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-205 |
7.23e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 109.37 E-value: 7.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRA-VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:TIGR02868 334 TLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRApEAVTVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTELA-----------GERLDRLSGGQRQRCWL 156
Cdd:TIGR02868 414 CAQDAHL-FDTTVRENLRLAR----------PDATDEELWAALERVGLADWLralpdgldtvlGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTvAREGRTVVMVQHDL 205
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-223 |
8.01e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.14 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgqRQAAHRIALLP 89
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRAPEAVTV---AGLvrygrhphqGLLRQWsradERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK11247 88 QDARLLPWKKVidnVGL---------GLKGQW----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-227 |
1.23e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.62 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADvwksgqrQAAH 83
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-------GQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEAVTVAGLVRygRHPHQGLLRQWS---RADER--AV---------REALEATSTTELAGERLDRL--- 146
Cdd:PRK11701 74 DLYALSEAERRRLLRTEWGFVH--QHPRDGLRMQVSaggNIGERlmAVgarhygdirATAGDWLERVEIDAARIDDLptt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 -SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:PRK11701 152 fSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
...
gi 2543669097 225 GEG 227
Cdd:PRK11701 232 ESG 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-230 |
1.51e-26 |
|
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: 106.04 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 40 VVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHR--IALLPQSPRAPEAVTVAGLVRYGRHpHQGLLRq 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLrhINMVFQSYALFPHMTVEENVAFGLK-MRKVPR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 118 wSRADERaVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD--LGHVVDvLELVRTVAREG 195
Cdd:TIGR01187 75 -AEIKPR-VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQ-LELKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 196 RTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPR 230
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPE 186
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-230 |
2.13e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.06 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 8 SGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwKSGQRQAAHRIAL 87
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--------RVGDITIDTARSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVTVAGLV--RYGRHPHQGLLRQW--------SRADERAVREALEATSTTELAGERLD---RLSGGQRQRC 154
Cdd:PRK11264 74 SQQKGLIRQLRQHVGFVfqNFNLFPHRTVLENIiegpvivkGEPKEEATARARELLAKVGLAGKETSyprRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPR 230
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-227 |
2.58e-26 |
|
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: 102.76 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGtVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGAdVWKSGQRQaahrIALLPQSPRApeavtvaGLV-- 104
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKK----INLPPQQRKI-------GLVfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 105 RYGRHPHQ--------GLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:cd03297 83 QYALFPHLnvrenlafGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 177 DlGHVVDVL--ELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03297 163 D-RALRLQLlpELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-234 |
2.73e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQ------RQAA----HRIALLPQspr 93
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKvderliRQEAgmvfQQFYLFPH--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 94 apeaVTVAGLVRYGrhPHQglLRQWSRADERAV-REALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:PRK09493 92 ----LTALENVMFG--PLR--VRGASKEEAEKQaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 173 TSALD--LGHvvDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVD 234
Cdd:PRK09493 164 TSALDpeLRH--EVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-248 |
3.71e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 104.02 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 15 LHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARL------HRPSrGTVLADGADVWKSGQ-RQAAHRIAL 87
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYS-GDVLLGGRSIFNYRDvLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRaPEAVTVAGLVRYGRHPHQGLLRQWSRADERAvreALEATSTTELAGERLD----RLSGGQRQRCWLAMVLAQQ 163
Cdd:PRK14271 106 LFQRPN-PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQA---RLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 164 TPVVLLDEPTSALDLGHVVDVLELVRTVArEGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVD----AELVR 239
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSspkhAETAR 260
|
....*....
gi 2543669097 240 SLYGVEADI 248
Cdd:PRK14271 261 YVAGLSGDV 269
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-242 |
3.82e-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: 102.62 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR-IALL 88
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAglvrygrhphQGLL-----RQWSRADERAVREA-LEATSTTELAGERLDRLSGGQRQRCWLAMVLAQ 162
Cdd:cd03218 81 PQEASIFRKLTVE----------ENILavleiRGLSKKEREEKLEElLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLY 242
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
8.69e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 3 NMSSPsgLEVRGLHvgypgravvrDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVlADGADVWKSGQRQAA 82
Cdd:PRK13634 13 QYKTP--FERRALY----------DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGERVITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 -----HRIALLPQSPRAP--EAvTVAGLVRYGrhPhqgllRQWSRADERAVREALEATSTTELAGERLDR----LSGGQR 151
Cdd:PRK13634 80 lkplrKKVGIVFQFPEHQlfEE-TVEKDICFG--P-----MNFGVSEEDAKQKAREMIELVGLPEELLARspfeLSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 152 QRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPR 230
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
.
gi 2543669097 231 D 231
Cdd:PRK13634 232 E 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-221 |
9.41e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.43 E-value: 9.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwksgQRQAAH 83
Cdd:COG4178 358 SEDGALALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-----------ARPAGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEAvTVAGLVRYGRHPHQgllrqwsrADERAVREALEATSTTELAgERLD-------RLSGGQRQRCWL 156
Cdd:COG4178 427 RVLFLPQRPYLPLG-TLREALLYPATAEA--------FSDAELREALEAVGLGHLA-ERLDeeadwdqVLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTvAREGRTVVMVQHDlAAAARYSDHVIAMKDG 221
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-246 |
1.08e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.87 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVgypgRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRIALL 88
Cdd:COG1129 257 LEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 P-----------QSPRapEAVTVAGLVRYGRHphqGLLRQwsRADERAVREALE-----ATSTTELAGErldrLSGGQRQ 152
Cdd:COG1129 333 PedrkgeglvldLSIR--ENITLASLDRLSRG---GLLDR--RRERALAEEYIKrlrikTPSPEQPVGN----LSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDT 232
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
250
....*....|....
gi 2543669097 233 VDAELVRSLYGVEA 246
Cdd:COG1129 482 TEEAIMAAATGGAA 495
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-230 |
1.10e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALAR---LHRPSR--GTVLADGADVW--KSGQRQAA 82
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRlleLNEEARveGEVRLFGRNIYspDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRAPEAVTVAGLVRYGRHpHQGLLRQWSRADERaVREALEATSTTELAGERLD----RLSGGQRQRCWLAM 158
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVK-LNGLVKSKKELDER-VEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREgRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPR 230
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-223 |
2.14e-25 |
|
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: 99.43 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGypgrAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRIALL 88
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSprapeavtvaglvrygRHpHQGLLRQWSraderaVREALEATSttelagerldRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03215 81 PED----------------RK-REGLVLDLS------VAENIALSS----------LLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-228 |
2.70e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHRIALL 88
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL----SRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSprapeavtvAGLVrygrhpHQ--GLLRQWS----------------RADERAVREALEATSTTELAGERLDRLSGGQ 150
Cdd:COG2884 78 RRR---------IGVV------FQdfRLLPDRTvyenvalplrvtgksrKEIRRRVREVLDLVGLSDKAKALPHELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 151 RQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGA 228
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-264 |
3.90e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.60 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 6 SPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRQAAHRI 85
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-PARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTV-AGLVRYGRHphqglLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQT 164
Cdd:PRK13536 117 GVVPQFDNLDLEFTVrENLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAEL---VRSL 241
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIgcqVIEI 271
|
250 260
....*....|....*....|...
gi 2543669097 242 YGVEADILRApvdgspVVVPRAR 264
Cdd:PRK13536 272 YGGDPHELSS------LVKPYAR 288
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-233 |
7.17e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 101.35 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGR--------AVVR---DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ 78
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 79 RQAAH---RIALLPQSPRA---P---------EAVTVAGLVrygrhphqgllrqwSRADERA-VREALEatsTTELAGER 142
Cdd:COG4608 88 RELRPlrrRMQMVFQDPYAslnPrmtvgdiiaEPLRIHGLA--------------SKAERRErVAELLE---LVGLRPEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 143 LDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIA 217
Cdd:COG4608 151 ADRypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAV 230
|
250
....*....|....*.
gi 2543669097 218 MKDGEVVgEGAPRDTV 233
Cdd:COG4608 231 MYLGKIV-EIAPRDEL 245
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
8-227 |
1.75e-24 |
|
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: 102.98 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 8 SGLEVRGLHV--GY-PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ---RQA 81
Cdd:COG5265 354 GGGEVRFENVsfGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQaslRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 ahrIALLPQsprapEAV----TVAGLVRYGRhPHqgllrqwsrADERAVREALEA-------TSTTE----LAGERLDRL 146
Cdd:COG5265 434 ---IGIVPQ-----DTVlfndTIAYNIAYGR-PD---------ASEEEVEAAARAaqihdfiESLPDgydtRVGERGLKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAARySDHVIAMKDGEVVGE 226
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
.
gi 2543669097 227 G 227
Cdd:COG5265 574 G 574
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-231 |
1.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRP---SRGTVLADGADVWKSGQR 79
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 80 QAAHRIALLPQSPRAP-EAVTVAGLVRYGRHPhqgllRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLA 157
Cdd:PRK13640 81 DIREKVGIVFQNPDNQfVGATVGDDVAFGLEN-----RAVPRPEmIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAArYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVE 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-245 |
2.17e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 100.26 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYP--GRAV--VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK---SGQRQAAH 83
Cdd:PRK11153 3 ELKNISKVFPqgGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlseKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQ-----SPRapeavTVAGLVRYgrhPHQglLRQWSRAD-ERAVREALEATSTTELAgerlDR----LSGGQRQR 153
Cdd:PRK11153 83 QIGMIFQhfnllSSR-----TVFDNVAL---PLE--LAGTPKAEiKARVTELLELVGLSDKA----DRypaqLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGA---- 228
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTvsev 228
|
250 260
....*....|....*....|
gi 2543669097 229 ---PRDTVDAELVRSLYGVE 245
Cdd:PRK11153 229 fshPKHPLTREFIQSTLHLD 248
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-231 |
2.23e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 1 MKNMSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksGQRQ 80
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---THVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 81 AAHR--------IALLPQsprapeaVTVAGLVRYGrhphqglLR-QWSRADE--RAVREALEATSTTELAGERLDRLSGG 149
Cdd:PRK09452 83 AENRhvntvfqsYALFPH-------MTVFENVAFG-------LRmQKTPAAEitPRVMEALRMVQLEEFAQRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 150 QRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGA 228
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
...
gi 2543669097 229 PRD 231
Cdd:PRK09452 229 PRE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-233 |
2.24e-24 |
|
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: 102.07 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSGLEVRGLHVGYPG----RAVVRDVGFSAPAGTVTSVVGPNGCGKS----TLLRALARLHRPSRGTVLADGADVWK 75
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 76 SGQRQAAH----RIALLPQSPRA---P---------EAVTVaglvrygrhpHQGLlrqwSRADERA-VREALEATSTTEl 138
Cdd:COG4172 81 LSERELRRirgnRIAMIFQEPMTslnPlhtigkqiaEVLRL----------HRGL----SGAAARArALELLERVGIPD- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 139 AGERLDR----LSGGQRQRCWLAMVLAQQtPVVLL-DEPTSALDlghVV---DVLELVRT-VAREGRTVVMVQHDLAAAA 209
Cdd:COG4172 146 PERRLDAyphqLSGGQRQRVMIAMALANE-PDLLIaDEPTTALD---VTvqaQILDLLKDlQRELGMALLLITHDLGVVR 221
|
250 260
....*....|....*....|....
gi 2543669097 210 RYSDHVIAMKDGEVVgEGAPRDTV 233
Cdd:COG4172 222 RFADRVAVMRQGEIV-EQGPTAEL 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-242 |
2.38e-24 |
|
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: 97.21 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLH--RPSRGTVLADGADVWK-SGQRQAAHRIA 86
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDlPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAPEAVTVAGLVRYgrhphqgllrqwsraderaVREAleatsttelagerldrLSGGQRQRCWLAMVLAQQTPV 166
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLRY-------------------VNEG----------------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH--DLAAAARySDHVIAMKDGEVVGEGaprdtvDAELVRSLY 242
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIVKSG------DKELALEIE 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-231 |
2.95e-24 |
|
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: 100.19 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQ--AAH--RIALLPQSPRAPEAVTVAG 102
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflPPEkrRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 103 LVRYGRhphqgllrQWSRADERAVREA--LEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGH 180
Cdd:TIGR02142 95 NLRYGM--------KRARPSERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 181 VVDVLELVRTVAREGRT-VVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-209 |
4.72e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.78 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRP---SRGTVLADGADVwkSGQRQAAHRI 85
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLVRYgrhphqGLLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQT 164
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAF------ALPPTIGRAQRRArVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAA 209
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQrGIPALLVTHDEEDAP 198
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
10-228 |
5.42e-24 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 101.50 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAV-VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:TIGR01192 335 VEFRHITFEFANSSQgVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSprapeavtvAGLVRYGRHPHQGLLRQWSRADEraVREALEATSTTE-----------LAGERLDRLSGGQRQRCWLA 157
Cdd:TIGR01192 415 FQD---------AGLFNRSIRENIRLGREGATDEE--VYEAAKAAAAHDfilkrsngydtLVGERGNRLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGA 228
Cdd:TIGR01192 484 RAILKNAPILVLDEATSALDVETEARVKNAIDAL-RKNRTTFIIAHRL-STVRNADLVLFLDQGRLIEKGS 552
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-229 |
7.99e-24 |
|
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: 96.41 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP--GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03244 3 IEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPrapeaVTVAGLVRYGRHPHqgllrqwSRADERAVREALEATSTTELAGERLDRL-----------SGGQRQRCWL 156
Cdd:cd03244 83 IPQDP-----VLFSGTIRSNLDPF-------GEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDlghvVDVLELVRTVARE---GRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEGAP 229
Cdd:cd03244 151 ARALLRKSKILVLDEATASVD----PETDALIQKTIREafkDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-227 |
1.11e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.57 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA---VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIA 86
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPrapeaVTVAGLVR----YGrhphqglLRQWSRADERAVREA---------LEATSTTELaGERLDRLSGGQRQR 153
Cdd:TIGR00958 559 LVGQEP-----VLFSGSVReniaYG-------LTDTPDEEIMAAAKAanahdfimeFPNGYDTEV-GEKGSQLSGGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALDlghvVDVLELVRTV-AREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEG 227
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALD----AECEQLLQESrSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-224 |
1.12e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.77 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSgLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLH--RPS---RGTVLADGADVW--KS 76
Cdd:PRK14239 1 MTEPI-LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYspRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQAAHRIALLPQSPRaPEAVTVAGLVRYGrhphqglLRQWSRAD----ERAVREALEATSTTELAGERLDR----LSG 148
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPN-PFPMSIYENVVYG-------LRLKGIKDkqvlDEAVEKSLKGASIWDEVKDRLHDsalgLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 149 GQRQRCWLAMVLAQQTPVVLLDEPTSALD---LGHVVDVLELVrtvaREGRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDpisAGKIEETLLGL----KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-222 |
1.60e-23 |
|
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: 95.23 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA-RLHRpsrgtvladgadvwKSGQRQAAHRIALLPQSPRAPEAvTVAG 102
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEK--------------LSGSVSVPGSIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 103 LVRYGrhphqgllrqwSRADERAVREALEATS------------TTELaGERLDRLSGGQRQRCWLAMVLAQQTPVVLLD 170
Cdd:cd03250 85 NILFG-----------KPFDEERYEKVIKACAlepdleilpdgdLTEI-GEKGINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 171 EPTSALDlGHVVDVL--ELVRTVAREGRTVVMVQHDLaAAARYSDHVIAMKDGE 222
Cdd:cd03250 153 DPLSAVD-AHVGRHIfeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-223 |
1.75e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 12 VRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwksgQRQAAHRIALLPQS 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----------SIPKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 92 PRAPEAVTVAGLVRYGRHPhqgllrqwSRADERAVREALEATSTTELAGERLDR-------------------------- 145
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAE--------LRALEAELEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsglgf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 -----------LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLgHVVDVLE--LVRtvaREGrTVVMVQHDlaaaaRY- 211
Cdd:COG0488 142 peedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLEefLKN---YPG-TVLVVSHD-----RYf 211
|
250
....*....|....*.
gi 2543669097 212 ----SDHVIAMKDGEV 223
Cdd:COG0488 212 ldrvATRILELDRGKL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-223 |
2.23e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 95.17 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAH---RIALLPQSPRA 94
Cdd:cd03292 10 YPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 95 PEAVTVAGLV----RYGRHPHqgllRQWsradERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLD 170
Cdd:cd03292 90 LPDRNVYENVafalEVTGVPP----REI----RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 171 EPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-213 |
2.34e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHR--PS---RGTVLADGADVWKSGQRQAA-- 82
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPVEvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRaPEAVTVAGLVRYGR--HPHQGLLRQWSradERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVL 160
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYGAriNGYKGDMDELV---ERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLAAAARYSD 213
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-229 |
2.34e-23 |
|
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: 94.79 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGR--AVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPrapeaVTVAGLVRYGRHPhqgllrqWSRADERAVREALEATsttelagERLDRLSGGQRQRCWLAMVLAQQTPVV 167
Cdd:cd03369 87 IPQDP-----TLFSGTIRSNLDP-------FDEYSDEEIYGALRVS-------EGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 168 LLDEPTSALDlghvVDVLELVRTVARE---GRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEGAP 229
Cdd:cd03369 148 VLDEATASID----YATDALIQKTIREeftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-203 |
2.48e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA----HRI 85
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPqsprapeAVTVAGLVRYgrhphqgllrqWSR---ADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQ 162
Cdd:PRK13539 83 AMKP-------ALTVAENLEF-----------WAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH 203
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-231 |
3.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 1 MKNMsspsgLEVRGLHVGY---PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADG-----AD 72
Cdd:PRK13650 1 MSNI-----IEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 73 VWksgqrQAAHRIALLPQSPRAP-EAVTVAGLVRYGRHpHQGLLRQWSRadERaVREALEATSTTELAGERLDRLSGGQR 151
Cdd:PRK13650 76 VW-----DIRHKIGMVFQNPDNQfVGATVEDDVAFGLE-NKGIPHEEMK--ER-VNEALELVGMQDFKEREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 152 QRCWLAMVLAQQTPVVLLDEPTSALD-LGHvvdvLELVRTVA--RE--GRTVVMVQHDLAAAArYSDHVIAMKDGEVVGE 226
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDpEGR----LELIKTIKgiRDdyQMTVISITHDLDEVA-LSDRVLVMKNGQVEST 221
|
....*
gi 2543669097 227 GAPRD 231
Cdd:PRK13650 222 STPRE 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-239 |
4.17e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYPGRA-VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSP---- 92
Cdd:PRK13657 343 SYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAglfn 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 93 RapeavTVAGLVRYGRhphqgllrqwSRADERAVREALEATSTTEL-----------AGERLDRLSGGQRQRCWLAMVLA 161
Cdd:PRK13657 423 R-----SIEDNIRVGR----------PDATDEEMRAAAERAQAHDFierkpdgydtvVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGAPRDTVD-----AE 236
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELVArggrfAA 565
|
...
gi 2543669097 237 LVR 239
Cdd:PRK13657 566 LLR 568
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-231 |
4.39e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPG-RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:PRK13652 4 IETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPE-AVTVAGLVRYGrhP-HQGLLRQwsrADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK13652 84 FQNPDDQIfSPTVEQDIAFG--PiNLGLDEE---TVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-229 |
4.83e-23 |
|
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: 94.42 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 1 MKNMSSPSgLEVRGLHVGYPGRA----VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKS 76
Cdd:COG4181 1 MSSSSAPI-IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQ-AAHRIA----------LLPqSPRAPEAVTVaglvrygrhPHQglLRQWSRADERAvREALEATSTTELAGERLDR 145
Cdd:COG4181 80 DEDArARLRARhvgfvfqsfqLLP-TLTALENVML---------PLE--LAGRRDARARA-RALLERVGLGHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDL--GHVvdVLELVRTVARE-GRTVVMVQHDLAAAARySDHVIAMKDGE 222
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAatGEQ--IIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*..
gi 2543669097 223 VVGEGAP 229
Cdd:COG4181 224 LVEDTAA 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-236 |
6.84e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 30 FSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKS--GQRQaahrIALLPQSPRAPEAVTVAGLVRYG 107
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppSRRP----VSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 108 RHPhqGLlrQWSRADERAVREALEATSTTELAgERL-DRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLE 186
Cdd:PRK10771 96 LNP--GL--KLNAAQREKLHAIARQMGIEDLL-ARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 187 LVRTVAREGR-TVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAE 236
Cdd:PRK10771 171 LVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-250 |
7.74e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.64 E-value: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRQAAHRIALLP 89
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRA-PEAVTVAGLVRYGRhpHQGLLRQWSRAderAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:PRK13537 87 QFDNLdPDFTVRENLLVFGR--YFGLSAAAARA---LVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAEL---VRSLYGVE 245
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIYGPD 241
|
....*
gi 2543669097 246 ADILR 250
Cdd:PRK13537 242 PVALR 246
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-229 |
8.43e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 8.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGA--DVWKSGQRQAAHRIAL 87
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAPEAVT-VAGLVRYGrhphqglLRQWSRADE---RAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQ 163
Cdd:PRK13638 82 VFQDPEQQIFYTdIDSDIAFS-------LRNLGVPEAeitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 164 TPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-257 |
8.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 8.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YPGRAVVrDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV-LADGADVWKSGQRQ---AAHRIALLPQSPRA 94
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIVVSSTSKQKEikpVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 95 PE-AVTVAGLVRYGRhphqgllRQWSRADERAVREALEATSTTELAGERLDR----LSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:PRK13643 96 QLfEETVLKDVAFGP-------QNFGIPKEKAEKIAAEKLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDaelvrslygvEADIL 249
Cdd:PRK13643 169 DEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ----------EVDFL 238
|
....*...
gi 2543669097 250 RAPVDGSP 257
Cdd:PRK13643 239 KAHELGVP 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-227 |
1.06e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTvLADGADVWKSGQRQAAHRIALLP 89
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGT-LNIAGNHFDFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSprapeavtvAGLV--RYGRHPH----QGLLRQWSR----ADERAVREALEATSTTELAgERLDR----LSGGQRQRCW 155
Cdd:PRK11124 82 RN---------VGMVfqQYNLWPHltvqQNLIEAPCRvlglSKDQALARAEKLLERLRLK-PYADRfplhLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 156 LAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-234 |
1.10e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 2 KNMSSPSGLEVRGLHVGypgravVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA 81
Cdd:PRK10070 27 QGLSKEQILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 AH----RIALLPQSPRAPEAVTVAGLVRYGRHpHQGLLRQWSRadERAVrEALEATSTTELAGERLDRLSGGQRQRCWLA 157
Cdd:PRK10070 101 REvrrkKIAMVFQSFALMPHMTVLDNTAFGME-LAGINAEERR--EKAL-DALRQVGLENYAHSYPDELSGGMRQRVGLA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 158 MVLAQQTPVVLLDEPTSALD-LGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVD 234
Cdd:PRK10070 177 RALAINPDILLMDEAFSALDpLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-224 |
1.13e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwKSGQRQaahRIALLP 89
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV---KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRA--PEAvTVAGLVRYGRhphqgllrqwSRADERAVREALEATStteLAGERLDR----LSGGQRQRCWLAMVLAQQ 163
Cdd:COG0488 385 QHQEEldPDK-TVLDELRDGA----------PGGTEQEVRGYLGRFL---FSGDDAFKpvgvLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 164 TPVVLLDEPTSALDLgHVVDVLE--LVRTvarEGrTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:COG0488 451 PNVLLLDEPTNHLDI-ETLEALEeaLDDF---PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-203 |
2.44e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 91.65 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKsgQRQAAHR-IALL 88
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE--QRDEPHEnILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPHQGllrqwsraDERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGG--------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH 203
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-231 |
2.83e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHR------PSRGTVLADGADVWKSGQRQAAHRIALLPQSPRAP 95
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 96 EAVTVAGLVRYGRHPHqGLLRQwsRADERAVREALEATSTTELAGERLD----RLSGGQRQRCWLAMVLAQQTPVVLLDE 171
Cdd:PRK14246 103 PHLSIYDNIAYPLKSH-GIKEK--REIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 172 PTSALDLGHVVDVLELVRTVAREgRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
24-227 |
2.96e-22 |
|
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: 96.35 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV------WKSGQ------------RQAAHRI 85
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiadpaWLRRQmgvvlqenvlfsRSIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALlpQSPRAPEAVTVAGLVRYGRHphqgllrqwsraderAVREALEATSTTELaGERLDRLSGGQRQRCWLAMVLAQQTP 165
Cdd:TIGR01846 552 AL--CNPGAPFEHVIHAAKLAGAH---------------DFISELPQGYNTEV-GEKGANLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEG 227
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRL-STVRACDRIIVLEKGQIAESG 673
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-223 |
3.16e-22 |
|
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: 91.85 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 31 SAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAhrIALLPQSPRAPEAVTVAGLVRYGRHP 110
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP--VSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 111 HQGLlrqwsRADERavrEALEATSTTELAGERLDRL----SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLE 186
Cdd:TIGR01277 98 GLKL-----NAEQQ---EKVVDAAQQVGIADYLDRLpeqlSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2543669097 187 LVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:TIGR01277 170 LVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-237 |
5.08e-22 |
|
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: 95.49 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 7 PSG-LEVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAH 83
Cdd:TIGR01842 313 PEGhLSVENVTIVPPGgkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEAVTVAGLVRYGRHphqgllrqwsrADERAVREALEATSTTEL-----------AGERLDRLSGGQRQ 152
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGEN-----------ADPEKIIEAAKLAGVHELilrlpdgydtvIGPGGATLSGGQRQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGaPRDT 232
Cdd:TIGR01842 462 RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGC-VDKILVLQDGRIARFG-ERDE 539
|
....*
gi 2543669097 233 VDAEL 237
Cdd:TIGR01842 540 VLAKL 544
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-221 |
5.33e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 91.73 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGL-------HVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA 82
Cdd:COG4778 5 LEVENLsktftlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQS------------PRAPEAVTVAglvrygrHPhqglLRQWSRADERAVREALEATSTTELAgERLDRL---- 146
Cdd:COG4778 85 REILALRRRtigyvsqflrviPRVSALDVVA-------EP----LLERGVDREEARARARELLARLNLP-ERLWDLppat 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 147 -SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDG 221
Cdd:COG4778 153 fSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-227 |
5.55e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTvLADGADVWKSGQRQAAHRIALL 88
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ-LNIAGHQFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSprapeavtvAGLV--RYGRHPH----QGLL----RQWSRADERAVREALEATSTTELAgERLDR----LSGGQRQRC 154
Cdd:COG4161 81 RQK---------VGMVfqQYNLWPHltvmENLIeapcKVLGLSKEQAREKAMKLLARLRLT-DKADRfplhLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-215 |
5.66e-22 |
|
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: 92.04 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPS-----------------RGTVLADGADVWKSGQRQAAHRIALLPQSPRApea 97
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwdeildefRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 vtVAGLVRygrhphqGLLrqwSRADERAVREAL-EATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:cd03236 103 --VKGKVG-------ELL---KKKDERGKLDELvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 2543669097 177 DLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHV 215
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-245 |
5.80e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.07 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 6 SPSGLEVRGLHVgYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKS-TLLRALARLH---RPSRGTVLADGADVWKSGQRqa 81
Cdd:PRK10418 1 MPQQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 AHRIALLPQSPRApeavTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTElaGERLDRL-----SGGQRQRCWL 156
Cdd:PRK10418 78 GRKIATIMQNPRS----AFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLEN--AARVLKLypfemSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 157 AMVLAQQTPVVLLDEPTSALDL---GHVVDVLElvRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG------ 227
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVvaqARILDLLE--SIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGdvetlf 229
|
250 260
....*....|....*....|..
gi 2543669097 228 -APRDTVDAELV---RSLYGVE 245
Cdd:PRK10418 230 nAPKHAVTRSLVsahLALYGME 251
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-227 |
8.88e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.89 E-value: 8.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA--VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQ-RQAahr 84
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSEAAlRQA--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQSPrapeavtvaglvrygrHPHQGLLRQ-----WSRADERAVREALEATSTTELA--GERLD--------RLSGG 149
Cdd:PRK11160 416 ISVVSQRV----------------HLFSATLRDnlllaAPNASDEALIEVLQQVGLEKLLedDKGLNawlgeggrQLSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 150 QRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAReGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEG 227
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-226 |
1.60e-21 |
|
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: 91.02 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 23 AVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK--SGQRQAAHR-IALLPQSprAPEAVT 99
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldRKQRRAFRRdVQLVFQD--SPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 100 VAGLVRYG-RHPHQGLLRQWSRADERAVREALEATsttELAGERLDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTS 174
Cdd:TIGR02769 103 PRMTVRQIiGEPLRHLTSLDESEQKARIAELLDMV---GLRSEDADKlprqLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 175 ALDLGHVVDVLELVRTV-AREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-238 |
2.08e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.44 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRIALL 88
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPR-APEaVTVAGLVRYGRHPHQ-GLLRQwsRADERAVREALEATsttelaGERLD------RLSGGQRQRCWLAMVL 160
Cdd:PRK11288 85 YQELHlVPE-MTVAENLYLGQLPHKgGIVNR--RLLNYEAREQLEHL------GVDIDpdtplkYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVV-----GEGAPRDTVDA 235
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVatfddMAQVDRDQLVQ 235
|
...
gi 2543669097 236 ELV 238
Cdd:PRK11288 236 AMV 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-224 |
2.12e-21 |
|
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: 90.02 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA-RLHRPS--RGTVLADG----ADVWKSgqrqaahRIALLPQSPRA 94
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgRVEGGGttSGQILFNGqprkPDQFQK-------CVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 95 PEAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTS 174
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 175 ALDLGHVVDVLELVRTVAREGRTVVMVQH----DLaaaARYSDHVIAMKDGEVV 224
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIV 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-223 |
2.67e-21 |
|
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: 89.84 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 20 PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPRApEAVT 99
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVL-FARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 100 VAGLVRYGRH--PHQGLLRQWSRADERAVREALEATSTTElAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:cd03248 104 LQDNIAYGLQscSFECVKEAAQKAHAHSFISELASGYDTE-VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2543669097 178 LGHVVDVLELVRTvAREGRTVVMVQHDLAAAARySDHVIAMKDGEV 223
Cdd:cd03248 183 AESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-221 |
2.70e-21 |
|
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: 89.83 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA--HRIALLP-QSPRAPEAVTVa 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPwLTVRENIALAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 102 glvrygrhphQGLLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDL-- 178
Cdd:TIGR01184 80 ----------DRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAlt 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2543669097 179 -GHVVDvlELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDG 221
Cdd:TIGR01184 150 rGNLQE--ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-204 |
3.30e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 8 SGLEVRGLHVGYPG----RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-- 81
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 82 --AHriALLPQsprapeaVTVAGLVRYGRHphqglLRQWSRADERAV-REALEATSTTELAGERLDRLSGGQRQRCWLAM 158
Cdd:COG4525 82 fqKD--ALLPW-------LNVLDNVAFGLR-----LRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTV-AREGRTVVMVQHD 204
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-231 |
3.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YPGRAVVrDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ----RQAAHRIALLPQSPRA 94
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 95 PE-AVTVAGLVRYGrhPhqgllRQWSRADERAVREALEATSTTELAGERLDR----LSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:PRK13649 97 QLfEETVLKDVAFG--P-----QNFGVSQEEAEALAREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 170 DEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-235 |
3.88e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGadvwksgqrqaahRIAllpqsprAPEAVTvAGL 103
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVS-------ALLELG-AGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 104 vrygrHPH---------QGLLRQWSRADERAVREALEATSttELaGERLD----RLSGGQRQRcwLAMVLAQQTP--VVL 168
Cdd:COG1134 100 -----HPEltgreniylNGRLLGLSRKEIDEKFDEIVEFA--EL-GDFIDqpvkTYSSGMRAR--LAFAVATAVDpdILL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 169 LDEPTSaldlghVVDV------LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDA 235
Cdd:COG1134 170 VDEVLA------VGDAafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-236 |
7.21e-21 |
|
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: 88.70 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV------WKSGQ------------RQAA 82
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpaWLRRQvgvvlqenvlfnRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HRIALLPQSPRAPEAVTVAGLVryGRHPHqgllrqwsraderaVREALEATSTteLAGERLDRLSGGQRQRCWLAMVLAQ 162
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLA--GAHDF--------------ISELPEGYDT--IVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVArEGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGAPRDTVDAE 236
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-241 |
7.47e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA--RLHRPSRGTVLADGADV--WKSGQRqAAHRI 85
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDIleLSPDER-ARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLVR--YGRhphQGLLRQWSRADERAVREALEAtstTELAGERLDR-----LSGGQRQRCWLAM 158
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNFLRtaLNA---RRGEELSAREFLKLLKEKMKE---LGLDEDFLDRyvnegFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 159 VLAQQTPVVLLDEPTSALDlghvVDVL----ELVRTVAREGRTVVMVQH-----DLAAAarysDHVIAMKDGEVVGEGap 229
Cdd:COG0396 154 MLLLEPKLAILDETDSGLD----IDALrivaEGVNKLRSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSG-- 223
|
250
....*....|..
gi 2543669097 230 rdtvDAELVRSL 241
Cdd:COG0396 224 ----GKELALEL 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-231 |
1.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGAD------VWKSgqRQAAhriALLPQSP-RAPE 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenLWDI--RNKA---GMVFQNPdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 97 AVTVAGLVRYGrhPHQ-GLLRQWSRadERaVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSA 175
Cdd:PRK13633 100 ATIVEEDVAFG--PENlGIPPEEIR--ER-VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 176 LDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKE 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-231 |
1.19e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRD---VGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIA 86
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAP-EAVTVAGLVRYGRHpHQGLLRQwsrADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTP 165
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDVAFGME-NQGIPRE---EMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVA-REGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-245 |
1.36e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR-IALL 88
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPHQGL----LRQWSRADERAVREALEATSTTELaGERLDRLSGGQRQRCWLAMVLAQQT 164
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVcgvnIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGV 244
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGR 244
|
.
gi 2543669097 245 E 245
Cdd:PRK09700 245 E 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-231 |
2.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR--IALLPQSPRA---PEavTVA 101
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRkkVGLVFQYPEYqlfEE--TIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 102 GLVRYGrhphqglLRQWSRADERAVREALEATSTTELAGERL-DR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:PRK13637 103 KDIAFG-------PINLGLSEEEIENRVKRAMNIVGLDYEDYkDKspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 177 DLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-221 |
2.46e-20 |
|
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: 87.00 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 20 PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR----IALLPQSPRAP 95
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 96 EAvTVAGLVRYGRhphqgllrQWSRADERAVREA---------LEATSTTELaGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:cd03290 92 NA-TVEENITFGS--------PFNKQRYKAVTDAcslqpdidlLPFGDQTEI-GERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 167 VLLDEPTSALDLgHVVD------VLELVRTvarEGRTVVMVQHDLAAAArYSDHVIAMKDG 221
Cdd:cd03290 162 VFLDDPFSALDI-HLSDhlmqegILKFLQD---DKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-242 |
4.56e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 7 PSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAHR-- 84
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLPMHKra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 ---IALLPQsprapEA-----VTVAglvrygrhphQGLL-----RQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQ 150
Cdd:COG1137 77 rlgIGYLPQ-----EAsifrkLTVE----------DNILavlelRKLSKKErEERLEELLEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 151 RQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPR 230
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
250
....*....|..
gi 2543669097 231 DTVDAELVRSLY 242
Cdd:COG1137 222 EILNNPLVRKVY 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-226 |
1.27e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 14 GLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK-SGQRQAAHR--IALLPQ 90
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRrdIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 91 SprAPEAVTVAGLVRYG-RHPHQGLLRQWSRADERAVREALEAtstTELAGERLDR----LSGGQRQRCWLAMVLAQQTP 165
Cdd:PRK10419 97 D--SISAVNPRKTVREIiREPLRHLLSLDKAERLARASEMLRA---VDLDDSVLDKrppqLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVAREGRTV-VMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-231 |
1.69e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ----RQAAHRIALLPQSPRAP--EAv 98
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVFQFPESQlfED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TVAGLVRYGRHPHQGLLRQwsrADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDL 178
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDE---VKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 179 GHVVDVLELVRTVA-REGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13646 179 QSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-215 |
1.82e-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: 87.92 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPS-----------------RGTVLADGADVWKSGQRQAAHRIALLPQSPRApea 97
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELQDYFKKLANGEIKVAHKPQYVDLIPKV--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 vtVAGLVRygrhphqGLLRqwsRADER-AVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:COG1245 176 --FKGTVR-------ELLE---KVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|....*....
gi 2543669097 177 DLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHV 215
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-227 |
2.00e-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: 84.51 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 13 RGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWksgqrqaahriaLLpqsp 92
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS------------LL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 93 rapeAVTVaglvryGRHPHQ---------GLLRQWSRADERAVREALEATSttELaGERLDR----LSGGQRQRCWLAMV 159
Cdd:cd03220 90 ----GLGG------GFNPELtgreniylnGRLLGLSRKEIDEKIDEIIEFS--EL-GDFIDLpvktYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-218 |
2.38e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 16 HVGYP--GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPr 93
Cdd:PRK10247 12 NVGYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 94 apeavtvaglVRYGRHPHQGLLRQWS----RADERAVREALEatsTTELAGERLDR----LSGGQRQRCWLAMVLAQQTP 165
Cdd:PRK10247 91 ----------TLFGDTVYDNLIFPWQirnqQPDPAIFLDDLE---RFALPDTILTKniaeLSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDlAAAARYSDHVIAM 218
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD-KDEINHADKVITL 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-227 |
2.74e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGR--AVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSprapeaV-----TVAGLVRYGRHphqgllRQWSRAD-ERAVR--EALEATSTTE-----LAGERLDRLSGGQRQRC 154
Cdd:PRK11176 422 VSQN------VhlfndTIANNIAYART------EQYSREQiEEAARmaYAMDFINKMDngldtVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDlghvvdvLELVRTVA------REGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEG 227
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALD-------TESERAIQaaldelQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
10-241 |
3.00e-19 |
|
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: 84.62 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALArlHRPS----RGTVLADGADVWK-SGQRQAAHR 84
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIA--GHPSyevtSGTILFKGQDLLElEPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQSPRAPEAVTVAGLVRYGRHPHQGlLRQWSRADERAVREAL-EATSTTELAGERLDR-----LSGGQRQRCWLAM 158
Cdd:TIGR01978 79 LFLAFQYPEEIPGVSNLEFLRSALNARRS-ARGEEPLDLLDFEKLLkEKLALLDMDEEFLNRsvnegFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHdlaaaarYS--------DHVIAMKDGEVVGEGapr 230
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH-------YQrllnyikpDYVHVLLDGRIVKSG--- 227
|
250
....*....|.
gi 2543669097 231 dtvDAELVRSL 241
Cdd:TIGR01978 228 ---DVELAKEL 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-235 |
4.54e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.09 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGR----AVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA--- 82
Cdd:PRK10535 5 LELKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 --------HRIALLPQSPrAPEAVTV----AGLVRYGRHphqgllrqwSRADERAVREALeatsttelaGERLD----RL 146
Cdd:PRK10535 85 rehfgfifQRYHLLSHLT-AAQNVEVpavyAGLERKQRL---------LRAQELLQRLGL---------EDRVEyqpsQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGE 226
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
....*....
gi 2543669097 227 GAPRDTVDA 235
Cdd:PRK10535 225 PPAQEKVNV 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
24-221 |
5.23e-19 |
|
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: 83.17 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK-SGQRQAAHRIA----------LLPQSp 92
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlSSNERAKLRNKklgfiyqfhhLLPDF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 93 RAPEAVTVAGLVRYGRHPHqgllrqwsrADERAvREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:TIGR02211 99 TALENVAMPLLIGKKSVKE---------AKERA-YEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2543669097 173 TSALDLGHVVDVLELVRTVAREGRT-VVMVQHDLAAAARYsDHVIAMKDG 221
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-229 |
7.13e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSgLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgQRQAAH 83
Cdd:PRK11300 1 MSQPL-LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI----EGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLP-----QSPRAPEAVTVAG--LVRYGRHPHQGLLRQW--SRADERAVREALEATST-------TELAGERLDRLS 147
Cdd:PRK11300 76 QIARMGvvrtfQHVRLFREMTVIEnlLVAQHQQLKTGLFSGLlkTPAFRRAESEALDRAATwlervglLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 148 GGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
...
gi 2543669097 227 GAP 229
Cdd:PRK11300 236 GTP 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-227 |
8.72e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGR-----------AVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRpSRGTVLADGADVWKSGQ 78
Cdd:PRK15134 276 LDVEQLQVAFPIRkgilkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 79 RQ---AAHRIALLPQSPRA---PEaVTVAGLVRYGRHPHQGLLRQWSRadERAVREALEATStteLAGERLDR----LSG 148
Cdd:PRK15134 355 RQllpVRHRIQVVFQDPNSslnPR-LNVLQIIEEGLRVHQPTLSAAQR--EQQVIAVMEEVG---LDPETRHRypaeFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 149 GQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGR-TVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-235 |
9.00e-19 |
|
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: 86.33 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYpGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPRAPEA 97
Cdd:TIGR01193 484 GY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 VTVAGLVrYGRHP---HQGLLRQWSRADERAVREALEATSTTELAGERLDrLSGGQRQRCWLAMVLAQQTPVVLLDEPTS 174
Cdd:TIGR01193 563 SILENLL-LGAKEnvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 175 ALDL---GHVVDVLelvrtVAREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRDTVDA 235
Cdd:TIGR01193 641 NLDTiteKKIVNNL-----LNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-222 |
1.03e-18 |
|
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: 80.57 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwksgQRQAAHRIALLP 89
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QsprapeavtvaglvrygrhphqgllrqwsraderavrealeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 170 DEPTSALDLGHvVDVLElvRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGE 222
Cdd:cd03221 95 DEPTNHLDLES-IEALE--EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-231 |
1.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADG----ADVWKSGQRQAAHRIALLPQSPRAP--EAvTV 100
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQFPEAQlfEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 101 AGLVRYGrhPhqgllRQWSRADERAVREALEATSTTELAGERLDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:PRK13641 104 LKDVEFG--P-----KNFGFSEDEAKEKALKWLKKVGLSEDLISKspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 177 DLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-233 |
1.08e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.62 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVR---DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVW-------KSGQRQAAHRIALLPQs 91
Cdd:TIGR03269 294 RGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWvdmtkpgPDGRGRAKRYIGILHQ- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 92 prapeavtvaglvRYGRHPHQGLLRQWSRA------DERAVREAL----EATSTTELAGERLDR----LSGGQRQRCWLA 157
Cdd:TIGR03269 373 -------------EYDLYPHRTVLDNLTEAiglelpDELARMKAVitlkMVGFDEEKAEEILDKypdeLSEGERHRVALA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTvARE--GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTV 233
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSILK-AREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-203 |
1.16e-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: 82.16 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKsgQRQAAHR-IALL 88
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--QRDSIARgLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYGRHPHqgllrqwsraDERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADH----------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH 203
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-227 |
1.32e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 84.25 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-------GRAVVR---DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVW---KS 76
Cdd:PRK11308 6 LQAIDLKKHYPvkrglfkPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQAAHRIALLPQSPrapeavtvaglvrYG----RHPHQGLLR-------QWSRADERAvrEALEATSTTELAGERLDR 145
Cdd:PRK11308 86 AQKLLRQKIQIVFQNP-------------YGslnpRKKVGQILEepllintSLSAAERRE--KALAMMAKVGLRPEHYDR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 ----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKD 220
Cdd:PRK11308 151 yphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYL 230
|
....*..
gi 2543669097 221 GEVVGEG 227
Cdd:PRK11308 231 GRCVEKG 237
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-206 |
2.17e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPS-----------------RGTVLADGADVWKSGQRQAAHRIALLPQSPRApea 97
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQNYFKKLYNGEIKVVHKPQYVDLIPKV--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 vtVAGLVRygrhphqGLLRqwsRADER-AVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:PRK13409 176 --FKGKVR-------ELLK---KVDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 2543669097 177 DLGHVVDVLELVRTVArEGRTVVMVQHDLA 206
Cdd:PRK13409 244 DIRQRLNVARLIRELA-EGKYVLVVEHDLA 272
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-226 |
2.22e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA----HRIA-------LLPQSp 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGfiyqfhhLLPDF- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 93 RAPEAVTVAGLVRyGRHPHQgllrqwsrADERAvREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:PRK11629 103 TALENVAMPLLIG-KKKPAE--------INSRA-LEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 173 TSALDLGHVVDVLELVRTV-AREGRTVVMVQHDLAAAARYSDHViAMKDGEVVGE 226
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
28-247 |
2.29e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 28 VGFSAPAGTVTSVVGPNGCGKSTLLRALARL---HRPSRGTVLADGADVWKSGQ------RQAAHRIALLPQ-----SPR 93
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlardirKSRANTGYIFQQfnlvnRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 94 APEAVTVAGLvryGRHPH-QGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:PRK09984 103 VLENVLIGAL---GSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 173 TSALDLGHVVDVLELVRTVAR-EGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPR----DTVDaELVRSLYGVEAD 247
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQqfdnERFD-HLYRSINRVEEN 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-227 |
2.39e-18 |
|
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: 82.00 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSgQRQAAHRIALLPQSPRA-----PEAV 98
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR-RKKFLRRIGVVFGQKTQlwwdlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TVAGLVR-YGRHPhqgllrqwSRADERaVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:cd03267 115 SFYLLAAiYDLPP--------ARFKKR-LDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 178 LGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:cd03267 186 VVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-208 |
3.85e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA--HRIAL 87
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVvfQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSprapeavTVAGLVRYGRHphqglLRQWSRADERAV-REALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK11248 82 LPWR-------NVQDNVAFGLQ-----LAGVEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAA 208
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEA 192
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
10-227 |
3.86e-18 |
|
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: 84.22 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP--GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIAL 87
Cdd:TIGR03796 478 VELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQsprapEAVTVAGLVRYGrhphqglLRQWSRA--DERAVREALEATSTTELAG----------ERLDRLSGGQRQRCW 155
Cdd:TIGR03796 558 VDQ-----DIFLFEGTVRDN-------LTLWDPTipDADLVRACKDAAIHDVITSrpggydaelaEGGANLSGGQRQRLE 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 156 LAMVLAQQTPVVLLDEPTSALDlghVVDVLELVRTVAREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEG 227
Cdd:TIGR03796 626 IARALVRNPSILILDEATSALD---PETEKIIDDNLRRRGCTCIIVAHRL-STIRDCDEIIVLERGKVVQRG 693
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
128-232 |
5.26e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 128 EALE-ATSTTELAG---ERLDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVV 199
Cdd:PRK13651 140 EAKKrAAKYIELVGldeSYLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTII 219
|
90 100 110
....*....|....*....|....*....|...
gi 2543669097 200 MVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDT 232
Cdd:PRK13651 220 LVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-241 |
7.49e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRI-ALLPQSPRAP- 95
Cdd:PRK13644 11 YPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLvGIVFQNPETQf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 96 EAVTVAGLVRYGrhPHQGLLRQWSRadERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSA 175
Cdd:PRK13644 91 VGRTVEEDLAFG--PENLCLPPIEI--RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 176 LDLGHVVDVLELVRTVAREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSL 241
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-240 |
7.50e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.19 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:PRK13632 9 KVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAP-EAVTVAGLVRYGRHPhqgllRQWSRADERA-VREALEATSTTELagerLDR----LSGGQRQRCWLAMVLAQ 162
Cdd:PRK13632 89 FQNPDNQfIGATVEDDIAFGLEN-----KKVPPKKMKDiIDDLAKKVGMEDY----LDKepqnLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVAREG-RTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRDTV-DAELVRS 240
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILnNKEILEK 238
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-290 |
1.45e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.90 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLadgadvwksgqrqAAHRIALLPQSPRAPEAvTVA 101
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQQAWIMNA-TVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 102 GLVRYGRHPHQGLLRQWSR-----ADERAVREALEatstTELaGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:PTZ00243 739 GNILFFDEEDAARLADAVRvsqleADLAQLGGGLE----TEI-GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 177 DlGHVVD-VLELVRTVAREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGVEADILRAPVDG 255
Cdd:PTZ00243 814 D-AHVGErVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKDSKEGD 891
|
250 260 270
....*....|....*....|....*....|....*.
gi 2543669097 256 SPVVVPRARTADANLADPYPADAGQVD-AGRVEAAS 290
Cdd:PTZ00243 892 ADAEVAEVDAAPGGAVDHEPPVAKQEGnAEGGDGAA 927
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-226 |
2.42e-17 |
|
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: 81.79 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGL---HVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHrPSR--GTVLADGADV-WKSGQRQAAH 83
Cdd:TIGR02633 258 LEARNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVdIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPR---------APEAVTVAGLVRYGrhphqGLLRQWSRADERAVREALE----ATSTTELAgerLDRLSGGQ 150
Cdd:TIGR02633 337 GIAMVPEDRKrhgivpilgVGKNITLSVLKSFC-----FKMRIDAAAELQIIGSAIQrlkvKTASPFLP---IGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 151 RQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-227 |
3.81e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.04 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLhRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:PRK11174 350 IEAEDLEILSPdGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAvTVAGLVRYGRHphqgllrqwsRADERAVREALEATSTTELA-----------GERLDRLSGGQRQRCWLA 157
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLLGNP----------DASDEQLQQALENAWVSEFLpllpqgldtpiGDQAAGLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLG---HVVDVLelvrTVAREGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEG 227
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHseqLVMQAL----NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-231 |
6.24e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.38 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 1 MKNMSSPSGLEVRGLHVGY--PGRAV--VRDVGFSAPAGTVTSVVGPNGCGKS----TLLRALARLHRPSrGTVLADGAD 72
Cdd:PRK09473 4 LAQQQADALLDVKDLRVTFstPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 73 VWKSGQRQ----AAHRIALLPQSP--------RAPEAVT-VAGLvrygrhpHQGLLRqwSRADERAVReALEATSTTElA 139
Cdd:PRK09473 83 ILNLPEKElnklRAEQISMIFQDPmtslnpymRVGEQLMeVLML-------HKGMSK--AEAFEESVR-MLDAVKMPE-A 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 140 GERLD----RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRT-VVMVQHDLAAAARYSDH 214
Cdd:PRK09473 152 RKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDK 231
|
250
....*....|....*..
gi 2543669097 215 VIAMKDGEVVGEGAPRD 231
Cdd:PRK09473 232 VLVMYAGRTMEYGNARD 248
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-224 |
9.45e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 9.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 17 VGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwksgQRQAAHRIALLPQS----P 92
Cdd:PRK09544 12 VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKlyldT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 93 RAPEAVTVAGLVRYGRHphqgllrqwsRADeraVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTK----------KED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 173 TSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLaaaarysdHVIAMKDGEVV 224
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL--------HLVMAKTDEVL 192
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-231 |
1.17e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.97 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQaaHRIALLPQSPRAPEAVTVA 101
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 102 GLVRYG-----RHPhqgllRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:PRK10851 93 DNIAFGltvlpRRE-----RPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 177 DLGHVVDVLELVRTVAREGR-TVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-229 |
1.28e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGAdvwksgqrqaahRIALLPQSPRApeav 98
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK------------RMNDVPPAERG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 tvAGLV--RYGRHPHQGLLRQWS------RADERAVREALEATSTTELAGERLDR----LSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK11000 77 --VGMVfqSYALYPHLSVAENMSfglklaGAKKEEINQRVNQVAEVLQLAHLLDRkpkaLSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 167 VLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-241 |
2.26e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 7 PSGLEVRGLHvgypGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRI 85
Cdd:PRK11288 255 EVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiRAGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGlVR-------YGRHPHQGLL--RQWSR--ADERAVREALEATSTTELAGErldrLSGGQRQRC 154
Cdd:PRK11288 331 MLCPEDRKAEGIIPVHS-VAdninisaRRHHLRAGCLinNRWEAenADRFIRSLNIKTPSREQLIMN----LSGGNQQKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEgAPRDTVD 234
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE-LAREQAT 484
|
....*..
gi 2543669097 235 AELVRSL 241
Cdd:PRK11288 485 ERQALSL 491
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-228 |
2.43e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGY----PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK--------SG 77
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqvielSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 78 QRQAAHR------IALLPQSPRAP--EAVTVAGLVRYGRHPHQGLLRQWSRADERAVREALEATSTTELAGERLDRLSGG 149
Cdd:PRK10261 93 QSAAQMRhvrgadMAMIFQEPMTSlnPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 150 QRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGA 228
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-242 |
2.49e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR-IALL 88
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQsprapEAVTVAGLVRYGRHPHQGLLRQWSRADERAVR--EALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK10895 84 PQ-----EASIFRRLSVYDNLMAVLQIRDDLSAEQREDRanELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLY 242
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-226 |
4.29e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGL---HVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRAL-ARLHRPSRGTVLADGADVWKSGQRQA-AHR 84
Cdd:PRK13549 260 LEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAiAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 IALLPQSPRAPEAVTVAG------LVRYGRHPHQGLLRqwSRADERAVREALEA----TSTTELAgerLDRLSGGQRQRC 154
Cdd:PRK13549 340 IAMVPEDRKRDGIVPVMGvgknitLAALDRFTGGSRID--DAAELKTILESIQRlkvkTASPELA---IARLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-247 |
5.49e-16 |
|
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: 78.06 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPrapeaVTVAGL 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP-----VLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 104 VRYGRHPhqgllrqWSRADERAVREALEATSTTELAGERLDR-----------LSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:TIGR00957 1376 LRMNLDP-------FSQYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 173 TSALDLghvvDVLELVRTVAR---EGRTVVMVQHDLAAAARYSdHVIAMKDGEVVGEGAPRDTVDAELVrsLYGVEAD 247
Cdd:TIGR00957 1449 TAAVDL----ETDNLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRGI--FYSMAKD 1519
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-203 |
6.37e-16 |
|
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: 73.73 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP-GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwksgQRQAAHRIALL 88
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPeavtvaglvrygrhphQGLLRQ-----WSraderavrealeatsttelagerlDRLSGGQRQRCWLAMVLAQQ 163
Cdd:cd03223 70 PQRPYLP----------------LGTLREqliypWD------------------------DVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2543669097 164 TPVVLLDEPTSALDlghvVDVLELVRTVARE-GRTVVMVQH 203
Cdd:cd03223 110 PKFVFLDEATSALD----EESEDRLYQLLKElGITVISVGH 146
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-232 |
7.51e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 7.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHV-GYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQRQAAhRIA 86
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItgLSPRERRRL-GVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPR----APEAvTVA---GLVRYGRHP--HQGLLRqWSRADERAvREALE-----ATSTTELAGerldRLSGGQRQ 152
Cdd:COG3845 337 YIPEDRLgrglVPDM-SVAenlILGRYRRPPfsRGGFLD-RKAIRAFA-EELIEefdvrTPGPDTPAR----SLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDT 232
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-231 |
7.80e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 3 NMSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV---WKSGQR 79
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 80 QAAHRIALLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRAderAVREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHS---TVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 160 LAQQTPVVLLDEPTSALD---LGHVVDVL-ELVRTVareGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRD 231
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDpitMGVLVKLIsELNSAL---GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-224 |
1.32e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQ---RQAAHRIALLPQSPRA---PEaV 98
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPLAslnPR-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TVAG-----LVRYgrHPHqgLLRQwsraderAVREALEATST-TELAGERLDR----LSGGQRQRCWLAMVLAQQTPVVL 168
Cdd:PRK15079 116 TIGEiiaepLRTY--HPK--LSRQ-------EVKDRVKAMMLkVGLLPNLINRypheFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 169 LDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
21-239 |
1.53e-15 |
|
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: 76.53 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHRIAL---LPQSPRAPEA 97
Cdd:TIGR03797 465 GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL--AGLDVQAVRRQLgvvLQNGRLMSGS 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 V--TVAGLVRYGrhphqgLLRQWSRADERAVREALEA------TSTTELAGErldrLSGGQRQRCWLAMVLAQQTPVVLL 169
Cdd:TIGR03797 543 IfeNIAGGAPLT------LDEAWEAARMAGLAEDIRAmpmgmhTVISEGGGT----LSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 170 DEPTSALD---LGHVVDVLElvrtvaREGRTVVMVQHDLaAAARYSDHVIAMKDGEVVGEG-----APRDTVDAELVR 239
Cdd:TIGR03797 613 DEATSALDnrtQAIVSESLE------RLKVTRIVIAHRL-STIRNADRIYVLDAGRVVQQGtydelMAREGLFAQLAR 683
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-229 |
1.71e-15 |
|
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: 74.37 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksgqrqaahriALLPQSPRAPEAVTVAGLVrYGRHPHQGL 114
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTVRDLL-SSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 115 LRQWSRaderavrEALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVA-R 193
Cdd:cd03237 92 HPYFKT-------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAeN 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 2543669097 194 EGRTVVMVQHDLAAAARYSDHVIAMkDGE--VVGEGAP 229
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVF-EGEpsVNGVANP 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-236 |
1.83e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 2 KNMSSPSGLEVRGL------HVGY-PG-RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV 73
Cdd:PLN03232 1221 ENNRPVSGWPSRGSikfedvHLRYrPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 74 WKSGQRQAAHRIALLPQSPrapeaVTVAGLVR-----YGRHPHQGLLRQWSRADERAV--REALEATSTTELAGErldRL 146
Cdd:PLN03232 1301 AKFGLTDLRRVLSIIPQSP-----VLFSGTVRfnidpFSEHNDADLWEALERAHIKDVidRNPFGLDAEVSEGGE---NF 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGhvVDVLeLVRTVAREGR--TVVMVQHDLAAAARySDHVIAMKDGEVV 224
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVR--TDSL-IQRTIREEFKscTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
250
....*....|..
gi 2543669097 225 GEGAPRDTVDAE 236
Cdd:PLN03232 1449 EYDSPQELLSRD 1460
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-222 |
1.85e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRpSRGTVLADGAdVWKSGQRQAAHRIAL- 87
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-VEFFNQNIYERRVNLn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 ---------LPQSPRAPEAV--TVA-GLVRYGRHPHQGLlrqwsradERAVREALEATSTTELAGERLDR----LSGGQR 151
Cdd:PRK14258 85 rlrrqvsmvHPKPNLFPMSVydNVAyGVKIVGWRPKLEI--------DDIVESALKDADLWDEIKHKIHKsaldLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 152 QRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVA-REGRTVVMVQHDLAAAARYSDHVIAMKDGE 222
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-211 |
2.09e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.13 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 20 PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRG-TVLADGAdvwksgqrqaahRIALLPQSPRAPEAV 98
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGI------------KVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TVAGLVRYGRHPHQGLLRQWSR-----ADERA-----------VREALEAT------STTELAGERL---------DRLS 147
Cdd:TIGR03719 84 TVRENVEEGVAEIKDALDRFNEisakyAEPDAdfdklaaeqaeLQEIIDAAdawdldSQLEIAMDALrcppwdadvTKLS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 148 GGQRQRCWLAMVLAQQTPVVLLDEPTSALDlGHVVDVLElvRTVAREGRTVVMVQHDlaaaaRY 211
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPGTVVAVTHD-----RY 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-261 |
2.44e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYPGRAVVRdVGFSAPAGTVTSVVGPNGCGKS-TLLRALARLHRPsrGTVLAD-----GADVWKSGQRQ----AAHRIAL 87
Cdd:PRK11022 17 SAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEklefnGQDLQRISEKErrnlVGAEVAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 88 LPQSPRAP--EAVTVAGLVRYGRHPHQGLLRQWSRadERAVrEALEATSTTELAgERLD----RLSGGQRQRCWLAMVLA 161
Cdd:PRK11022 94 IFQDPMTSlnPCYTVGFQIMEAIKVHQGGNKKTRR--QRAI-DLLNQVGIPDPA-SRLDvyphQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVAR-EGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG-------APRDTV 233
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGkahdifrAPRHPY 249
|
250 260
....*....|....*....|....*...
gi 2543669097 234 DAELVRSLYGVEADilRAPVDGSPVVVP 261
Cdd:PRK11022 250 TQALLRALPEFAQD--KARLASLPGVVP 275
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-234 |
2.83e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 32 APAGTVTSVVGPNGCGKSTLLRALARLHRPS---RGTVLADGADVWKSGQRQaahRIALLPQ------SPRAPEAVTVAG 102
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRA---ISAYVQQddlfipTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 103 LVRYGRHPHQGLLRQwsraderAVREALEATSTTELA------GERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:TIGR00955 125 HLRMPRRVTKKEKRE-------RVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 177 D---LGHVVDVLelvRTVAREGRTVVMVQHDLAAAA-RYSDHVIAMKDGEVVGEGAPRDTVD 234
Cdd:TIGR00955 198 DsfmAYSVVQVL---KGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
40-258 |
3.56e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 40 VVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPrapeaVTVAGLVR-----YGRHPHQGL 114
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAP-----VLFSGTVRfnldpFNEHNDADL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 115 LRQWSRADERAV--REALEATSTTELAGErldRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGhvVDVLeLVRTVA 192
Cdd:PLN03130 1345 WESLERAHLKDVirRNSLGLDAEVSEAGE---NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR--TDAL-IQKTIR 1418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 193 REGRTVVMvqhdLAAAARY-----SDHVIAMKDGEVVGEGAPRDTVDAE------LVRSLYGVEADILRAPVDGSPV 258
Cdd:PLN03130 1419 EEFKSCTM----LIIAHRLntiidCDRILVLDAGRVVEFDTPENLLSNEgsafskMVQSTGAANAQYLRSLVFGGDE 1491
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-209 |
8.05e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHRIAL-L 88
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEYHQDLLyL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRAPEAVTVAGLVRYgrhphqgLLRQWSRADERAVREALEATStteLAGeRLD----RLSGGQRQRCWLAMVLAQQT 164
Cdd:PRK13538 80 GHQPGIKTELTALENLRF-------YQRLHGPGDDEALWEALAQVG---LAG-FEDvpvrQLSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2543669097 165 PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH-DLAAAA 209
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHqDLPVAS 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-229 |
8.79e-15 |
|
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: 74.66 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKS--GQRQAahrIALLPQSPRAPEAV 98
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldAVRQS---LGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TVAGLVRYGRhphQGLLRQWSRAdERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDL 178
Cdd:TIGR01257 1019 TVAEHILFYA---QLKGRSWEEA-QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 179 GHVVDVLELVRTVaREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:TIGR01257 1095 YSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-226 |
9.24e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAA---HRIALLPQSPRAPEA 97
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 VTVaglvrYGRHPHQGLLRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSAL 176
Cdd:PRK10908 94 RTV-----YDNVAIPLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2543669097 177 DLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-215 |
1.37e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 20 PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRG-TVLADGAdvwksgqrqaahRIALLPQSPRAPEAV 98
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGI------------KVGYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 TVAGLVRYGRHPHQGLLRQWSR---------------ADERA-VREALEAT------STTELAGERL---------DRLS 147
Cdd:PRK11819 86 TVRENVEEGVAEVKAALDRFNEiyaayaepdadfdalAAEQGeLQEIIDAAdawdldSQLEIAMDALrcppwdakvTKLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 148 GGQRQRCWLAMVLAQQTPVVLLDEPTSALDlGHVVDVLElvRTVAREGRTVVMVQHDlaaaaRYS-DHV 215
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--QFLHDYPGTVVAVTHD-----RYFlDNV 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
35-242 |
2.22e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV--WKSGQ--RQAahrIALLPQSPRAPEAVTVAGLVRYGrhp 110
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdWQTAKimREA---VAIVPEGRRVFSRMTVEENLAMG--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 111 hqGLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRT 190
Cdd:PRK11614 105 --GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 191 VAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSLY 242
Cdd:PRK11614 183 LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-233 |
2.53e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA-----------VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGA--DVWKS 76
Cdd:PRK10261 314 LQVRNLVTRFPLRSgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSP 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 77 GQRQAAHR-IALLPQSPRAP--EAVTVAGLVRYGRHPHqGLLRqwSRADERAVREALEATS-TTELAGERLDRLSGGQRQ 152
Cdd:PRK10261 394 GKLQALRRdIQFIFQDPYASldPRQTVGDSIMEPLRVH-GLLP--GKAAAARVAWLLERVGlLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 153 RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVgEGAPRD 231
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV-EIGPRR 549
|
..
gi 2543669097 232 TV 233
Cdd:PRK10261 550 AV 551
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-238 |
2.92e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 3 NMSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQaA 82
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HR--IALLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSR-ADERAVREALEAT-STTELAGERLDRLSGGqrqrcwlam 158
Cdd:PRK15439 84 HQlgIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQlLAALGCQLDLDSSaGSLEVADRQIVEILRG--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 159 vLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELV 238
Cdd:PRK15439 155 -LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-224 |
3.37e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKsgQRQA-AHRIAL-----------LP--Q 90
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK--RRKEfARRIGVvfgqrsqlwwdLPaiD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 91 SPRapeavtvaglvrygrhphqgLLRQWSRADERAVREALEatsttELAgERLD----------RLSGGQRQRCWLAMVL 160
Cdd:COG4586 116 SFR--------------------LLKAIYRIPDAEYKKRLD-----ELV-ELLDlgelldtpvrQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 161 AQQTPVVLLDEPTSALDlghVV---DVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:COG4586 170 LHRPKILFLDEPTIGLD---VVskeAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-227 |
8.24e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGY-PGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALL 88
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPrAPEAVTVAGLVRYGRHphqgllrqwsrADERAVREALEATSTTELA-----------GERLDRLSGGQRQRCWLA 157
Cdd:PRK10790 421 QQDP-VVLADTFLANVTLGRD-----------ISEEQVWQALETVQLAELArslpdglytplGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 158 MVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVaREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEG 227
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-231 |
1.25e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 8 SGLEVRGLHVGYPGRA-VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwksGQRQAAHR-I 85
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPADRdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSprapeavtvaglvrYGRHPHQ--------GL-LRQWSRAdERAVREAlEATSTTELaGERLDR----LSGGQRQ 152
Cdd:PRK11650 79 AMVFQN--------------YALYPHMsvrenmayGLkIRGMPKA-EIEERVA-EAARILEL-EPLLDRkpreLSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 153 RcwLAM--VLAQQTPVVLLDEPTSALDLGHVVDV-LELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:PRK11650 142 R--VAMgrAIVREPAVFLFDEPLSNLDAKLRVQMrLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
..
gi 2543669097 230 RD 231
Cdd:PRK11650 220 VE 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-229 |
1.27e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV-LADgadvWKSGQRQAAHRIALLPQSPRAPEAVTVAG 102
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqVGD----IYIGDKKNNHELITNPYSKKIKNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 103 LVRY-GRHPHQGLLRQWSRAD------------ERAVREALEATSTTELAGERLDR----LSGGQRQRCWLAMVLAQQTP 165
Cdd:PRK13631 117 RVSMvFQFPEYQLFKDTIEKDimfgpvalgvkkSEAKKLAKFYLNKMGLDDSYLERspfgLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 166 VVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-177 |
1.60e-13 |
|
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: 70.71 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 7 PSG--LEVRGLHVGYP--GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRpSRGTVLADGADvWKSGQRQAA 82
Cdd:TIGR01271 1213 PSGgqMDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS-WNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HR-IALLPQsprapEAVTVAGLVRYGRHPHQgllrQWSRADERAVREALEATSTTELAGERLD--------RLSGGQRQR 153
Cdd:TIGR01271 1291 RKaFGVIPQ-----KVFIFSGTFRKNLDPYE----QWSDEEIWKVAEEVGLKSVIEQFPDKLDfvlvdggyVLSNGHKQL 1361
|
170 180
....*....|....*....|....
gi 2543669097 154 CWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-224 |
2.15e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSgLEVRGLHVGYPG----RAVVRDVGFSAPAGTVTSVVGPNGCGKS-TLLRALARLHRPS----RGTVLADGADVW 74
Cdd:PRK15134 1 MTQPL-LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 75 KSGQRQAAH----RIALLPQSPRAP---------EAVTVAGLvrygrhpHQGLLRQWSRADeraVREALEATSTTELAGE 141
Cdd:PRK15134 80 HASEQTLRGvrgnKIAMIFQEPMVSlnplhtlekQLYEVLSL-------HRGMRREAARGE---ILNCLDRVGIRQAAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 142 RLD---RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIA 217
Cdd:PRK15134 150 LTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAV 229
|
....*..
gi 2543669097 218 MKDGEVV 224
Cdd:PRK15134 230 MQNGRCV 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-225 |
2.29e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARL--HRPSRGTVLADGADVWKSGQRQAAHR-IA 86
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAgIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAPEAVTVAGLVRYGRHPHQGLLRQWSRADERAvREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVG 225
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-243 |
2.40e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQR--QAA----- 82
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssQEAgigii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 83 HR-IALLPQsprapeaVTVAGLVRYGRHPHQGLLR-QWSRADERAvrEALEAT-----STTELAGErldrLSGGQRQRCW 155
Cdd:PRK10762 85 HQeLNLIPQ-------LTIAENIFLGREFVNRFGRiDWKKMYAEA--DKLLARlnlrfSSDKLVGE----LSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 156 LAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDA 235
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED 231
|
....*...
gi 2543669097 236 ELVRSLYG 243
Cdd:PRK10762 232 SLIEMMVG 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-226 |
3.62e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 26 RDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR-IALLPQSPR-------APEA 97
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPEDRQssglyldAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 VTVAGLVrygrHPHQGLLRQwsRADERAVREALEATSTTELAGER--LDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSA 175
Cdd:PRK15439 360 WNVCALT----HNRRGFWIK--PARENAVLERYRRALNIKFNHAEqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 176 LDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-245 |
4.35e-13 |
|
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: 69.08 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARL--HRPSRGTVLADGADVWKSGQRQAAHR-IA 86
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAPEAVTVAGLVRYGRH-PHQGLLRQWS----RADERAVREALEATSTTELAGErldrLSGGQRQRCWLAMVLA 161
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEiTLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGD----YGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 162 QQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAELVRSL 241
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMM 237
|
....
gi 2543669097 242 YGVE 245
Cdd:TIGR02633 238 VGRE 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-229 |
6.32e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 37 VTSVVGPNGCGKSTLLRALARLHRPSRG-TVLAD---GADVWKSGQRQAAHR-IALLPQSPR------APEAVTVAGLVR 105
Cdd:PRK13645 39 VTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaiPANLKKIKEVKRLRKeIGLVFQFPEyqlfqeTIEKDIAFGPVN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 106 YGRHPHQGLlrqwsradeRAVREALEATSTTELAGERLD-RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDV 184
Cdd:PRK13645 119 LGENKQEAY---------KKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2543669097 185 LELVRTVARE-GRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAP 229
Cdd:PRK13645 190 INLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-231 |
6.76e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 11 EVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQA-AHRIALLP 89
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QsprapeavtvaGLVR--------------YGRhphqgLLRQwsRADERAVR--EALEATSTTELAgerlDR----LSGG 149
Cdd:NF033858 83 Q-----------GLGKnlyptlsvfenldfFGR-----LFGQ--DAAERRRRidELLRATGLAPFA----DRpagkLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 150 QRQRCWLAMVLAQQTPVVLLDEPTSAldlghvVDVL------ELVRTV--AREGRTVVMVQHDLAAAARYsDHVIAMKDG 221
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTG------VDPLsrrqfwELIDRIraERPGMSVLVATAYMEEAERF-DWLVAMDAG 213
|
250
....*....|
gi 2543669097 222 EVVGEGAPRD 231
Cdd:NF033858 214 RVLATGTPAE 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-224 |
7.63e-13 |
|
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: 65.75 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALArLHRPSR----GTVLADGADVwKSGQRQAAHRIALLPQSpr 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA-NRTEGNvsveGDIHYNGIPY-KEFAEKYPGEIIYVSEE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 94 apeavtvaglvrygrHPHQGLLrqwsraderAVREALEATstTELAGERLDR-LSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:cd03233 92 ---------------DVHFPTL---------TVRETLDFA--LRCKGNEFVRgISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 173 TSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYS--DHVIAMKDGEVV 224
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQI 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-177 |
7.98e-13 |
|
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: 68.42 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV----------------------- 66
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeigetvklayvdqsrdaldpnkt 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 67 ----LADGADVWKSGQRQAAHRiallpqsprapeavtvAGLVRYGrhphqgllrqWSRADERavrealeatsttelagER 142
Cdd:TIGR03719 403 vweeISGGLDIIKLGKREIPSR----------------AYVGRFN----------FKGSDQQ----------------KK 440
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 143 LDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:TIGR03719 441 VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-247 |
1.02e-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: 68.43 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 30 FSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGAdvwksgqrqaahrIALLPQSPRApEAVTVAGLVRYGRH 109
Cdd:TIGR00957 659 FSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWI-QNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 110 PHQGLLRQWSRADER-AVREALEATSTTELaGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD-------LGHV 181
Cdd:TIGR00957 725 LNEKYYQQVLEACALlPDLEILPSGDRTEI-GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHV 803
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 182 VDVLELVRtvareGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGA-----PRDTVDAELVRSLYGVEAD 247
Cdd:TIGR00957 804 IGPEGVLK-----NKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSyqellQRDGAFAEFLRTYAPDEQQ 868
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-229 |
1.31e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADgadvwksgqrqaaHRIALLPQSPRAPEAVTVAGLVR-----YGRH 109
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDLLRsitddLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 110 PHQGllrqwsraderavrEALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVR 189
Cdd:PRK13409 432 YYKS--------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2543669097 190 TVARE-GRTVVMVQHDLAAAARYSDHVIamkdgevVGEGAP 229
Cdd:PRK13409 498 RIAEErEATALVVDHDIYMIDYISDRLM-------VFEGEP 531
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-219 |
1.88e-12 |
|
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: 63.92 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 23 AVVRDVGFsaPAGTVTSVVGPNGCGKSTLLRALarlhrpsrgtvladgadvwksgqrqaahriallpqsprapeavtvaG 102
Cdd:cd03227 11 FVPNDVTF--GEGSLTIITGPNGSGKSTILDAI----------------------------------------------G 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 103 LVRYGRHPHQGLLRQWSRADERAVREAleatsttELAGERlDRLSGGQRQRCWLAMVLA----QQTPVVLLDEPTSALDL 178
Cdd:cd03227 43 LALGGAQSATRRRSGVKAGCIVAAVSA-------ELIFTR-LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2543669097 179 GHVVDVLELVRTVAREGRTVVMVQHDLAAAARySDHVIAMK 219
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-204 |
2.92e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.81 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYPGRAVV-RDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLadgadvwksgqRQAAHRIALLPQSprape 96
Cdd:PLN03073 517 GYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQH----- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 97 avTVAGLvRYGRHPHQGLLRQWSRADERAVREALEATSTT-ELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSA 175
Cdd:PLN03073 581 --HVDGL-DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170 180 190
....*....|....*....|....*....|
gi 2543669097 176 LDLghvvDVLE-LVRTVAREGRTVVMVQHD 204
Cdd:PLN03073 658 LDL----DAVEaLIQGLVLFQGGVLMVSHD 683
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-233 |
7.96e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA-RLHRPS-RGTVLADGADVWKsgqrQAAHRIALLPQS----PR-- 93
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK----QILKRTGFVTQDdilyPHlt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 94 APEAVTVAGLVRYGRhphqGLLRQ-WSRADERAVRE-ALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDE 171
Cdd:PLN03211 157 VRETLVFCSLLRLPK----SLTKQeKILVAESVISElGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 172 PTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAA-RYSDHVIAMKDGEVVGEGAPRDTV 233
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-227 |
1.10e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 8 SGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCgkstllrALARLHRPSRGTVLADGADVWK----SGQRQAAH 83
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA-------A**RGALPAHV*GPDAGRRPWRf*twCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPRAPEAVTVAG---LVRYGRhphqglLRQWSRADERA-VREALEATSTTELAGERLDRLSGGQRQRCWLAMV 159
Cdd:NF000106 85 RTIG*HRPVR*GRRESFSGrenLYMIGR------*LDLSRKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543669097 160 LAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-236 |
1.20e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHR-IALLPQSPRA--------- 94
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITESRRDngffpnfsi 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 95 PEAVTVAGLVRYGRHphQGLLRQWSRADERAVREALEATSTTELAG--ERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEP 172
Cdd:PRK09700 359 AQNMAISRSLKDGGY--KGAMGLFHEVDEQRTAENQRELLALKCHSvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 173 TSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGEGAPRDTVDAE 236
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-247 |
1.25e-11 |
|
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: 64.82 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRAL-----------------------ARLHRPSR--- 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvalcekcGYVERPSKvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 64 ------GTVLADGADVWKSGQ---RQAAHRIALLPQSPRA--PEAVTVAGLVRYgrhphqglLRQWSRADERAVREALEA 132
Cdd:TIGR03269 81 pcpvcgGTLEPEEVDFWNLSDklrRRIRKRIAIMLQRTFAlyGDDTVLDNVLEA--------LEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 133 TSTTELaGERLDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD-----LGHVVdvleLVRTVAREGRTVVMVQH 203
Cdd:TIGR03269 153 IEMVQL-SHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtakLVHNA----LEEAVKASGISMVLTSH 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2543669097 204 DLAAAARYSDHVIAMKDGEVVGEGAPrDTVDAELVRSLYGVEAD 247
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTP-DEVVAVFMEGVSEVEKE 270
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-224 |
2.33e-11 |
|
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: 63.66 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGLEVRGLHVGYPGRAvvRDVGFSA-------PAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGadvwksg 77
Cdd:COG4615 323 ADFQTLELRGVTYRYPGED--GDEGFTLgpidltiRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 78 qrqaahriallpqsprapEAVTVAGLVRYGRH-------PH--QGLLRQWSRADERAVR---EALEATSTTELAGERLD- 144
Cdd:COG4615 394 ------------------QPVTADNREAYRQLfsavfsdFHlfDRLLGLDGEADPARARellERLELDHKVSVEDGRFSt 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 145 -RLSGGQRQRcwLAMVLA--QQTPVVLLDE------P-------TsaldlghvvdvlELVRTVAREGRTVVMVQHDlaaa 208
Cdd:COG4615 456 tDLSQGQRKR--LALLVAllEDRPILVFDEwaadqdPefrrvfyT------------ELLPELKARGKTVIAISHD---- 517
|
250
....*....|....*....
gi 2543669097 209 ARY---SDHVIAMKDGEVV 224
Cdd:COG4615 518 DRYfdlADRVLKMDYGKLV 536
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-221 |
3.04e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.11 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALA-RLHRPSR-GTVLADGADVWKSGQRqaahRIALLPQSPRAPEAVTVaglvrygrhphq 112
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAgRKTAGVItGEILINGRPLDKNFQR----STGYVEQQDVHSPNLTV------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 113 gllrqwsraderavREALEATSTtelagerLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVA 192
Cdd:cd03232 97 --------------REALRFSAL-------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170 180 190
....*....|....*....|....*....|
gi 2543669097 193 REGRTVVMVQHDLAAAA-RYSDHVIAMKDG 221
Cdd:cd03232 156 DSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-224 |
3.51e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADV-WKSGQRQAAHRIALLPQSPRAPEA 97
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 98 VTVAGLVRYGRHPHQGLLRQWSRA--DERAVREALEATSTTElagERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSA 175
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGMFVDQDKMyrDTKAIFDELDIDIDPR---AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2543669097 176 LDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-177 |
7.46e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV----------------------- 66
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkigetvklayvdqsrdaldpnkt 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 67 ----LADGADVWKSGQRQAAHRiallpqsprapeavtvAGLVRYGrhphqgllrqWSRADERavrealeatsttELAGEr 142
Cdd:PRK11819 405 vweeISGGLDIIKVGNREIPSR----------------AYVGRFN----------FKGGDQQ------------KKVGV- 445
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 143 ldrLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:PRK11819 446 ---LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-227 |
7.92e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 19 YPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGA-------DVWKSgqrqaahRIALLP 89
Cdd:PRK10789 323 YPQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqlDSWRS-------RLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 90 QSPRApEAVTVAGLVRYGRhPHQgllrqwSRAD-ERAVREA--------LEATSTTELaGERLDRLSGGQRQRCWLAMVL 160
Cdd:PRK10789 396 QTPFL-FSDTVANNIALGR-PDA------TQQEiEHVARLAsvhddilrLPQGYDTEV-GERGVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543669097 161 AQQTPVVLLDEPTSALDLGHVVDVLELVRTvAREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEG 227
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQ-WGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-237 |
8.73e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.96 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRA---------VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQ 80
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 81 AAHRIALLPQSPRApeavtvaglvryGRHPHQGL-------LRQWSRADERAVREALEATstTELAGERLDR-------L 146
Cdd:PRK15112 85 RSQRIRMIFQDPST------------SLNPRQRIsqildfpLRLNTDLEPEQREKQIIET--LRQVGLLPDHasyyphmL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTV-AREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVG 225
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250
....*....|..
gi 2543669097 226 EGAPRDTVDAEL 237
Cdd:PRK15112 231 RGSTADVLASPL 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-229 |
1.14e-10 |
|
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: 61.72 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADgadvwksgqrqaaHRIALLPQ--SPRAPEAVtvaglvrygrhphQ 112
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQyiSPDYDGTV-------------E 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 113 GLLRQwsraderAVREALEATS-TTELAG----ERL-DR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVV 182
Cdd:COG1245 420 EFLRS-------ANTDDFGSSYyKTEIIKplglEKLlDKnvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2543669097 183 DVLELVRTVARE-GRTVVMVQHDLAAAARYSDHVIamkdgevVGEGAP 229
Cdd:COG1245 493 AVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM-------VFEGEP 533
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-241 |
2.79e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAV-VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwkSGQRQAAHRiALL 88
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYR-KLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQsprapeavtvaglVRYGRHPHQGLL-RQWSRADERAVR---EALEATSTTELAGERLD--RLSGGQRQRCWLAMVLAQ 162
Cdd:PRK10522 400 SA-------------VFTDFHLFDQLLgPEGKPANPALVEkwlERLKMAHKLELEDGRISnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 163 QTPVVLLDEPTSALDlGHVVDV--LELVRTVAREGRTVVMVQHDLAaaarYSDH---VIAMKDG---EVVGEgaPRDTVD 234
Cdd:PRK10522 467 ERDILLLDEWAADQD-PHFRREfyQVLLPLLQEMGKTIFAISHDDH----YFIHadrLLEMRNGqlsELTGE--ERDAAS 539
|
....*..
gi 2543669097 235 AELVRSL 241
Cdd:PRK10522 540 RDAVART 546
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-222 |
3.07e-10 |
|
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: 57.38 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIallpqsprapeavtvaglvrygrhphqgl 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLI----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 115 lrqwsraderavrealeatstteLAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVA-- 192
Cdd:smart00382 53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 2543669097 193 ----REGRTVVMVQHDL-----AAAARYSDHVIAMKDGE 222
Cdd:smart00382 110 llksEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-210 |
3.41e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 33 PAGTVtSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIA----------LLPQSPRAPEAVTVAG 102
Cdd:PRK10584 35 RGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkhvgfvfqsfMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 103 LVRyGRHPHQgllrqwSRADERAVREALEAtsttelaGERLD----RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDL 178
Cdd:PRK10584 114 LLR-GESSRQ------SRNGAKALLEQLGL-------GKRLDhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190
....*....|....*....|....*....|...
gi 2543669097 179 GHVVDVLELVRTVARE-GRTVVMVQHDLAAAAR 210
Cdd:PRK10584 180 QTGDKIADLLFSLNREhGTTLILVTHDLQLAAR 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-208 |
4.57e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 4 MSSPSGLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRqaAH 83
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA-TRGDR--SR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQSPR-APEAVTVAGL----VRYGRHPhqgllrqwsradERAVREALEATSTTELAGERLDRLSGGQRQRCWLAM 158
Cdd:PRK13543 83 FMAYLGHLPGlKADLSTLENLhflcGLHGRRA------------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2543669097 159 VLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAA 208
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-177 |
6.16e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 9 GLEVRGLHvgypgRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHrpsRGTVLADGADVW--KSGQRQA-AHRI 85
Cdd:COG2401 35 GVELRVVE-----RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDVPdnQFGREASlIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 ALLPQSPRAPEAVTVAGLvrygrhphqgllrqwsraderavrealeatSTTELAGERLDRLSGGQRQRCWLAMVLAQQTP 165
Cdd:COG2401 107 GRKGDFKDAVELLNAVGL------------------------------SDAVLWLRRFKELSTGQKFRFRLALLLAERPK 156
|
170
....*....|..
gi 2543669097 166 VVLLDEPTSALD 177
Cdd:COG2401 157 LLVIDEFCSHLD 168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-224 |
7.49e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV-LADGAdvwksgqrqaahRIALL 88
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENA------------NIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 89 PQSPRA--PEAVTVAglvrygrhphqGLLRQWSRA--DERAVREAL-EATSTTELAGERLDRLSGGQRQRCWLAMVLAQQ 163
Cdd:PRK15064 388 AQDHAYdfENDLTLF-----------DWMSQWRQEgdDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 164 TPVVLLDEPTSALDLGHVVDV---LELVrtvarEGrTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLnmaLEKY-----EG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-229 |
8.24e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 58.01 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLL-----RALAR-LHRpsRGTVLADGADVWksgQRQAAHRIALLPQSP--RAPE 96
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARrLHL--KKEQPGNHDRIE---GLEHIDKVIVIDQSPigRTPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 97 A--VTVAGLV--------------RYGRHPHQGLLRQWSRAD--ERAVREALE-------------ATSTTELA----GE 141
Cdd:cd03271 86 SnpATYTGVFdeirelfcevckgkRYNRETLEVRYKGKSIADvlDMTVEEALEffenipkiarklqTLCDVGLGyiklGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 142 RLDRLSGGQRQRCWLAMVLAQQTP---VVLLDEPTSAL---DLGHVVDVLElvRTVAReGRTVVMVQHDLaAAARYSDHV 215
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQ--RLVDK-GNTVVVIEHNL-DVIKCADWI 241
|
250 260
....*....|....*....|
gi 2543669097 216 IAM------KDGEVVGEGAP 229
Cdd:cd03271 242 IDLgpeggdGGGQVVASGTP 261
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-240 |
1.05e-09 |
|
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: 57.61 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSGL-------EVRGLHVGYPG--RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK 75
Cdd:cd03288 8 SSNSGLvglggeiKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 76 SGQRQAAHRIALLPQSPrapeaVTVAGLVRYGRHPHQGLlrqwsrADERaVREALEATS----TTELAG-------ERLD 144
Cdd:cd03288 88 LPLHTLRSRLSIILQDP-----ILFSGSIRFNLDPECKC------TDDR-LWEALEIAQlknmVKSLPGgldavvtEGGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 145 RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGhVVDVLELVRTVAREGRTVVMVQHdLAAAARYSDHVIAMKDGEVV 224
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAH-RVSTILDADLVLVLSRGILV 233
|
250 260
....*....|....*....|..
gi 2543669097 225 GEGAP------RDTVDAELVRS 240
Cdd:cd03288 234 ECDTPenllaqEDGVFASLVRT 255
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-245 |
1.41e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 2 KNMSSPSgLEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARlHrPS----RGTVLADGADVWKSG 77
Cdd:CHL00131 1 MNKNKPI-LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-H-PAykilEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 78 QRQAAHR-IALLPQSPRAPEAVTVAGLVRYG---RHPHQGLlrqwsraderavrEALEATSTTELAGERLDRL------- 146
Cdd:CHL00131 78 PEERAHLgIFLAFQYPIEIPGVSNADFLRLAynsKRKFQGL-------------PELDPLEFLEIINEKLKLVgmdpsfl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 --------SGGQRQRC-WLAMVLAqQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHdlaaaarYS----- 212
Cdd:CHL00131 145 srnvnegfSGGEKKRNeILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-------YQrlldy 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 2543669097 213 ---DHVIAMKDGEVVGEGaprdtvDAELVRSL--YGVE 245
Cdd:CHL00131 217 ikpDYVHVMQNGKIIKTG------DAELAKELekKGYD 248
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-203 |
1.50e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWK---SGQRQ---AAH 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlcTYQKQlcfVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIALLPQsprapeaVTVAGLVRYGRHPHQGLLrqwsraderAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQ 163
Cdd:PRK13540 82 RSGINPY-------LTLRENCLYDIHFSPGAV---------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2543669097 164 TPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH 203
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-204 |
1.54e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 5 SSPSG---LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVladgadvwKSGQR-Q 80
Cdd:PRK11147 312 ASRSGkivFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKlE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 81 AA----HRIALLPQS------PRAPEAVTVAGLVRYGRHPHQGLLRQWSRAderavREALEAtsttelagerldrLSGGQ 150
Cdd:PRK11147 384 VAyfdqHRAELDPEKtvmdnlAEGKQEVMVNGRPRHVLGYLQDFLFHPKRA-----MTPVKA-------------LSGGE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2543669097 151 RQRCWLAMVLAQQTPVVLLDEPTSALDlghvVDVLELVRT-VAREGRTVVMVQHD 204
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEElLDSYQGTVLLVSHD 496
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-223 |
1.84e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 18 GYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV-LADGADVWKSGQrqaaHRIALLpqspRAPE 96
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQ----HQLEFL----RADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 97 AvtvaglvrygrhPHQGLLRQWSRADERAVREAL-----EATSTTELAGerldRLSGGQRQRCWLAMVLAQQTPVVLLDE 171
Cdd:PRK10636 393 S------------PLQHLARLAPQELEQKLRDYLggfgfQGDKVTEETR----RFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 172 PTSALDLGHVVDVLELVrtVAREGRTVVmVQHDLAAAARYSDHVIAMKDGEV 223
Cdd:PRK10636 457 PTNHLDLDMRQALTEAL--IDFEGALVV-VSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-203 |
4.02e-09 |
|
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: 57.07 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 21 GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHrPSRGTVLADGADvwksgqrqaaHRIALLPQSPRapeaVTV 100
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAK----------GKLFYVPQRPY----MTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 101 AGL---VRYGRHPHQGLLRQWSRADERAVREALEATSTTELAG------ERLDRLSGGQRQRCWLAMVLAQQTPVVLLDE 171
Cdd:TIGR00954 529 GTLrdqIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGgwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 2543669097 172 PTSALDlghvVDVLELVRTVARE-GRTVVMVQH 203
Cdd:TIGR00954 609 CTSAVS----VDVEGYMYRLCREfGITLFSVSH 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-207 |
4.79e-09 |
|
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: 56.02 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYP--GRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRpSRGTVLADGADvWKSGQRQAAHR-IA 86
Cdd:cd03289 3 MTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVS-WNSVPLQKWRKaFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAPEAVTVAGLVRYGRHPHQGLlrqWSRADERAVREALEatsttELAGeRLD--------RLSGGQRQRCWLAM 158
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEI---WKVAEEVGLKSVIE-----QFPG-QLDfvlvdggcVLSHGHKQLMCLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2543669097 159 VLAQQTPVVLLDEPTSALDlGHVVDVLELVRTVAREGRTVVMVQHDLAA 207
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFADCTVILSEHRIEA 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-224 |
5.19e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHrPS---RGTVLADGADVWKSGQRQAAHR-- 84
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 85 ------IALLPQsprapeaVTVAGLVRYGRHPHQGLLRQWSRADERAvREALEATSTTELAGERLDRLSGGQRQRCWLAM 158
Cdd:NF040905 81 viihqeLALIPY-------LSIAENIFLGNERAKRGVIDWNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 159 VLAQQTPVVLLDEPTSAL---DLGHvvdVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVV 224
Cdd:NF040905 153 ALSKDVKLLILDEPTAALneeDSAA---LLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-233 |
6.01e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSGQRQAAHRIALLPQSPrapeaVTVAGL 103
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP-----VLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 104 VRYGRHPhqgllrqWSRADERAVREALEATSTTE-LAGER--LD--------RLSGGQRQ-RCWLAMVLAQQTPVVLLDE 171
Cdd:PTZ00243 1400 VRQNVDP-------FLEASSAEVWAALELVGLRErVASESegIDsrvleggsNYSVGQRQlMCMARALLKKGSGFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 172 PTSALDlgHVVD--VLELVRTvAREGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEGAPRDTV 233
Cdd:PTZ00243 1473 ATANID--PALDrqIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELV 1532
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-227 |
7.42e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRA-LARLHRPSRGTVLADGAdvwksgqrqaahrIALLPQSPRAPEAvTVAGLVR 105
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS-------------VAYVPQVSWIFNA-TVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 106 YGRHPHQGllRQWSRADERAVREALEATSTTELA--GERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDlGHVV- 182
Cdd:PLN03232 701 FGSDFESE--RYWRAIDVTALQHDLDLLPGRDLTeiGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD-AHVAh 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2543669097 183 DVLELVRTVAREGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEG 227
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-234 |
1.70e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGA----DV----WKSgqrqaahRIALLPQSPRAp 95
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkDInlkwWRS-------KIGVVSQDPLL- 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 96 EAVTVAGLVRYGRHPHQGL--LRQWSRADERAVREAL------------------EATSTTEL----------------- 138
Cdd:PTZ00265 472 FSNSIKNNIKYSLYSLKDLeaLSNYYNEDGNDSQENKnkrnscrakcagdlndmsNTTDSNELiemrknyqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 139 ---------------------AGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTV-AREGR 196
Cdd:PTZ00265 552 vskkvlihdfvsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENR 631
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2543669097 197 TVVMVQHDLaAAARYSDHVIAMKDGE--------VVGEGAPRDTVD 234
Cdd:PTZ00265 632 ITIIIAHRL-STIRYANTIFVLSNRErgstvdvdIIGEDPTKDNKE 676
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-227 |
2.19e-08 |
|
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: 52.71 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRalarlhrpsrgTVLAdgadvwKSGQRqaahRIALLPQSPRAPEAVTVAGLv 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLY------ASGKA----RLISFLPKFSRNKLIFIDQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 105 rygrhphqgllrqwsraderavrEALEATSTTELA-GERLDRLSGGQRQRCWLAMVLAQQTP--VVLLDEPTSALDLGHV 181
Cdd:cd03238 69 -----------------------QFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2543669097 182 VDVLELVRTVAREGRTVVMVQHDLaAAARYSDHVIAM------KDGEVVGEG 227
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-216 |
7.44e-08 |
|
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: 51.84 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 37 VTSVVGPNGCGKSTLLR----ALARLHRPSRGTVLADgADVWKSGQRQAAHRIALlpqSPRAPEAVTVAGLVRYGRHP-- 110
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHD-PKLIREGEVRAQVKLAF---ENANGKKYTITRSLAILENVif 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 111 -HQGLLRqWSRADERavrealeatsttelagerlDRLSGGQRQ------RCWLAMVLAQQTPVVLLDEPTSALDLGHVVD 183
Cdd:cd03240 100 cHQGESN-WPLLDMR-------------------GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2543669097 184 VL-ELVRTVAREG-RTVVMVQHD--LAAAArysDHVI 216
Cdd:cd03240 160 SLaEIIEERKSQKnFQLIVITHDeeLVDAA---DHIY 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-227 |
8.41e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 22 RAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRA-LARLHRPSRGTVLADGadvwksgqrqaahRIALLPQSPRAPEAvTV 100
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 101 AGLVRYGRhPHQGLlRQWSRADERAVREALE---ATSTTELaGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:PLN03130 696 RDNILFGS-PFDPE-RYERAIDVTALQHDLDllpGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2543669097 178 lGHVV-DVLELVRTVAREGRTVVMVQHDLAAAARYsDHVIAMKDGEVVGEG 227
Cdd:PLN03130 773 -AHVGrQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-231 |
8.84e-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: 53.09 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 143 LDR----LSGGQRQRCWLAMVLAQQTPVVL--LDEPTSALdlgHVVDVLELVRTVAR---EGRTVVMVQHDlAAAARYSD 213
Cdd:TIGR00630 482 LSRaagtLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDNRRLINTLKRlrdLGNTLIVVEHD-EDTIRAAD 557
|
90 100
....*....|....*....|....
gi 2543669097 214 HVIAM------KDGEVVGEGAPRD 231
Cdd:TIGR00630 558 YVIDIgpgageHGGEVVASGTPEE 581
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-227 |
1.52e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRG------TVLADgadvwksgqrqAAHRIALLP---------QS 91
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFD-----------AEKGICLPPekrrigyvfQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 92 PRAPEAVTVAGLVRYGrhphqglLRQWSRAD-ERAVR----EALeatsttelagerLDR----LSGGQRQRCWLAMVLAQ 162
Cdd:PRK11144 85 ARLFPHYKVRGNLRYG-------MAKSMVAQfDKIVAllgiEPL------------LDRypgsLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543669097 163 QTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRT-VVMVQHDLAAAARYSDHVIAMKDGEVVGEG 227
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-203 |
2.75e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 29 GFSAPaGTVTSVVGPNGCGKSTLLRALA-RLHRP--SRGTVLADGADVWKSGQRqaahRIALLPQSPRAPEAVTVAGLVR 105
Cdd:TIGR00956 784 GWVKP-GTLTALMGASGAGKTTLLNVLAeRVTTGviTGGDRLVNGRPLDSSFQR----SIGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 106 YG---RHPHQGLLRQWSRADErAVREALEATSTTE-LAGERLDRLSGGQRQRCWLAMVL-AQQTPVVLLDEPTSALDLGH 180
Cdd:TIGR00956 859 FSaylRQPKSVSKSEKMEYVE-EVIKLLEMESYADaVVGVPGEGLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQT 937
|
170 180
....*....|....*....|...
gi 2543669097 181 VVDVLELVRTVAREGRTVVMVQH 203
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-226 |
3.93e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLhVGyPGravVRDVGFSAPAGTVTSVVGPNGCGKSTLLR----ALARlhrpSRGTVLADGADVwksgqrqaahri 85
Cdd:PRK10762 258 LKVDNL-SG-PG---VNDVSFTLRKGEILGVSGLMGAGRTELMKvlygALPR----TSGYVTLDGHEV------------ 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 86 allpqSPRAPEAVTVAGLV-----RYGrhphQGL--------------LRQWSR-------ADER-AVREALEATST-TE 137
Cdd:PRK10762 317 -----VTRSPQDGLANGIVyisedRKR----DGLvlgmsvkenmsltaLRYFSRaggslkhADEQqAVSDFIRLFNIkTP 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 138 LAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIA 217
Cdd:PRK10762 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILV 467
|
....*....
gi 2543669097 218 MKDGEVVGE 226
Cdd:PRK10762 468 MHEGRISGE 476
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
35-229 |
4.47e-07 |
|
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: 49.11 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGAdvwksgqrqaahRIALLPQSPRapeavtvaglvrygrhphqgl 114
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYID--------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 115 lrqwsraderavrealeatsttelagerldrLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVARE 194
Cdd:cd03222 72 -------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 2543669097 195 G-RTVVMVQHDLAAAARYSDHVIamkdgevVGEGAP 229
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIH-------VFEGEP 149
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-242 |
8.80e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 LSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVG 225
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
90
....*....|....*....
gi 2543669097 226 EGAPRDTVDAELVR--SLY 242
Cdd:PRK10982 472 IVDTKTTTQNEILRlaSLH 490
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-229 |
9.06e-07 |
|
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: 50.01 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 LSGGQRQRCWLAMVLAQQT---PVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLaAAARYSDHVI------ 216
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADYIIdlgpeg 908
|
90
....*....|...
gi 2543669097 217 AMKDGEVVGEGAP 229
Cdd:TIGR00630 909 GDGGGTVVASGTP 921
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-203 |
2.12e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALA--RLHRPSRGTVLADGADVWK-SGQRQAAHRIA 86
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLElSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 87 LLPQSPRAPEAV-------TVAGLVRYGRhpHQGLLRQWSRADerAVREALEATSTTElagERLDR-----LSGGQRQRC 154
Cdd:PRK09580 82 MAFQYPVEIPGVsnqfflqTALNAVRSYR--GQEPLDRFDFQD--LMEEKIALLKMPE---DLLTRsvnvgFSGGEKKRN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2543669097 155 WLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQH 203
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-226 |
3.64e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGL---HVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRAL-ARLH-RPSRGTVLADGADVWKSGQRQA-AH 83
Cdd:NF040905 258 FEVKNWtvyHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfGRSYgRNISGTVFKDGKEVDVSTVSDAiDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 84 RIA-----------LLPQSPRapEAVTVAGLVRYGRHphqGLLrqwSRADERAV----REAL--EATSTTELAGerldRL 146
Cdd:NF040905 338 GLAyvtedrkgyglNLIDDIK--RNITLANLGKVSRR---GVI---DENEEIKVaeeyRKKMniKTPSVFQKVG----NL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 147 SGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLAAAARYSDHVIAMKDGEVVGE 226
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-244 |
4.10e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGYPGRAVVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHR----------------------------- 60
Cdd:PTZ00265 1169 MDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeq 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 61 -------------------------PSRGTVLADGADVWKSGQRQAAHRIALLPQSPRAPEaVTVAGLVRYGRHphQGLL 115
Cdd:PTZ00265 1249 nvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGKE--DATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 116 RQWSRADE-RAVREALEATSTT--ELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGH-------VVDVL 185
Cdd:PTZ00265 1326 EDVKRACKfAAIDEFIESLPNKydTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliektIVDIK 1405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 186 ElvrtvaREGRTVVMVQHDLAAAARySDHVIAMKDGEVVGEGAPRDTVDAELVRSLYGV 244
Cdd:PTZ00265 1406 D------KADKTIITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAHGTHEELLSVQDGV 1457
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-219 |
4.60e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 140 GERLD--RLSGGQRQ------RCWLAMVLAQ------QTPVVLLDEPTSALDLGHVVDVLELVRTVAREG-RTVVMVQHD 204
Cdd:PRK02224 774 GEPLEpeQLSGGERAlfnlslRCAIYRLLAEgiegdaPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHD 853
|
90
....*....|....*..
gi 2543669097 205 --LAAAArysDHVIAMK 219
Cdd:PRK02224 854 deLVGAA---DDLVRVE 867
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-221 |
2.59e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 24 VVRDVGFSAPAGTVTSVVGPNGCGKSTLLRALArlHRPSRGTVlaDGaDVWKSG----QRQAAHRIALLPQSPRAPEAVT 99
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTGGYI--EG-DIRISGfpkkQETFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 100 VAGLVRYG---RHPHQ-GLLRQWSRADEraVREALEATSTTE----LAGerLDRLSGGQRQRCWLAMVLAQQTPVVLLDE 171
Cdd:PLN03140 970 VRESLIYSaflRLPKEvSKEEKMMFVDE--VMELVELDNLKDaivgLPG--VTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 172 PTSALDLGHVVDVLELVRTVAREGRTVVMVQH----DLAAAArysDHVIAMKDG 221
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-231 |
3.59e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 10 LEVRGLHVGY-----PGRAVVRdVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRgTVLAD-----GADVWKSGQR 79
Cdd:PRK15093 4 LDIRNLTIEFktsdgWVKAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNW-RVTADrmrfdDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 80 Q----AAHRIALL---PQSPRAPEAvtvaglvRYGRHPHQGLL------RQWSRADERAvREALEATSTTELAGERlD-- 144
Cdd:PRK15093 82 ErrklVGHNVSMIfqePQSCLDPSE-------RVGRQLMQNIPgwtykgRWWQRFGWRK-RRAIELLHRVGIKDHK-Dam 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 145 -----RLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELV-RTVAREGRTVVMVQHDLAAAARYSDHVIAM 218
Cdd:PRK15093 153 rsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250
....*....|...
gi 2543669097 219 KDGEVVgEGAPRD 231
Cdd:PRK15093 233 YCGQTV-ETAPSK 244
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
142-227 |
3.88e-05 |
|
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: 43.79 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 142 RLDR----LSGGQRQRCWLAMVLAQQTPVVL--LDEPTSALdlgHVVDVLELVRTVAR---EGRTVVMVQHDLaAAARYS 212
Cdd:cd03270 130 TLSRsaptLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HPRDNDRLIETLKRlrdLGNTVLVVEHDE-DTIRAA 205
|
90 100
....*....|....*....|.
gi 2543669097 213 DHVIAM------KDGEVVGEG 227
Cdd:cd03270 206 DHVIDIgpgagvHGGEIVAQG 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
146-231 |
4.29e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 LSGGQRQRCWLAMVLAQ-QTP--VVLLDEPTSAL---DLGHVVDVLElvRTVAReGRTVVMVQHDL---AAAarysDHVI 216
Cdd:COG0178 827 LSGGEAQRVKLASELSKrSTGktLYILDEPTTGLhfhDIRKLLEVLH--RLVDK-GNTVVVIEHNLdviKTA----DWII 899
|
90 100
....*....|....*....|.
gi 2543669097 217 AM------KDGEVVGEGAPRD 231
Cdd:COG0178 900 DLgpeggdGGGEIVAEGTPEE 920
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-218 |
4.51e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 140 GERLDRLSGGQRQRCWLAMVLAQQTP---VVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLaAAARYSDHVI 216
Cdd:PRK00635 804 GRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
..
gi 2543669097 217 AM 218
Cdd:PRK00635 883 EL 884
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-205 |
4.65e-05 |
|
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: 45.00 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 29 GFSAPA----------GTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVWKSgQRQAAHRIALLPQSPRAPEAV 98
Cdd:TIGR01257 1949 GTSSPAvdrlcvgvrpGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-ISDVHQNMGYCPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 99 T-VAGLVRYGRhphqgLLRQWSRADERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:TIGR01257 2028 TgREHLYLYAR-----LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180
....*....|....*....|....*...
gi 2543669097 178 LGHVVDVLELVRTVAREGRTVVMVQHDL 205
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
141-190 |
1.30e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 42.67 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 141 ERLDRLSGGQRQRCWLAMVLA----QQTPVVLLDEPTSALDLGHVVDVLELVRT 190
Cdd:cd03273 162 ESLTELSGGQRSLVALSLILAlllfKPAPMYILDEVDAALDLSHTQNIGRMIKT 215
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-231 |
1.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 138 LAGER-LDRLSGGQRQRCWLAMVLAQQTPVV--LLDEPTSALdlgHVVDVLELVRTVAR---EGRTVVMVQHDlAAAARY 211
Cdd:PRK00635 468 LTPERaLATLSGGEQERTALAKHLGAELIGItyILDEPSIGL---HPQDTHKLINVIKKlrdQGNTVLLVEHD-EQMISL 543
|
90 100
....*....|....*....|....*.
gi 2543669097 212 SDHVI------AMKDGEVVGEGAPRD 231
Cdd:PRK00635 544 ADRIIdigpgaGIFGGEVLFNGSPRE 569
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-204 |
1.70e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 35 GTVTSVVGPNGCGKSTLLRALarlhrpsRGTVLADGADVWKSGQRQAAHRIALLPQSPRAPEAVTVAGLVRYgRHPHQGL 114
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREY-RQLEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 115 LRQWSRADERAVR------EALEATSTTELAG----------ERLDR----LSGGQRQRCWLAMVLAQQTPVVLLDEPTS 174
Cdd:PRK10636 99 HDANERNDGHAIAtihgklDAIDAWTIRSRAAsllhglgfsnEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
170 180 190
....*....|....*....|....*....|
gi 2543669097 175 ALDLGHVVdvlELVRTVAREGRTVVMVQHD 204
Cdd:PRK10636 179 HLDLDAVI---WLEKWLKSYQGTLILISHD 205
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
141-189 |
2.00e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 2.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2543669097 141 ERLDRLSGGQRQRCWLAMVLAQQ----TPVVLLDEPTSALDLGHVVDVLELVR 189
Cdd:pfam02463 1073 KNLDLLSGGEKTLVALALIFAIQkykpAPFYLLDEIDAALDDQNVSRVANLLK 1125
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-177 |
3.32e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 25 VRDVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTVLADGADVwKSGQRQAAHRIALLPQSPRAPEAVTVaglv 104
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIATRRRVGYMSQAFSLYGELTV---- 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 105 rygrhpHQGL-----LRQWSRAD-ERAVREALEATSTTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALD 177
Cdd:NF033858 357 ------RQNLelharLFHLPAAEiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-231 |
4.29e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 140 GERLDRLSGGQRQRCWLA--MVLAQQTPVV-LLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHDLaAAARYSDHVI 216
Cdd:PRK00635 1694 GQNLSSLSLSEKIAIKIAkfLYLPPKHPTLfLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLI 1772
|
90 100
....*....|....*....|.
gi 2543669097 217 AM------KDGEVVGEGAPRD 231
Cdd:PRK00635 1773 EMgpgsgkTGGKILFSGPPKD 1793
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
37-60 |
5.28e-04 |
|
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: 40.84 E-value: 5.28e-04
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
37-66 |
6.85e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 6.85e-04
10 20 30
....*....|....*....|....*....|
gi 2543669097 37 VTSVVGPNGCGKSTLLRALARLHRPSRGTV 66
Cdd:COG4637 23 LTVLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
30-58 |
6.95e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 6.95e-04
10 20
....*....|....*....|....*....
gi 2543669097 30 FSAPAGtVTSVVGPNGCGKSTLLRALARL 58
Cdd:COG3950 21 FDNPPR-LTVLVGENGSGKTTLLEAIALA 48
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-201 |
7.07e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 34 AGTVTSVVGPNGCGKSTLLRALArlhrpsrgtvladGADVWKSGQRQAA-HRIALLpqsprAPEAVtvaglvrygrhphQ 112
Cdd:PRK10938 28 AGDSWAFVGANGSGKSALARALA-------------GELPLLSGERQSQfSHITRL-----SFEQL-------------Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 113 GLLRQ-WSR-------ADE----RAVREA-LEATSTTELAGER---------LDR----LSGGQRQRCWLAMVLAQQTPV 166
Cdd:PRK10938 77 KLVSDeWQRnntdmlsPGEddtgRTTAEIiQDEVKDPARCEQLaqqfgitalLDRrfkyLSTGETRKTLLCQALMSEPDL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2543669097 167 VLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMV 201
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
146-229 |
1.46e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 146 LSGGQRQRCWLAMVLAQ----QTpVVLLDEPTSALdlgHVVDV---LE-LVRTVAReGRTVVMVQHDL----AAaarysD 213
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKrstgKT-LYILDEPTTGL---HFEDIrklLEvLHRLVDK-GNTVVVIEHNLdvikTA-----D 900
|
90 100
....*....|....*....|..
gi 2543669097 214 HVIAM------KDGEVVGEGAP 229
Cdd:PRK00349 901 WIIDLgpeggdGGGEIVATGTP 922
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-216 |
1.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 141 ER-LDRLSGGQRQ------RCWLAMVLAQQTPVVLLDEPTSALDLGHVVDVLELVRTVAREGRTVVMVQHD--LAAAAry 211
Cdd:PRK03918 783 ERpLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDeeLKDAA-- 860
|
....*
gi 2543669097 212 sDHVI 216
Cdd:PRK03918 861 -DYVI 864
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-66 |
1.83e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2543669097 27 DVGFSAPAGTVTSVVGPNGCGKSTLLRALARLHRPSRGTV 66
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
30-55 |
1.91e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 1.91e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
135-203 |
2.47e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543669097 135 TTELAGERLDRLSGGQRQRCWLAMVLAQQTPVVLLDEPTSALDLgHVvdVLELVRTVAREGRTVVMVQH 203
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HA--VLWLETYLLKWPKTFIVVSH 399
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-231 |
3.11e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543669097 143 LDR----LSGGQRQRCWLAmvlaqqTPV------VL--LDEPTSAL---DLGHVVDVLELVRTVareGRTVVMVQHD--- 204
Cdd:COG0178 479 LDRsagtLSGGEAQRIRLA------TQIgsglvgVLyvLDEPSIGLhqrDNDRLIETLKRLRDL---GNTVIVVEHDedt 549
|
90 100 110
....*....|....*....|....*....|....
gi 2543669097 205 -LAAaarysDHVIAM------KDGEVVGEGAPRD 231
Cdd:COG0178 550 iRAA-----DYIIDIgpgageHGGEVVAQGTPEE 578
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
37-55 |
3.49e-03 |
|
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: 37.83 E-value: 3.49e-03
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
37-58 |
4.11e-03 |
|
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: 38.44 E-value: 4.11e-03
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
135-192 |
4.31e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543669097 135 TTELAGE--RLDRLSGGQRQRCWLAMVLAQQ----TPVVLLDEPTSALDLGHVVDVLELVRTVA 192
Cdd:cd03272 146 TNMKQDEqqEMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDAALDAQYRTAVANMIKELS 209
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
32-57 |
6.88e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 37.32 E-value: 6.88e-03
10 20
....*....|....*....|....*.
gi 2543669097 32 APAGTVTSVVGPNGCGKSTLLRALAR 57
Cdd:cd01882 36 EPPPLVVVVVGPPGVGKSTLIRSLIK 61
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-66 |
7.69e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.77 E-value: 7.69e-03
10 20 30
....*....|....*....|....*....|.
gi 2543669097 36 TVTSVVGPNGCGKSTLLRALARLHRPSRGTV 66
Cdd:PRK13541 27 AITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
30-56 |
7.82e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 37.05 E-value: 7.82e-03
10 20
....*....|....*....|....*..
gi 2543669097 30 FSAPagtVTSVVGPNGCGKSTLLRALA 56
Cdd:COG3910 35 FHPP---VTFFVGENGSGKSTLLEAIA 58
|
|
| |
