|
Name |
Accession |
Description |
Interval |
E-value |
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-256 |
1.90e-172 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 475.66 E-value: 1.90e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|....*
gi 492172462 242 IMREPVAGTPMCIVE 256
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-254 |
4.02e-130 |
|
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: 368.60 E-value: 4.02e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|...
gi 492172462 242 IMREPVAGTPMCI 254
Cdd:COG1120 241 VIEDPVTGRPLVL 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-254 |
1.10e-93 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 276.19 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGV 92
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYGRSPHNSlwGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:COG4604 91 TVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 173 SHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQImrEPVAGTP 251
Cdd:COG4604 169 KHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV--EEIDGKR 246
|
...
gi 492172462 252 MCI 254
Cdd:COG4604 247 ICV 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-254 |
1.33e-88 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 263.77 E-value: 1.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQI 242
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
250
....*....|..
gi 492172462 243 MREPVAGTPMCI 254
Cdd:PRK10253 248 IDDPVAGTPLVV 259
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-221 |
6.05e-85 |
|
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: 251.20 E-value: 6.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPq 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 vlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03214 80 -------------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-252 |
3.59e-83 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 249.65 E-value: 3.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYGRSPHnslwGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ------- 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVF 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....*.
gi 492172462 237 DVHVQIMREPVAGTPM 252
Cdd:COG4559 238 GADLRVLAHPEGGCPQ 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
3.73e-82 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 246.54 E-value: 3.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARelackVA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIPEG--VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMqGGRLVTCGAPGDVLTAELVCQVFDV 238
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYGG 237
|
....*..
gi 492172462 239 HVQIMRE 245
Cdd:COG1121 238 PVALLAH 244
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-252 |
1.45e-77 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 235.44 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYGRSPhnslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA---- 159
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 160 --IVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVF 236
Cdd:PRK13548 159 prWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
250
....*....|....*.
gi 492172462 237 DVHVQIMREPVAGTPM 252
Cdd:PRK13548 239 GADVLVQPHPETGAPL 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-255 |
2.54e-76 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 232.37 E-value: 2.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQL 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 178 LLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQIMREPVAGTPMCIV 255
Cdd:PRK10575 186 VLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPVSFV 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-251 |
5.50e-70 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 220.87 E-value: 5.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHV 240
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDART 240
|
250
....*....|.
gi 492172462 241 QIMREPVAGTP 251
Cdd:PRK09536 241 AVGTDPATGAP 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-212 |
1.27e-68 |
|
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: 210.85 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARelackVAFLPQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 VLPIPEG--VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVM 212
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-230 |
4.88e-60 |
|
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: 189.47 E-value: 4.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQ------VLPIpegvnVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1122 81 FQnpddqlFAPT-----VEEDVAFG--PENL---GLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-212 |
4.61e-57 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 180.89 E-value: 4.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLsldgkgysqlsARELACKVAFLPQVLPIPEG 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 --VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQAcRYADHLAVM 212
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-231 |
1.54e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.03 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAcKVAFLP 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:COG1131 80 QEPALYPDLTVRENLRF--------FARLYGLPRKEarerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAEL 231
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-227 |
5.84e-55 |
|
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: 176.97 E-value: 5.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAcKVAFLP 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYgrspHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:COG4555 81 DERGLYDRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-216 |
4.60e-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: 173.81 E-value: 4.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlpiPE--- 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN---PDdqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 -GVNVRQLVAYGrsPHNSLwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03225 89 fGPTVEEEVAFG--LENLG---LPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492172462 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-255 |
6.71e-54 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 175.40 E-value: 6.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ--------SGSLSLDGKGYSQLSARE 74
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 75 LACKVAFLPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 155 AQ---------DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRLVTCGAPG 224
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|.
gi 492172462 225 DVLTAELVCQVFDVHVQIMREPvAGTPMCIV 255
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAG-DGVPPVIV 270
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-256 |
2.45e-53 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 173.10 E-value: 2.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRSPHNSlwgrlSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ-------DAAIVLLDEPTTYLD 171
Cdd:COG4138 91 ALHQPAGAS-----SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQIMRepVAGTP 251
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE--VEGHR 243
|
....*
gi 492172462 252 MCIVE 256
Cdd:COG4138 244 WLIPT 248
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
4.09e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 172.55 E-value: 4.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA---C 77
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQVLPIPEGVNVRQLVAYGRSPHNSLW----GRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 154 LAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG3638 161 LVQEPKLILADEPVASLDpkTARQV--MDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238
|
.
gi 492172462 231 L 231
Cdd:COG3638 239 L 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
4.27e-50 |
|
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: 171.62 E-value: 4.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGY-----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAc 77
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 kvAFLPQVLPI---PEG-----VNVRQLVAYGRSPHnslwGRLSGADQHS-VDQALQRMEL-ATLAERPLSDLSGGQRQR 147
Cdd:COG1123 339 --ELRRRVQMVfqdPYSslnprMTVGDIIAEPLRLH----GLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
...
gi 492172462 227 LTA 229
Cdd:COG1123 493 FAN 495
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
1.26e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 154.60 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVAFLP 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYGrsphnsLWGRLSGADQH--SVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFG------LKLRGVPKAEIraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
1.32e-46 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 154.97 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC- 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 --KVAFLPQvlpipegvnvrqlvaygrSPHNSLWGRLSGADQ----------HSVDQALQRMELATLAERPLSD------ 139
Cdd:cd03257 81 rkEIQMVFQ------------------DPMSSLNPRMTIGEQiaeplrihgkLSKKEARKEAVLLLLVGVGLPEevlnry 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 ---LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:cd03257 143 pheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
....*.
gi 492172462 216 RLVTCG 221
Cdd:cd03257 223 KIVEEG 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-217 |
2.62e-46 |
|
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: 152.55 E-value: 2.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAFLP 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03230 80 EEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
2.81e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.91 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MS-ILKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSARE 74
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 75 LACKVAFLPQVlpiPE----GVNVRQLVAYGrsphnSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAW 149
Cdd:COG1123 81 RGRRIGMVFQD---PMtqlnPVTVGDQIAEA-----LENLGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 492172462 229 A 229
Cdd:COG1123 233 A 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-216 |
4.80e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 148.93 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQ 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 vlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-232 |
7.93e-45 |
|
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: 150.67 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA-CKVA-- 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 F-LPQVLP---IPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:cd03219 81 FqIPRLFPeltVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-236 |
1.27e-44 |
|
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: 150.41 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGA-TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KV 79
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVLPIPEGVNVRQLVAYGR----SPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 156 QDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDvLTAELV 232
Cdd:cd03256 161 QQPKLILADEPVASLDpaSSRQV--MDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVL 237
|
....
gi 492172462 233 CQVF 236
Cdd:cd03256 238 DEIY 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-218 |
1.55e-43 |
|
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: 146.63 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 6 AQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELACKVAFLPQ 84
Cdd:cd03226 2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 vlpipegvNV-RQLvaYGRSPHNSLwgRLS----GADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:cd03226 79 --------DVdYQL--FTDSVREEL--LLGlkelDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-218 |
3.75e-43 |
|
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: 146.87 E-value: 3.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGA----TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVlpiPEG-VNVRQLVayGRSPHNSLWGRLSGADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:COG1124 82 QMVFQD---PYAsLHPRHTV--DRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
5.53e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.34 E-value: 5.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGvNVRQLVAYGRSPHNSLWgrlsgaDQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKF------DRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
8.87e-43 |
|
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: 144.54 E-value: 8.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGySQLSARELACKVAFLP 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAygrsphnsLWGRLSG--ADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:COG4133 82 HADGLKPELTVRENLR--------FWAALYGlrADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-227 |
2.43e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 147.60 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG-YSQLSARELacKV 79
Cdd:COG1118 1 MSI-EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRER--RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQvlpipegvN--------VRQLVAYG---RSPhnslwgrlSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQR 147
Cdd:COG1118 78 GFVFQ--------HyalfphmtVAENIAFGlrvRPP--------SKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
.
gi 492172462 227 L 227
Cdd:COG1118 222 Y 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-255 |
3.67e-42 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 144.31 E-value: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLVAYG 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPHNSLwgrlsGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ-------DAAIVLLDEPTTYLDISH 174
Cdd:PRK03695 94 QPDKTRT-----EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQimREPVAGTPMCI 254
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR--RLDVEGHPMLI 246
|
.
gi 492172462 255 V 255
Cdd:PRK03695 247 S 247
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
3.60e-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: 144.47 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelacKVA 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR------------DVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPqvlpiPE--GVN-------------VRQLVAYG---RsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLS 141
Cdd:COG3842 71 GLP-----PEkrNVGmvfqdyalfphltVAENVAFGlrmR--------GVPKAEIRArVAELLELVGLEGLADRYPHQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 142 GGQRQRAWLAMILAQDAAIVLLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRI 214
|
....*....
gi 492172462 218 VTCGAPGDV 226
Cdd:COG3842 215 EQVGTPEEI 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-232 |
4.41e-41 |
|
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: 141.71 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA-CKV 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 A--FlpQVLPIPEGVNVRQ--LVAYGRSPHNSLWGRLSG---------ADQHSVDQALQRMELATLAERPLSDLSGGQRQ 146
Cdd:COG0411 82 ArtF--QNPRLFPELTVLEnvLVAAHARLGRGLLAALLRlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGD 225
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*..
gi 492172462 226 VLTAELV 232
Cdd:COG0411 240 VRADPRV 246
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
5.64e-41 |
|
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: 140.78 E-value: 5.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARIL-----TPQSGSLSLDGKGYSQLSAR--ELA 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 CKVAFLPQvLPIPEGVNVRQLVAYGRSPHNSLWGRLSGAdqhSVDQALQRMELATLAERPLS--DLSGGQRQRAWLAMIL 154
Cdd:cd03260 81 RRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGIKLKEELDE---RVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-238 |
6.86e-41 |
|
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: 140.37 E-value: 6.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 24 FSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlSARELACKVAFLPQV------LPIpegvNVRQL 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefawdFPI----SVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR03771 72 VMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 178 LLDLMRELSAEGKTVITVLHDINQACRYADHLaVMQGGRLVTCGAPGDVLTAELVCQVFDV 238
Cdd:TIGR03771 152 LTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-245 |
1.14e-40 |
|
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: 140.60 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSG-SLSLDGKGYSQLSARELACKV 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVL--PIPEGVNVRQLVAYGRspHNS--LWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1119 81 GLVSPALqlRFPRDETVLDVVLSGF--FDSigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG-KTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSE 238
|
250
....*....|.
gi 492172462 235 VFDVHVQIMRE 245
Cdd:COG1119 239 AFGLPVEVERR 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-230 |
2.33e-40 |
|
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: 139.34 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA---CKV 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQvlpipEG-----VNVRQLVAYgrsP---HnslwGRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWL 150
Cdd:COG1127 85 GMLFQ-----GGalfdsLTVFENVAF---PlreH----TDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 151 AMILAQDAAIVLLDEPTTYLD-ISHQVeLLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
..
gi 492172462 229 AE 230
Cdd:COG1127 232 SD 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-228 |
5.64e-40 |
|
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: 138.59 E-value: 5.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLpipegvn 93
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQI------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 vrqlvayGRSPHNSLWG------RLSGADQHSVDQ------ALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03295 85 -------GLFPHMTVEEnialvpKLLKWPKEKIREradellALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 162 LLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:cd03295 158 LMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-230 |
1.18e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.19 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 23 SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL--SARelacKVAFLPQvlpipEG-----VNVR 95
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAER----PVSMLFQ-----ENnlfphLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYGRSPHnslwGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:COG3840 90 QNIGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 176 VELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG3840 166 QEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-227 |
1.44e-39 |
|
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: 144.13 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGvNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAER-------PLSD----LSGGQRQRAWLA 151
Cdd:COG4988 417 PQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQAcRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELL 559
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
1.32e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHL----DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA- 76
Cdd:COG1136 3 PLLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 ---CKVAFLPQ---VLPipeGVNVRQLVAYgrsPHnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWL 150
Cdd:COG1136 83 lrrRHIGFVFQffnLLP---ELTALENVAL---PL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRLV 218
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-223 |
2.37e-38 |
|
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: 134.35 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL---ACK 78
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 79 VAFLPQVLPIPEGVNVRQLVAYGR----SPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 155 AQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDpkTSKQV--MDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-217 |
3.32e-38 |
|
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: 133.00 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGA----TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC-- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 --KVAFLPQ---VLPipeGVNVRQLVAYGrsphnSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:cd03255 81 rrHIGFVFQsfnLLP---DLTALENVELP-----LLLAGVPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRL 217
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-228 |
6.71e-38 |
|
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: 133.01 E-value: 6.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 7 QHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL---ACKVAFLP 83
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYGRSPHnslwGRLSgaDQHSVDQALQRMELATLAE----RPlSDLSGGQRQRAWLAMILAQDAA 159
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLREH----TRLS--EEEIREIVLEKLEAVGLRGaedlYP-AELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 160 IVLLDEPTTYLD-ISHQVeLLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:cd03261 157 LLLYDEPTAGLDpIASGV-IDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
5.00e-37 |
|
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: 130.09 E-value: 5.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYsQLSARElacKVAFLP 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARN---RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVR-QLVAYGRsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03269 77 EERGLYPKMKVIdQLVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-202 |
1.40e-36 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 128.31 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKVAFlpqVLPIPE- 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGL---VFQDPDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 ---GVNVRQLVAYGrsPHNSlwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:TIGR01166 80 qlfAADVDQDVAFG--PLNL---GLSEAEVERrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDINQA 202
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-216 |
1.55e-36 |
|
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: 127.50 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGAT--RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQvlpipegvnvrqlvaygrSPHnslwgRLSGadqhsvdqalqrmelaTLAErplSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03228 81 VPQ------------------DPF-----LFSG----------------TIRE---NILSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINQAcRYADHLAVMQGGR 216
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-216 |
3.20e-36 |
|
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: 126.92 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA--RELACKVAF 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLPIPEGVNVRQLVAYGrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
3.30e-36 |
|
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: 127.69 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgYSQLSAR-ELACKVAFL 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPqKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGVNVRQLVAYgrsphNSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLDY-----IAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
4.82e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARelacKVAFL 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 pqvlpiPE--G----VNVR-QLVAYGRsphnsLWGrLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:COG4152 77 ------PEerGlypkMKVGeQLVYLAR-----LKG-LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 155 AQDAAIVLLDEPTTYLD-IShqVELL-DLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:COG4152 145 LHDPELLILDEPFSGLDpVN--VELLkDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
4.96e-36 |
|
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: 125.45 E-value: 4.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 99 AYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-232 |
8.46e-36 |
|
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: 127.41 E-value: 8.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-V 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQ---VLPipeGVNVR---QLVAYGRSphnslwgrlsgaDQHSVDQALQRM-----ELATLAERPLSDLSGGQRQRA 148
Cdd:COG0410 81 GYVPEgrrIFP---SLTVEenlLLGAYARR------------DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 149 WLAMILAQDAAIVLLDEPTtyLDISHQV--ELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
....*.
gi 492172462 227 LTAELV 232
Cdd:COG0410 224 LADPEV 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
8.51e-36 |
|
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: 127.17 E-value: 8.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-VAFL 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGVNVR---QLVAYGRSPhnslwgrlsGADQHSVDQALQRM-ELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03224 81 PEGRRIFPELTVEenlLLGAYARRR---------AKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-218 |
1.91e-35 |
|
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: 126.05 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYG----ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlSARELACKV 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQ---VLPipeGVNVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:cd03293 76 GYVFQqdaLLP---WLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 157 DAAIVLLDEPTTYLD----ISHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRLV 218
Cdd:cd03293 149 DPDVLLLDEPFSALDaltrEQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-226 |
2.48e-35 |
|
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: 126.30 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVA 80
Cdd:cd03296 1 MSI-EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIPEGVNVRQLVAYG-RSPHNSlwGRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGlRVKPRS--ERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-236 |
3.76e-35 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 126.92 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackVAFLPQVLPIPEG--VNVRQ 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 97 LVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQV 176
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 177 ELLDLMRELSAEGKTVITVLHDINQACRYADHlAVMQGGRLVTCGAPGDVLTAELVCQVF 236
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGPTETTFTAENLELAF 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-221 |
4.50e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.30 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKG-YS-QLSARE 74
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDiYDpDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 75 LACKVAFLPQVL-PIPEGV--NvrqlVAYG-RsphnsLWGRLSGAD-QHSVDQALQRMEL-----ATLAERPLSdLSGGQ 144
Cdd:COG1117 90 LRRRVGMVFQKPnPFPKSIydN----VAYGlR-----LHGIKSKSElDEIVEESLRKAALwdevkDRLKKSALG-LSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 145 RQRAWLAMILAQDAAIVLLDEPTTYLD-IS-HQVEllDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-221 |
4.80e-35 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 124.91 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFspPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL--SARelacKVAFLPQVLPIPE 90
Cdd:cd03298 10 YGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppADR----PVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GVNVRQLVAYGRSPhnSLwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03298 84 HLTVEQNVGLGLSP--GL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492172462 171 DISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03298 160 DPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-228 |
6.83e-35 |
|
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: 126.03 E-value: 6.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---GYSQLSARELACKVAFLPQvlpIPEgvnvRQL 97
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLKDLRKKVGLVFQ---FPE----HQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 --------VAYGrsPHNslWGrLSGADQHS-VDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR04521 96 feetvykdIAFG--PKN--LG-LSEEEAEErVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 168 TYLDISHQVELLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-227 |
7.39e-35 |
|
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: 131.43 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGY-GATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:COG4987 334 LELEDVSFRYpGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLPIPEGvNVRQ--LVAYGRSPHNSLWgrlsgadqhsvdQALQRMELATLAERpLSD------------LSGGQRQR 147
Cdd:COG4987 414 VPQRPHLFDT-TLREnlRLARPDATDEELW------------AALERVGLGDWLAA-LPDgldtwlgeggrrLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDInQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
8.58e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 8.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFlpqVLPIPE----GVNVRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13635 84 GM---VFQNPDnqfvGATVQDDVAFGLEnigvPREEMVER--------VDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-228 |
8.89e-35 |
|
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: 125.83 E-value: 8.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC-----------KVAFL 82
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVlpipegvNVRQLVAYGRSphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03294 115 PHR-------TVLENVAFGLE----VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:cd03294 184 MDEAFSALDplirREMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-239 |
1.44e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.07 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAF 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLPIPEGVNVRQ-LVAYGRsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK13537 85 VPQFDNLDPDFTVREnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVH 239
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIY 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-232 |
1.83e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.37 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAF 81
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQ-VLPIPEgVNVRQLVAYGRSPHNslWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQ-----RAwlamiL 154
Cdd:COG1129 84 IHQeLNLVPN-LSVAENIFLGREPRR--GGLIDWRAMRRrARELLARLGLDIDPDTPVGDLSVAQQQlveiaRA-----L 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 155 AQDAAIVLLDEPTTYLDiSHQVE-LLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:COG1129 156 SRDARVLILDEPTASLT-EREVErLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELV 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-234 |
2.38e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.85 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFlpqVLPIPE----G 91
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL---VFQDPDdqvfS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 VNVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:PRK13647 95 STVWDDVAFG--PVNM---GLDKDEvERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 171 DISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-221 |
2.74e-34 |
|
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: 123.25 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYgrsphnslWGRLSGADQHSVDQAL----QRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03266 100 EY--------FAGLYGLKGDELTARLeelaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03266 172 TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-226 |
3.53e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.35 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVA 80
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIPEGVNVRQLVAYGRS--PHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTvlPRRE---RPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-223 |
5.09e-34 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 122.23 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgkGYSQLSARELACK-VAFLPQVLPIPE 90
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--GYSIRTDRKAARQsLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GVNVRQLVAYgrspHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03263 89 ELTVREHLRF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492172462 171 DISHQVELLDLMRELSaEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:cd03263 165 DPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-229 |
7.12e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 122.41 E-value: 7.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKVA 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdlTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQ---------VLpipEGVNVRQLVAYGRSPHNslwgrlsgADQHSVDQaLQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:COG1126 81 MVFQqfnlfphltVL---ENVTLAPIKVKKMSKAE--------AEERAMEL-LERVGLADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLD---IShqvELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
.
gi 492172462 229 A 229
Cdd:COG1126 226 N 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
4.20e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.26 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVA 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQ---VLPipeGVNVRQLVAYG---RsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG3839 79 MVFQsyaLYP---HMTVYENIAFPlklR--------KVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 154 LAQDAAIVLLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-212 |
4.31e-33 |
|
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: 125.86 E-value: 4.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvN 93
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATL-AERPL----------SDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:TIGR02857 412 IAENIRLAR----------PDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQACRyADHLAVM 212
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
6.36e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.58 E-value: 6.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARela 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 ckVAFLPQ---VLPipegvNVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG1116 82 --RGVVFQepaLLPw---lTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 154 LAQDAAIVLLDEPTTYLD----ISHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRLV 218
Cdd:COG1116 153 LANDPEVLLMDEPFGALDaltrERLQDELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
2.28e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.80 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKV 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQ----VLPIPegvNVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13639 81 GIVFQnpddQLFAP---TVEEDVAFG--PLNL---GLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
2.79e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlpiPE----GVN 93
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQN---PDnqfiGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13632 101 VEDDIAFGlenkKVPPKKMKDI--------IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 170 LDISHQVELLDLMRELSAEG-KTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-218 |
3.64e-32 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 117.40 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPaGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYsqLSARELAC------KVAFLPQVLPIPEGVNV 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINlppqqrKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYGrsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03297 93 RENLAFG------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492172462 175 QVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-230 |
1.11e-31 |
|
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: 123.02 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQL 97
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-TIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRsphnslwgrlSGADQHSVDQALQRMELATLAER-------PLSD----LSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG2274 569 ITLGD----------PDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 167 TTYLDISHQVELLDLMRELSAeGKTVITVLHDINQAcRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG2274 639 TSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-198 |
2.53e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.94 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 6 AQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQV 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 86 LPIPEGVNVRQLVAYGRSPHNSLWGRL---------SGADQHSVDQALQRME--------------LATL------AERP 136
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELeeleaklaePDEDLERLAELQEEFEalggweaearaeeiLSGLgfpeedLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 137 LSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIsHQVELLDlmRELSAEGKTVITVLHD 198
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLE--EFLKNYPGTVLVVSHD 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-218 |
3.62e-31 |
|
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: 117.46 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSAREL 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 76 ----ACKVAFLPQ--------VLPIpegvnvRQLVAYGRSPHnslwGRLSGADQHS-VDQALQRMELaTLAERPLSD--- 139
Cdd:COG0444 81 rkirGREIQMIFQdpmtslnpVMTV------GDQIAEPLRIH----GGLSKAEARErAIELLERVGL-PDPERRLDRyph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 -LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:COG0444 150 eLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
.
gi 492172462 218 V 218
Cdd:COG0444 230 V 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-226 |
4.45e-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: 115.03 E-value: 4.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaflpQVLPIP--- 89
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK------------------DITNLPphk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 EGVN-VRQlvAYGRSPHNSLW---------GRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03300 72 RPVNtVFQ--NYALFPHLTVFeniafglrlKKLPKAEIKErVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 159 AIVLLDEPTTYLDI----SHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:cd03300 150 KVLLLDEPLGALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-225 |
6.09e-31 |
|
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: 114.39 E-value: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 6 AQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdgKGYSQLS-ARELACKVAFLPQ 84
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVRePREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 VLPIPEGVNVRQ-LVAYGRsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03265 81 DLSVDDELTGWEnLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGD 225
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
6.10e-31 |
|
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: 112.52 E-value: 6.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFL 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQvlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
1.98e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.85 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKGYSQLSAREL 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 76 ACKVAFLPQVL-PIPEgVNVRQLVAYGRSphnslWGRLSGAD---QHSVDQALQRMEL-ATLAER---PLSDLSGGQRQR 147
Cdd:PRK14247 81 RRRVQMVFQIPnPIPN-LSIFENVALGLK-----LNRLVKSKkelQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
.
gi 492172462 228 T 228
Cdd:PRK14247 234 T 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
1.07e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYG----ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-- 74
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 75 LACKVAFLPQVlpipegvNVRQLVAYGRsphnslwgRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWL 150
Cdd:COG4525 81 VFQKDALLPWL-------NVLDNVAFGL--------RLRGVPKAErrarAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDI----SHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRLV 218
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQR---TGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-239 |
1.14e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.77 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAFLPQVLPIPEGV 92
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQ-LVAYGRsphnslWGRLSGADQHSVDQALqrMELATL---AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK13536 130 TVREnLLVFGR------YFGMSTREIEAVIPSL--LEFARLeskADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVH 239
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIY 272
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-218 |
1.21e-29 |
|
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: 111.14 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQLV 98
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRSPHNSL----WGRLSGADQHSVDQA--LQRMelatLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03245 99 TLGAPLADDErilrAAELAGVTDFVNKHPngLDLQ----IGERGRG-LSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 173 SHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRLV 218
Cdd:cd03245 174 NSEERLKERLRQL-LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-217 |
1.55e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 109.23 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipegvNVrQL 97
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ--------DD-EL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 vaygrsphnslwgrLSGadqhsvdqalqrmelaTLAErplSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:cd03246 88 --------------FSG----------------SIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492172462 178 LLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRL 217
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
2.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKV 79
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFlpqVLPIPE----GVNVRQLVAYG----RSPHNSLwgrlsgadQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13636 85 GM---VFQDPDnqlfSASVYQDVSFGavnlKLPEDEV--------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-221 |
3.04e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipE 90
Cdd:COG1132 348 SYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ-----D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GV----NVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAERpLSD------------LSGGQRQRAWLAMIL 154
Cdd:COG1132 423 TFlfsgTIRENIRYGR----------PDATDEEVEEAAKAAQAHEFIEA-LPDgydtvvgergvnLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQAcRYADHLAVMQGGRLVTCG 221
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
3.68e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckv 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVLPIPE----GVNVRQLVAYGrsPHNslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:PRK13652 78 KFVGLVFQNPDdqifSPTVEQDIAFG--PIN--LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
4.69e-29 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 109.19 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL--------ACKVAFlpqvlpip 89
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghrnAMKPAL-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 egvNVRQLVAYgrsphnslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13539 89 ---TVAENLEF--------WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*...
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-218 |
6.04e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 108.84 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA--RELACKV-- 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalRRIGALIea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 -AFLPQVLpipegvnvrqlvayGRSpHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03268 81 pGFYPNLT--------------ARE-NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-228 |
7.48e-29 |
|
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: 112.12 E-value: 7.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgYSQLSARELackvaFLPqvlpiPE----GV---- 92
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARGI-----FLP-----PHrrriGYvfqe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 -------NVRQLVAYGRsphnslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:COG4148 86 arlfphlSVRGNLLYGR------KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
1.71e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 106.63 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYG--ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSArELACKVAF 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQvlpipegvnvrqlvaygrSPHnsLWGrlsgadqhsvdqalqrmelATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03247 80 LNQ------------------RPY--LFD-------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDInQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
2.03e-28 |
|
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: 107.64 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 23 SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckVAFLPQVLPIPEGVNVRQLVAYGR 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP--VSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 103 SPhnSLwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLM 182
Cdd:TIGR01277 96 HP--GL--KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 492172462 183 RELSAEGK-TVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-221 |
2.23e-28 |
|
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: 107.74 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKgysQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYgrSPHNSLWGRLSGA--DQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03234 98 VRETLTY--TAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLH----DInqaCRYADHLAVMQGGRLVTCG 221
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
3.97e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqlsarelackva 80
Cdd:COG4161 1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 fLPQVLPIPEGVNVRQLVA-----YGRSPHNSLWGRLSGA--------DQHSVDQA---LQRMELATLAER-PLSdLSGG 143
Cdd:COG4161 68 -FSQKPSEKAIRLLRQKVGmvfqqYNLWPHLTVMENLIEApckvlglsKEQAREKAmklLARLRLTDKADRfPLH-LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 144 QRQRAWLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDpeITAQV--VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-217 |
5.19e-28 |
|
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: 106.46 E-value: 5.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA--RELACKVAF 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQ---------VLpipEGVNVRQLVAYGRSPHNslwgrlsgADQHSVdQALQRMELATLAERPLSDLSGGQRQRAWLAM 152
Cdd:cd03262 81 VFQqfnlfphltVL---ENITLAPIKVKGMSKAE--------AEERAL-ELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-218 |
6.25e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 6.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKGysqlsarelaCKVAFL 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET----------VKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVL-PIPEGVNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMelatL-----AERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:COG0488 384 DQHQeELDPDKTVLDELRDGA----------PGGTEQEVRGYLGRF----LfsgddAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELsaEGkTVITVLHDinqacRY-----ADHLAVMQGGRLV 218
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-227 |
8.20e-28 |
|
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: 111.38 E-value: 8.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGv 92
Cdd:COG4618 342 GSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAygrsphnslwgRLSGADQHSVDQAlqrmelATLA-------------ERPLSD----LSGGQRQRAWLAMILA 155
Cdd:COG4618 421 TIAENIA-----------RFGDADPEKVVAA------AKLAgvhemilrlpdgyDTRIGEggarLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-227 |
1.39e-27 |
|
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: 105.88 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVAFLPQVLPIPEGVNVRQLV 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRSphNSLWGRLSgaDQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVEL 178
Cdd:cd03299 93 AYGLK--KRKVDKKE--IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492172462 179 LDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03299 169 REELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-228 |
1.72e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.95 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysqLSARELACKVAFLPQvlpiPEGV 92
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPKVDERLIRQ----EAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYgrsPH-----NSLWG--RLSGAD-QHSVDQALQRMELATLAER----PlSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK09493 82 VFQQFYLF---PHltaleNVMFGplRVRGASkEEAEKQARELLAKVGLAERahhyP-SELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-226 |
1.82e-27 |
|
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: 105.68 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-VAFL 82
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQvlpipeGvnvRQLVAYGRSPHNSLWG--RLSGADQHSVDQALQRME-LATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:TIGR03410 81 PQ------G---REIFPRLTVEENLLTGlaALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-227 |
1.94e-27 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 105.78 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 8 HLDIGYGATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---KGYSQLSARElacKVAFLP 83
Cdd:cd03253 5 NVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRR---AIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 Q--VLpipegVN--VRqlvaygrspHNSLWGRLSGADQHSVDQA--------LQRMELA---TLAERPLSdLSGGQRQRA 148
Cdd:cd03253 82 QdtVL-----FNdtIG---------YNIRYGRPDATDEEVIEAAkaaqihdkIMRFPDGydtIVGERGLK-LSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-199 |
2.00e-27 |
|
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: 110.26 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 26 PPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---------KG------YSQLSARELacKVAFLPQ-VLPIP 89
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkrfRGtelqdyFKKLANGEI--KVAHKPQyVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 EGV--NVRQLvaygrsphnslwgrLSGADQH-SVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG1245 174 KVFkgTVREL--------------LEKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDI 199
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
2.59e-27 |
|
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: 109.77 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGA----TRIVQDLSFSPPAGQVTALIGPNGCGKS----TLLKAFARILTPQSGSLSLDGKGYSQLSA 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 73 RELaCKV-----AFLPQ--------VLPIpegvnVRQlVAYGRSPHnslwGRLSGAdqhsvdQALQRM-ELATL-----A 133
Cdd:COG4172 84 REL-RRIrgnriAMIFQepmtslnpLHTI-----GKQ-IAEVLRLH----RGLSGA------AARARAlELLERvgipdP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 134 ERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADH 208
Cdd:COG4172 147 ERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADR 226
|
250 260
....*....|....*....|.
gi 492172462 209 LAVMQGGRLVTCGAPGDVLTA 229
Cdd:COG4172 227 VAVMRQGEIVEQGPTAELFAA 247
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-230 |
3.27e-27 |
|
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: 105.01 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 7 QHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQ 84
Cdd:cd03251 4 KNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 VLPIPEGvNVRQLVAYGRsphnslwgrlSGADQHSVDQALQR-------MEL-----ATLAERPlSDLSGGQRQRAWLAM 152
Cdd:cd03251 84 DVFLFND-TVAENIAYGR----------PGATREEVEEAARAanahefiMELpegydTVIGERG-VKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-221 |
4.77e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqLSARELACKVA 80
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLpipeGVNVRQlvaYGRSPHNSLWGRLSGA--------DQHSVDQA---LQRMELATLAER-PLSdLSGGQRQRA 148
Cdd:PRK11124 79 ELRRNV----GMVFQQ---YNLWPHLTVQQNLIEApcrvlglsKDQALARAeklLERLRLKPYADRfPLH-LSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeITAQI--VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-234 |
4.97e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 23 SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS-ARElacKVAFLPQVLPIPEGVNVRQLVAYG 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpSRR---PVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPhnSLwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDL 181
Cdd:PRK10771 96 LNP--GL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 182 MRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVTCGApgdvlTAELVCQ 234
Cdd:PRK10771 172 VSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP-----TDELLSG 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-226 |
6.63e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGS---LSLDGKGYSQLSARELA 76
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 CKVAFlpqVLPIPE----GVNVRQLVAYG----RSPHNSLwgrlsgadQHSVDQALQRMELATLAERPLSDLSGGQRQRA 148
Cdd:PRK13640 84 EKVGI---VFQNPDnqfvGATVGDDVAFGlenrAVPRPEM--------IKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-224 |
7.51e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.59 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElackVAF 81
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE----IPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLpipeGV---------------NVR-QLVAYGRSPHnslwgrlsgADQHSVDQALQRMELATLAERPLSDLSGGQR 145
Cdd:COG2884 77 LRRRI----GVvfqdfrllpdrtvyeNVAlPLRVTGKSRK---------EIRRRVREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPG 224
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-218 |
9.30e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.07 E-value: 9.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQVLP-IPEgVNV 94
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHlVPE-MTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYGRSPHNSLWGRLSGADQHSVDQaLQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQ-LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK11288 176 IEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-229 |
1.47e-26 |
|
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: 108.03 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQLV 98
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYG-TLRDNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRsPHnslwgrlsgADQHSVDQALQRMELATLA-------ERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR03375 560 ALGA-PY---------ADDEEILRAAELAGVTEFVrrhpdglDMQIGErgrsLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 168 TYLDISHQVELLDLMRELSAeGKTVITVLHDiNQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR03375 630 SAMDNRSEERFKDRLKRWLA-GKTLVLVTHR-TSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-229 |
1.93e-26 |
|
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: 103.04 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackVAFLPQVLPIPEG 91
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKEL---RKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 VN------VRQLVAYgrsPHnSLWGrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03258 91 FNllssrtVFENVAL---PL-EIAG-VPKAEIEErVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
2.06e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:PRK13648 6 SIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFlpqVLPIPE----GVNVRQLVAYGRSPHNslwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13648 86 GI---VFQNPDnqfvGSIVKYDVAFGLENHA-----VPYDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-227 |
2.83e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL-DGKGYSQLSARELACKVAFLPQVLPIPEGV- 92
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 ---NVRQLVAYGrsPHNslwgrLSGADQHSVDQALQRMELATLA----ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK13643 98 feeTVLKDVAFG--PQN-----FGIPKEKAEKIAAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-228 |
3.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.76 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGY----SQLSARELACKVAFlpqVLPIPEGV---- 92
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSL---VFQFPEAQlfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYGrsPHNslwgrLSGADQHSVDQALQRMELATLAERPLS----DLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK13641 102 TVLKDVEFG--PKN-----FGFSEDEAKEKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-229 |
3.23e-26 |
|
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: 106.66 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRSPHNS---LWGRLSGAdqHSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:TIGR01842 409 AENIARFGENADPEkiiEAAKLAGV--HELILRLPDGYDTVIGPGG-ATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 171 DISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR01842 486 DEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-199 |
4.30e-26 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 106.43 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 26 PPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---------KG------YSQLSARELacKVAFLPQ-VLPIP 89
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlkrfRGtelqnyFKKLYNGEI--KVVHKPQyVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 EGV--NVRQLvaygrsphnslwgrLSGADQHSV-DQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK13409 174 KVFkgKVREL--------------LKKVDERGKlDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 492172462 167 TTYLDISHQVELLDLMRELsAEGKTVITVLHDI 199
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-198 |
5.48e-26 |
|
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: 105.91 E-value: 5.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVlPIPEGVNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAERpLSD------------LSGGQRQRAWL 150
Cdd:TIGR02868 415 AQD-AHLFDTTVRENLRLAR----------PDATDEELWAALERVGLADWLRA-LPDgldtvlgeggarLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHD 198
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-210 |
5.68e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKGY--SQLSAREL 75
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 76 ACKVAFLPQVlPIPEGVNVRQLVAYGrSPHNSLWGRLSGADQHSVDQALQRMELA-TLAERPLSdLSGGQRQRAWLAMIL 154
Cdd:PRK14243 90 RRRIGMVFQK-PNPFPKSIYDNIAYG-ARINGYKGDMDELVERSLRQAALWDEVKdKLKQSGLS-LSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINQACRYADHLA 210
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
6.05e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.06 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQvlpipegvnvrqlvaygrSPH---NSLWGRLSGADQHSVD----QALQRMELATLAE-------------RPlsdLS 141
Cdd:PRK11160 419 VSQ------------------RVHlfsATLRDNLLLAAPNASDealiEVLQQVGLEKLLEddkglnawlgeggRQ---LS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 142 GGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQG 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-232 |
6.30e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQVLPIPEG 91
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 VNVRQLVAYGRSPHNSLWGRLSGADQHsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:COG3845 95 LTVAENIVLGLEPTKGGRLDRKAARAR-IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:COG3845 174 PQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELA 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-199 |
9.84e-26 |
|
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: 101.67 E-value: 9.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 25 SPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLS--------LDGKGYSQL-----SARELACKVAFLPQ-VLPIPE 90
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeiLDEFRGSELqnyftKLLEGDVKVIVKPQyVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GV--NVRQLvaygrsphnslwgrLSGADQ-HSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:cd03236 102 AVkgKVGEL--------------LKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|..
gi 492172462 168 TYLDISHQVELLDLMRELSAEGKTVITVLHDI 199
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-227 |
1.14e-25 |
|
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: 103.27 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqlSARELAC------KVAFLPQVLPIPEGVNV 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFlppekrRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYGRSphnslwgRLSGADQHSVDQALQRM-ELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:TIGR02142 93 RGNLRYGMK-------RARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 174 HQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-223 |
1.30e-25 |
|
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: 102.57 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 34 LIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLpIPEgVNVRQLVAYGRsphnslwgRLS 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYAL-FPH-MTVEENVAFGL--------KMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 114 GADQHSVD----QALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS----HQVELLDLMREL 185
Cdd:TIGR01187 71 KVPRAEIKprvlEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 492172462 186 saeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:TIGR01187 151 ---GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-221 |
1.43e-25 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.02 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFlpQVLPIPEGV 92
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF--QNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYGRsphnslwgRLSGADQHSVDQALQR----MELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03301 88 TVYDNIAFGL--------KLRKVPKDEIDERVREvaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 169 YLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03301 160 NLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-229 |
1.53e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---------GY-SQLSARElackvaflpqvl 86
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelgaGFhPELTGRE------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 pipegvNVRqlvaygrsphnsLWGRLSGADQHSVDQALQRM-ELATLAE---RPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1134 108 ------NIY------------LNGRLLGLSRKEIDEKFDEIvEFAELGDfidQPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-226 |
1.85e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLpIPEgVNVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK11607 99 SYAL-FPH-MTVEQNIAFGlkqdKLPKAEIASR--------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 159 AIVLLDEPTTYLDIS----HQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK11607 169 KLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-227 |
2.09e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElacKVAFL 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLpIPeGVNVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK11248 78 NEGL-LP-WRNVQDNVAFGL----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGrlvtcgaPGDVL 227
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVV 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-217 |
2.13e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 99.85 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNV 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYG--RSPHNSLWGRLSGADQHSVDQALQRmELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03248 105 QDNIAYGlqSCSFECVKEAAQKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492172462 173 SHQVELLDLMRElSAEGKTVITVLHDINQACRyADHLAVMQGGRL 217
Cdd:cd03248 184 ESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-256 |
2.51e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.85 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPPAgqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG--YSQLSARELACKVAflpQVLPIPEG----VNVR 95
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLLALRQQVA---TVFQDPEQqifyTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYgrSPHNslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:PRK13638 97 SDIAF--SLRN--LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 176 VELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT-AELVCQ-------VFDVHVQImrepv 247
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQagltqpwLVKLHTQL----- 247
|
....*....
gi 492172462 248 aGTPMCIVE 256
Cdd:PRK13638 248 -GLPLCKTE 255
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-227 |
2.64e-25 |
|
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: 99.61 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPE 90
Cdd:cd03254 11 SYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GvNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAERpL------------SDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03254 91 G-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFIMK-LpngydtvlgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-227 |
4.13e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.00 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlsaRELACkvafl 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL---RDLYA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 pqvLPIPE---------GVnVRQLVAYGRSPHNSLWG----RLSGA-DQH------SVDQALQRMELAtlAERpLSDL-- 140
Cdd:PRK11701 78 ---LSEAErrrllrtewGF-VHQHPRDGLRMQVSAGGnigeRLMAVgARHygdiraTAGDWLERVEID--AAR-IDDLpt 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 --SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK11701 151 tfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|
gi 492172462 218 VTCGAPGDVL 227
Cdd:PRK11701 231 VESGLTDQVL 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-229 |
5.68e-25 |
|
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: 103.23 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGY-----------GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGKGYSQLS 71
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 72 ARELackvafLP-----QVlpipegV------------NVRQLVAYGRSPHNSlwgRLSGADQHS-VDQALQRMEL-ATL 132
Cdd:COG4172 354 RRAL------RPlrrrmQV------VfqdpfgslsprmTVGQIIAEGLRVHGP---GLSAAERRArVAEALEEVGLdPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 133 AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDInQACRY-ADHLA 210
Cdd:COG4172 419 RHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDL-AVVRAlAHRVM 497
|
250
....*....|....*....
gi 492172462 211 VMQGGRLVTCGAPGDVLTA 229
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDA 516
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-225 |
6.10e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 98.32 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSARELacKVA 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR--RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIPEGVNVRQLVAYGrsphnsLWGRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLA-MILAQDA 158
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFA------LPPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLrALLAEPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 159 AiVLLDEPTTYLDISHQVELLDLMRE-LSAEGKTVITVLHDINqacryadhlAVMQGGRLVTCGAPGD 225
Cdd:COG4136 154 A-LLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEE---------DAPAAGRVLDLGNWQH 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-218 |
8.38e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.56 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK-GYSQlsARELACKVAFL----PQV---LPIPE 90
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKR--RKKFLRRIGVVfgqkTQLwwdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GVNVRQLVaYGRSPhnslwgrlsGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03267 115 SFYLLAAI-YDLPP---------ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492172462 171 DISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03267 185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-218 |
1.19e-24 |
|
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: 98.38 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQL 97
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSPhnslwgrlsgADQHSVDQALQR-------MELA----TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:cd03249 97 IRYGKPD----------ATDEEVEEAAKKanihdfiMSLPdgydTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 167 TTYLD-ISHQV--ELLDLMRelsaEGKTVITVLHDINqACRYADHLAVMQGGRLV 218
Cdd:cd03249 167 TSALDaESEKLvqEALDRAM----KGRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
1.51e-24 |
|
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: 95.21 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLP 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QvlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSaegKTVITVLHD---INQAC 203
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYP---GTVILVSHDryfLDQVA 134
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-221 |
1.99e-24 |
|
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: 96.47 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKgysQLSARELACKVAFLPQvlpip 89
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 egvnvrqlvaygrspHNSLWGRLSgadqhsVDQALQrmeLAtlAErpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:cd03213 90 ---------------DDILHPTLT------VRETLM---FA--AK--LRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLH----DINQACryaDHLAVMQGGRLVTCG 221
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHqpssEIFELF---DKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-226 |
2.39e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA----RELACKVAFlpqVLPIPEGV 92
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGL---VFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 ----NVRQLVAYGrsPHNSlwgrlsGADQHSVdQALQRMELA------TLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13649 98 lfeeTVLKDVAFG--PQNF------GVSQEEA-EALAREKLAlvgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-221 |
2.41e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKG-YS-QLSAREL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNiYSpRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 76 ACKVAFLPQvLPIPEGVNVRQLVAYGRsphnslwgRLSGA-DQHSVDQALQR-MELATLAER---PLSD----LSGGQRQ 146
Cdd:PRK14239 85 RKEIGMVFQ-QPNPFPMSIYENVVYGL--------RLKGIkDKQVLDEAVEKsLKGASIWDEvkdRLHDsalgLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLD-ISH-QVE--LLDLMRELsaegkTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDpISAgKIEetLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-218 |
3.64e-24 |
|
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: 96.65 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC----KVAFLPQVLPIPE 90
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GVNVRQLVAYgrsPhnSLWGRLSGADQHSVDQA-LQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:TIGR02211 97 DFTALENVAM---P--LLIGKKSVKEAKERAYEmLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492172462 170 LDISHQVELLDLMRELSAEGKT-VITVLHDINQACRyADHLAVMQGGRLV 218
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKK-LDRVLEMKDGQLF 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-226 |
3.98e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL------DGKGYSQLsaRELACKVAFlpqVLPI 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL--KPLRKKVGI---VFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 89 PEgvnvRQL--------VAYGrsPHNSlwgrlsGAdqhSVDQALQR----MELATLAERPLS----DLSGGQRQRAWLAM 152
Cdd:PRK13634 94 PE----HQLfeetvekdICFG--PMNF------GV---SEEDAKQKaremIELVGLPEELLArspfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-199 |
5.09e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.65 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgkgysqlsarelaCKVAFLPQVLPIPEGVNVRQL-----VAYGRS 103
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDLlrsitDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 104 PHNSlwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMR 183
Cdd:PRK13409 432 YYKS--------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170
....*....|....*..
gi 492172462 184 ELSAE-GKTVITVLHDI 199
Cdd:PRK13409 498 RIAEErEATALVVDHDI 514
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-229 |
5.96e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK------GYSQLSARELACKVAFL-PQVLPIPE 90
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVfQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 gVNVRQLVAYGRSPHNSLWGRlsgADQHSVDQALQRM----ELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK14246 105 -LSIYDNIAYPLKSHGIKEKR---EIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 167 TTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-221 |
7.94e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQL 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYG--RSPHNSLwgrLSGADQHSVDQALQRME--LATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:TIGR00958 575 IAYGltDTPDEEI---MAAAKAANAHDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492172462 174 HQVELLDLMrelSAEGKTVITVLHDInQACRYADHLAVMQGGRLVTCG 221
Cdd:TIGR00958 652 CEQLLQESR---SRASRTVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-232 |
1.66e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS---ARELACKVAFlpQVLPIP 89
Cdd:PRK09700 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGIIY--QELSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 EGVNVRQLVAYGRSPHNSLWGrLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK09700 93 DELTVLENLYIGRHLTKKVCG-VNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-221 |
4.19e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.52 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ-----SGSLSLDGKG-YS-QLSARELA 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiYSpDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 CKVAFLPQVL-PIPEgVNVRQLVAYGRSPHNSLWGRlsGADQHSVDQALQRMELATLAERPLSD----LSGGQRQRAWLA 151
Cdd:PRK14267 85 REVGMVFQYPnPFPH-LTIYDNVAIGVKLNGLVKSK--KELDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-202 |
4.71e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVlPIPEGVNVRQLVAYgrsPhnslWG-RLSGADQHSVDQALQRMELA-TLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK10247 87 AQT-PTLFGDTVYDNLIF---P----WQiRNQQPDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHD---INQA 202
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDkdeINHA 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-214 |
5.07e-23 |
|
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: 94.01 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelacKVAFLPQVLPIPEGVNVRQLvaygrsphnsL 108
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD------------TVSYKPQYIKADYEGTVRDL----------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 WGRLSGADQHS--VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS 186
Cdd:cd03237 83 SSITKDFYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*....
gi 492172462 187 AEG-KTVITVLHDINQACRYADHLAVMQG 214
Cdd:cd03237 163 ENNeKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-199 |
6.72e-23 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 97.55 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgkgysqlsarelaCKVAFLPQVLPIPEGVNVRQLV--AYGRSPHN 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYISPDYDGTVEEFLrsANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 107 SLWgrlsgadQHSVdqaLQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS 186
Cdd:COG1245 433 SYY-------KTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
170
....*....|....
gi 492172462 187 AE-GKTVITVLHDI 199
Cdd:COG1245 503 ENrGKTAMVVDHDI 516
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-227 |
7.78e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA----CKVAFLPQVLPIPEGVNV 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYGRSphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK10070 124 LDNTAFGME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 175 QVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK10070 200 RTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-223 |
9.77e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaFLPQVLPIPEGV 92
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---------------RMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 N-VRQlvAYGRSPHNSL-----WG-RLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11000 78 GmVFQ--SYALYPHLSVaenmsFGlKLAGAKkeeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 162 LLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-227 |
1.09e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.12 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGVNVRQLvaygrsphnsLWGRLSGADQHSVDQALQRMELATLAER-PL----------SDLSGGQRQRAWLA 151
Cdd:TIGR01193 554 PQEPYIFSGSILENL----------LLGAKENVSQDEIWAACEIAEIKDDIENmPLgyqtelseegSSISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMreLSAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVL 227
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-226 |
1.21e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.96 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSIlKAQHLDIGYG-----ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYS--QLSAR 73
Cdd:PRK13637 1 MSI-KIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 74 ELACKVAFlpqVLPIPEgvnvRQL--------VAYGrsPHNslwgrLSGADQHSVDQALQRMELA-----TLAERPLSDL 140
Cdd:PRK13637 80 DIRKKVGL---VFQYPE----YQLfeetiekdIAFG--PIN-----LGLSEEEIENRVKRAMNIVgldyeDYKDKSPFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVT 219
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
....*..
gi 492172462 220 CGAPGDV 226
Cdd:PRK13637 226 QGTPREV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-236 |
1.31e-22 |
|
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: 92.61 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-VAFL 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGVNVRQ---LVAYGRsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIR--------GLSKKEREEkLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLD-ISHQvELLDLMRELSAEGktvITVL---HDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQ-DIQKIIKILKDRG---IGVLitdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRK 228
|
..
gi 492172462 235 VF 236
Cdd:cd03218 229 VY 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-221 |
3.01e-22 |
|
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: 91.44 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---------GY-SQLSARElackvaflpqvl 86
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllglggGFnPELTGRE------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 pipegvNVRqlvaygrsphnsLWGRLSGADQHSVDQALQRM-ELATLAE---RPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03220 104 ------NIY------------LNGRLLGLSRKEIDEKIDEIiEFSELGDfidLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-226 |
3.05e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.24 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVA 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLpIPEgVNVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK09452 92 FQSYAL-FPH-MTVFENVAFGlrmqKTPAAEITPR--------VMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 157 DAAIVLLDEPTTYLDI----SHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK09452 162 KPKVLLLDESLSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-228 |
3.31e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.58 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLK--AFARILtpQSGSLSLDGKGYSQLSARELAC-KVAFLPQVLpip 89
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSliAGARKI--QQGRVEVLGGDMADARHRRAVCpRIAYMPQGL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 eGVN------VRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:NF033858 86 -GKNlyptlsVFENLDF--------FGRLFGQDAAErrrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLD-ISHQV--ELLDLMRElSAEGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAPGDVLT 228
Cdd:NF033858 157 LLILDEPTTGVDpLSRRQfwELIDRIRA-ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-225 |
3.42e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.63 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS--ARELaCKV----AFLPQvL 86
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRDI-CMVfqsyALFPH-M 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 PIPEGvnvrqlVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK11432 94 SLGEN------VGYGL----KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 167 TTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGD 225
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-228 |
5.02e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.06 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGY---------GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 72 ARElacKVAFLPQVLPI----PEGVNVRQLV-AYGRSPHNSLWGrLSGADQ-HSVDQALQRMELA-TLAERPLSDLSGGQ 144
Cdd:PRK10419 81 RAQ---RKAFRRDIQMVfqdsISAVNPRKTVrEIIREPLRHLLS-LDKAERlARASEMLRAVDLDdSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 145 RQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTV-ITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
....*
gi 492172462 224 GDVLT 228
Cdd:PRK10419 237 GDKLT 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-198 |
1.04e-21 |
|
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: 89.77 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KVAFLPQVLPIPEGVNVRQL 97
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRsphnslwgRLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:cd03292 99 VAFAL--------EVTGVPpreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180
....*....|....*....|....*
gi 492172462 174 HQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-236 |
1.07e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.34 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-V 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQvlpipEGVNVRQLVAYgrsphNSLWGRLS-----GADQHSvDQALQRME---LATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK10895 81 GYLPQ-----EASIFRRLSVY-----DNLMAVLQirddlSAEQRE-DRANELMEefhIEHLRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAEL 231
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
....*
gi 492172462 232 VCQVF 236
Cdd:PRK10895 230 VKRVY 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-218 |
1.09e-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: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL---SARELACKVAFLPQvlPIPEGVNV 94
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQ--DSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLV-AYGRSPHNSLwGRLSGADQHSVDQALQRM-EL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:TIGR02769 104 RMTVrQIIGEPLRHL-TSLDESEQKARIAELLDMvGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492172462 172 ISHQVELLDLMRELSAEGKTV-ITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-229 |
1.10e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 94.01 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRI--VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLPIPEGvNVRQLVAYGRsphnslwgrLSGADQHSVDQALQRMELATLAER-PL----------SDLSGGQRQRAWL 150
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGR---------TEQADRAEIERALAAAYAQDFVDKlPLgldtpigengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-216 |
1.78e-21 |
|
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: 89.07 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIPEGvNVRQL 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGrSPHNSLWGRlsgadqhSV------DQALQRME---LATLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03250 86 ILFG-KPFDEERYE-------KVikacalEPDLEILPdgdLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492172462 169 YLDiSHQVELL--DLMRELSAEGKTVITVLHDInQACRYADHLAVMQGGR 216
Cdd:cd03250 157 AVD-AHVGRHIfeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-197 |
2.51e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 88.57 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLsARELACKVAFLP 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVaygrsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:TIGR01189 80 HLPGLKPELSALENL--------HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-227 |
2.94e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlpipEGV 92
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQL----RLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYgrsPHNSLWGRLSG--------------ADQHSVDQALQRMELATLAERPL----SDLSGGQRQRAWLAMIL 154
Cdd:PRK10619 91 RTRLTMVF---QHFNLWSHMTVlenvmeapiqvlglSKQEARERAVKYLAKVGIDERAQgkypVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-229 |
7.04e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.60 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTP----QSGSLSLDGKGY--SQLSARELAC-----KVAFLPqvl 86
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapCALRGRKIATimqnpRSAFNP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 pipegvnVRQLVAYGRSPHNSLwGRLSgadqhSVDQALQRMELATLAE--RPLS----DLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK10418 95 -------LHTMHTHARETCLAL-GKPA-----DDATLTAALEAVGLENaaRVLKlypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-226 |
1.08e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYS---------------------QLSARELAC 77
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwdirnkagmvfqnpdnQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQVLPI-PEGVNVRqlvaygrsphnslwgrlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK13633 106 DVAFGPENLGIpPEEIRER------------------------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-217 |
1.36e-20 |
|
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: 85.95 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGatriVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAF 81
Cdd:cd03215 4 VLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LP---------QVLPIPEGVNVRQLvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAM 152
Cdd:cd03215 80 VPedrkreglvLDLSVAENIALSSL------------------------------------------LSGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-230 |
1.39e-20 |
|
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: 87.54 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 7 QHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqlsareLACKVAFLPQ 84
Cdd:cd03252 4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA------LADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 VlpipeGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQR-------MEL-----ATLAERPLSdLSGGQRQRAWLAM 152
Cdd:cd03252 78 V-----GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLagahdfiSELpegydTIVGEQGAG-LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-228 |
1.42e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.98 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KVAFlpqvlpIPE 90
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrKIGM------IFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GVN------VRQLVAYgrsphnSLwgRLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:COG1135 90 HFNllssrtVAENVAL------PL--EIAGVPkaeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 161 VLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHD---INQACryaDHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1135 162 LLCDEATSALDpeTTRSI--LDLLKDINRElGLTIVLITHEmdvVRRIC---DRVAVLENGRIVEQGPVLDVFA 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-218 |
1.65e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLdigyGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAF 81
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LP---------QVLPIPEGVNVRQLVAYGRsphnslWGRLSGADQHS-VDQALQRMELATL-AERPLSDLSGGQRQRAWL 150
Cdd:COG1129 332 VPedrkgeglvLDLSIRENITLASLDRLSR------GGLLDRRRERAlAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-226 |
1.69e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.30 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG-KGYSQLSARELACKVAFLPQVLPIPEGV----N 93
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKRIGMVFQFPESQlfedT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGrsPHNSlwgrlsGADQHSV-DQALQR-MELA----TLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PRK13646 103 VEREIIFG--PKNF------KMNLDEVkNYAHRLlMDLGfsrdVMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 168 TYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-223 |
2.13e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.51 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KVAFLPQVLPIPE 90
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 GVNVRQLVAYGRSPHNslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK11831 98 DMNVFDNVAYPLREHT----QLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 170 LD-ISHQVeLLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:PRK11831 174 QDpITMGV-LVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
3.51e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.52 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDI-GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILtPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGvNVRQLVAYGRSphnslwgrlsGADQHSVDQALQRMELATLAER-------PLSD----LSGGQRQRAWLA 151
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLLGNP----------DASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 152 MILAQDAAIVLLDEPTTYLDiSHQVELldLMRELS--AEGKTVITVLHDINQACRYaDHLAVMQGGRLVTCG 221
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLD-AHSEQL--VMQALNaaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
14-218 |
5.89e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.09 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckvAFLPQVLPI---PE 90
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELR---PLRRRMQMVfqdPY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 G-VN----VRQLVAYGRSPHnslwGRLSGAD-QHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:COG4608 106 AsLNprmtVGDIIAEPLRIH----GLASKAErRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINqACRY-ADHLAVMQGGRLV 218
Cdd:COG4608 182 DEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS-VVRHiSDRVAVMYLGKIV 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-221 |
6.45e-20 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 88.65 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipEGV----N 93
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQ-----ENVlfsrS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRS----PHNSLWGRLSGAdqHSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:TIGR01846 547 IRDNIALCNPgapfEHVIHAAKLAGA--HDFISELPQGYNTEVGEKG-ANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492172462 170 LDISHQVELLDLMRELSAeGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:TIGR01846 624 LDYESEALIMRNMREICR-GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESG 673
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-223 |
7.88e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFlpqVLPIPE----GVN 93
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGM---VFQNPDnqfvGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13650 99 VEDDVAFGLEnkgiPHEEMKER--------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 170 LDISHQVELLDLMRELSAE-GKTVITVLHDINQACrYADHLAVMQGGRLVTCGAP 223
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-222 |
1.07e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLS--------LDGKGYSQLSAR 73
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShiellgrtVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 74 ELACKVAFLPQVLPIPEGVNVRQLVAYGRSPHNSLWGR----LSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAW 149
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA-EGKTVITVLHDINQACRYADHLAVMQGGRLVTCGA 222
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-197 |
1.95e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGysqlsarelacKVAFLPQVLPIPEGvNVR 95
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLG-TLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYgrsPHnslwgrlsGADQHS---VDQALQRMELATLAERpLSD-------LSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:COG4178 444 EALLY---PA--------TAEAFSdaeLREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGkTVITVLH 197
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGT-TVISVGH 542
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-230 |
1.97e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGAT-----RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKGYSQLSARELAC 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQvlPIPEGVNVRQLVAY-GRSPHNSLWGRLSGAD---------QHSVDQA------LQRMEL-ATLAERPLSDL 140
Cdd:PRK13631 100 ITNPYSK--KIKNFKELRRRVSMvFQFPEYQLFKDTIEKDimfgpvalgVKKSEAKklakfyLNKMGLdDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTC 220
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|
gi 492172462 221 GAPGDVLTAE 230
Cdd:PRK13631 258 GTPYEIFTDQ 267
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-248 |
1.98e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSldgKGYSQLS-ARE---LACKVAFLpqvLPI 88
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---AGTAPLAeAREdtrLMFQDARL---LPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 89 PEgvnVRQLVAYGrsphnslwgrLSGadqHSVDQALQRMELATLAER----PLSdLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:PRK11247 96 KK---VIDNVGLG----------LKG---QWRDAALQALAAVGLADRanewPAA-LSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL---VTCGAP-----GDVLTAELVCQV 235
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLPrprrrGSARLAELEAEV 238
|
250
....*....|...
gi 492172462 236 FDvhvQIMREPVA 248
Cdd:PRK11247 239 LQ---RVMSRGES 248
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-235 |
2.38e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDL---SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFlpqVLPIPE----GVNVRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13642 84 GM---VFQNPDnqfvGATVEDDVAFGMEnqgiPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVL-TA 229
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFaTS 231
|
....*.
gi 492172462 230 ELVCQV 235
Cdd:PRK13642 232 EDMVEI 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
3.87e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKA-QHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSldgkgysqlsaRELACKV 79
Cdd:PRK09544 1 MTSLVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVL----PIPEGVnvrqlvaygrsphnSLWGRLS-GADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK09544 70 GYVPQKLyldtTLPLTV--------------NRFLRLRpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDI 199
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-221 |
3.94e-19 |
|
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: 86.41 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 7 QHLDIGYGATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---KGYSQLSARElacKVAFL 82
Cdd:COG5265 361 ENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASLRA---AIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQ--VLpipegVN--VRQLVAYGRSphnslwgrlsGADQHSVDQALQRMEL-----------ATL-AERPLSdLSGGQRQ 146
Cdd:COG5265 438 PQdtVL-----FNdtIAYNIAYGRP----------DASEEEVEAAARAAQIhdfieslpdgyDTRvGERGLK-LSGGEKQ 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHdinqacR-----YADHLAVMQGGRLVTCG 221
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH------RlstivDADEILVLEAGRIVERG 574
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-221 |
4.17e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTP-----QSGSLSLDGKG-YSQLSARELAC 77
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSiFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQvLPIPEGVNVRQLVAYGRSPHNslwgRLSGADQHSVDQA-LQRMELATLAERPLSD----LSGGQRQRAWLAM 152
Cdd:PRK14271 102 RVGMLFQ-RPNPFPMSIMDNVLAGVRAHK----LVPRKEFRGVAQArLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLAR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-218 |
4.55e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.60 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckvAFLPQV----------- 85
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA---KYIGRVfqdpmmgtaps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 86 LPIPEgvNVrqLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELAtLAER---PLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1101 97 MTIEE--NL--ALAYRRGKRRGLRRGLTKKRRELFRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 163 LDEPTTYLD--ISHQVelLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:COG1101 172 LDEHTAALDpkTAALV--LELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-232 |
4.70e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.87 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS---ARELAckV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG--I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVLPIPEGVNVRQLVAYGRSPHNslwgrlsgADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPKRQ--------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-197 |
7.48e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.77 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSArELACKVAFLP 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVLPIPEGVNVRQLVAYgrsphnslWGRLSGADQhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03231 80 HAPGIKTTLSVLENLRF--------WHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-226 |
1.68e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.35 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLpIPEgVN 93
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYAL-YPH-MS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRsphnslwgRLSGADQHSVDQ----ALQRMELATLAERPLSDLSGGQRQRawLAMILA--QDAAIVLLDEPT 167
Cdd:PRK11650 93 VRENMAYGL--------KIRGMPKAEIEErvaeAARILELEPLLDRKPRELSGGQRQR--VAMGRAivREPAVFLFDEPL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 168 TYLD----ISHQVELLDLMRELSAegkTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK11650 163 SNLDaklrVQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-221 |
1.92e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.09 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDL---SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---GYSQLSARELACKVaflpqvl 86
Cdd:PRK11308 22 FKPERLVKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllKADPEAQKLLRQKI------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 pipegvnvrQLVAygRSPHNSLWGR----------------LSGADQhsVDQALQRMELATL----AERPLSDLSGGQRQ 146
Cdd:PRK11308 95 ---------QIVF--QNPYGSLNPRkkvgqileepllintsLSAAER--REKALAMMAKVGLrpehYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-200 |
1.99e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.83 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaflpqvlpIP---EGVNVR 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----------------------VPfkrRKEFAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QL-VAYG-RSphnSLWGRLSGAD----------------QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:COG4586 96 RIgVVFGqRS---QLWWDLPAIDsfrllkaiyripdaeyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTviTVL---HDIN 200
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGT--TILltsHDMD 216
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-229 |
2.53e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.77 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAflpqvlpipegv 92
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPA------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYgRS------PHNSLWGRLS------GADQH----SVDQALQRMElATLAERPLSD--------LSGGQRQRA 148
Cdd:COG4598 86 DRRQLQRI-RTrlgmvfQSFNLWSHMTvlenviEAPVHvlgrPKAEAIERAE-ALLAKVGLADkrdaypahLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
.
gi 492172462 229 A 229
Cdd:COG4598 244 N 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-227 |
3.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL---DGKGYSQLSARELAC--------KVAFLPQVLPIP 89
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLeklviqktRFKKIKKIKEIR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 90 EGVNV------RQL-------------VAYGRSPhnslwgrlsgadQHSVDQALQRMELATLAERPLS----DLSGGQRQ 146
Cdd:PRK13651 105 RRVGVvfqfaeYQLfeqtiekdiifgpVSMGVSK------------EEAKKRAAKYIELVGLDESYLQrspfELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
.
gi 492172462 227 L 227
Cdd:PRK13651 253 L 253
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
10-218 |
3.71e-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: 83.45 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 10 DIGYGATRI----VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQV 85
Cdd:TIGR03796 482 NITFGYSPLepplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 86 LPIPEGvNVRQLVaygrsphnSLWGR------LSGADQ----HSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILA 155
Cdd:TIGR03796 562 IFLFEG-TVRDNL--------TLWDPtipdadLVRACKdaaiHDVITSRPGGYDAELAEGG-ANLSGGQRQRLEIARALV 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 156 QDAAIVLLDEPTTYLDIshQVELLdLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRLV 218
Cdd:TIGR03796 632 RNPSILILDEATSALDP--ETEKI-IDDNLRRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVV 690
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-240 |
3.83e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.54 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckvAFLPQVLPIPEGVN----- 93
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR---KARRQIGMIFQHFNllssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 -VRQLVAygrsphnsLWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK11153 98 tVFDNVA--------LPLELAGTPKAEikarVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 169 YLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV-------LTAELVCQVFDVHV 240
Cdd:PRK11153 170 ALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVfshpkhpLTREFIQSTLHLDL 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
4.10e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGK----GYS----QLSAREL 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRveffNQNiyerRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 76 ACKVAFL---PQVLPIpegvNVRQLVAYGRS-----PHNSLWGRLSGA--DQHSVDQALQRMELATLaerplsDLSGGQR 145
Cdd:PRK14258 87 RRQVSMVhpkPNLFPM----SVYDNVAYGVKivgwrPKLEIDDIVESAlkDADLWDEIKHKIHKSAL------DLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLD------ISHQVELLDLMRELsaegkTVITVLHDINQACRYADHLAVMQG----- 214
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL-----TMVIVSHNLHQVSRLSDFTAFFKGnenri 231
|
250
....*....|....
gi 492172462 215 GRLVTCGAPGDVLT 228
Cdd:PRK14258 232 GQLVEFGLTKKIFN 245
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-230 |
5.01e-18 |
|
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: 83.08 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYG--ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLkafaRIL----TPQSGSLSLDGKGYSQLSARELAc 77
Cdd:TIGR03797 452 IEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVR- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 kvaflpqvlpipegvnvRQL---VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAE----RPL----------SDL 140
Cdd:TIGR03797 527 -----------------RQLgvvLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEdiraMPMgmhtviseggGTL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAegkTVITVLHDINqACRYADHLAVMQGGRLVTC 220
Cdd:TIGR03797 590 SGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV---TRIVIAHRLS-TIRNADRIYVLDAGRVVQQ 665
|
250
....*....|
gi 492172462 221 GAPGDVLTAE 230
Cdd:TIGR03797 666 GTYDELMARE 675
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-228 |
5.07e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSL---SLDGKGYSQLSA-RELACKVAFLPQVLPIpeGVNVRQLVAYGrsP 104
Cdd:PRK13644 28 GEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGiRKLVGIVFQNPETQFV--GRTVEEDLAFG--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 105 HNSLWGRLSgaDQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRE 184
Cdd:PRK13644 104 ENLCLPPIE--IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492172462 185 LSAEGKTVITVLHDINQaCRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK13644 182 LHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
14-216 |
6.07e-18 |
|
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: 80.17 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRI--VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG----YSQLSARELackVA------- 80
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREI---LAlrrrtig 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 ----FLpQVLPipeGVNVRQLVAygrsphNSLwgRLSGADQhsvDQALQRME--LATL--AERpLSDL-----SGGQRQR 147
Cdd:COG4778 97 yvsqFL-RVIP---RVSALDVVA------EPL--LERGVDR---EEARARARelLARLnlPER-LWDLppatfSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-215 |
7.10e-18 |
|
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: 79.82 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackVAFlpQVLPIPEGVNVRQLV 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVF--QNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRsphNSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR01184 76 ALAV---DRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 492172462 178 LLD-LMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:TIGR01184 153 LQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-235 |
1.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSppAGQVTALIGPNGCGKSTLLKAFARILTPQSG-SLSLDGKGYSQL----SARELACKVAFlpqVLPIPE----G 91
Cdd:PRK13645 31 SLTFK--KNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLkkikEVKRLRKEIGL---VFQFPEyqlfQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 VNVRQLVAYGrsPHNSlwgrlsGADQHSVDQAL-QRMELATL----AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK13645 106 ETIEKDIAFG--PVNL------GENKQEAYKKVpELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 167 TTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT-AELVCQV 235
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSnQELLTKI 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-218 |
2.12e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGY---GATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARIL-TPQ----SGSLSLDGKGYSQLS 71
Cdd:PRK15134 3 QPLLAIENLSVAFrqqQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 72 AREL----ACKVAF------------------LPQVLPIPEGVnvRQLVAYGRSphnslwgrLSGADQHSVDQALQRmel 129
Cdd:PRK15134 83 EQTLrgvrGNKIAMifqepmvslnplhtlekqLYEVLSLHRGM--RREAARGEI--------LNCLDRVGIRQAAKR--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 130 atLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADH 208
Cdd:PRK15134 150 --LTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADR 226
|
250
....*....|
gi 492172462 209 LAVMQGGRLV 218
Cdd:PRK15134 227 VAVMQNGRCV 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-217 |
2.86e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC----KVAFLPQ---VLP- 87
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQfhhLLPd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 88 --IPEGVNVRQLVAyGRSPHNSlwgrlsgadQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK11629 102 ftALENVAMPLLIG-KKKPAEI---------NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492172462 166 PTTYLDISHQVELLDLMRELSA-EGKTVITVLHDINQACRYADHLAvMQGGRL 217
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-223 |
3.33e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 77.45 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGA--TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHsvdqalqrmelatlaerplSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGG-------------------LNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAP 223
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
3.49e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS----AREla 76
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrARL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 cKVAFLPQVLPIPEGVNVRQ---LVAYGRsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAM 152
Cdd:COG1137 79 -GIGYLPQEASIFRKLTVEDnilAVLELR--------KLSKKEREErLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 153 ILAQDAAIVLLDEPTTYLD-IShqV-ELLDLMRELSAEGktvITVL---HDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpIA--VaDIQKIIRHLKERG---IGVLitdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
....*....
gi 492172462 228 TAELVCQVF 236
Cdd:COG1137 225 NNPLVRKVY 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-219 |
3.52e-17 |
|
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: 77.86 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHL----DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS----AR 73
Cdd:COG4181 7 PIIELRGLtktvGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 74 ELACKVAFLPQ--------------VLPIpEGVNVRQlvAYGRSphnslwgrlsgadqhsvDQALQRMELATLAE-RPlS 138
Cdd:COG4181 87 LRARHVGFVFQsfqllptltalenvMLPL-ELAGRRD--ARARA-----------------RALLERVGLGHRLDhYP-A 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 139 DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRyADHLAVMQGG 215
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQI--IDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
....
gi 492172462 216 RLVT 219
Cdd:COG4181 223 RLVE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-172 |
4.73e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 80.36 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKgysqlsarelACKVAFL 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE----------TVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQvlpipegvnvrqlvayGRS---PHNSLWGRLSGADQHSVdqaLQRMELATLA------------ERPLSDLSGGQRQR 147
Cdd:TIGR03719 391 DQ----------------SRDaldPNKTVWEEISGGLDIIK---LGKREIPSRAyvgrfnfkgsdqQKKVGQLSGGERNR 451
|
170 180
....*....|....*....|....*
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-218 |
5.47e-17 |
|
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: 79.84 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELAckvAFlpqvlpipegvnvRQLVA- 99
Cdd:COG4615 352 DLTIRR--GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNRE---AY-------------RQLFSa 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 100 ----YgrspH--NSLWGRLSGADQHSVDQALQRMELA---TLAERPLS--DLSGGQRQRawLAMILA--QDAAIVLLDE- 165
Cdd:COG4615 411 vfsdF----HlfDRLLGLDGEADPARARELLERLELDhkvSVEDGRFSttDLSQGQRKR--LALLVAllEDRPILVFDEw 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 166 -----PtTYLDISHQvELLDLMRelsAEGKTVITVLHDInqacRY---ADHLAVMQGGRLV 218
Cdd:COG4615 485 aadqdP-EFRRVFYT-ELLPELK---ARGKTVIAISHDD----RYfdlADRVLKMDYGKLV 536
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-221 |
5.49e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.87 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQSGSL-----SLDGK---GYSQLSARELACKVAFLPQ---VLP-- 87
Cdd:PRK11264 23 DLEVKP--GEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArslSQQKGLIRQLRQHVGFVFQnfnLFPhr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 88 -----IPEG-VNVR-----QLVAYGRsphnslwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK11264 101 tvlenIIEGpVIVKgepkeEATARAR-------------------ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-223 |
6.38e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.15 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQ- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQD-PVLFSGTIRSn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 97 LVAYGRSPHNSLWgrlsgadqhsvdQALQRMELATLAERPL-----------SDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:cd03244 98 LDPFGEYSDEELW------------QALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 166 PTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAP 223
Cdd:cd03244 166 ATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-226 |
6.81e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKvafl 82
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 pqvlpipeGV-----NVR----------QLVAYGRSPHNSLwgrLSG---------ADQHSVDQA---LQRMELATLAER 135
Cdd:PRK11300 81 --------GVvrtfqHVRlfremtvienLLVAQHQQLKTGL---FSGllktpafrrAESEALDRAatwLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 136 PLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQG 214
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250
....*....|..
gi 492172462 215 GRLVTCGAPGDV 226
Cdd:PRK11300 230 GTPLANGTPEEI 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-230 |
7.97e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---------------GYSQLSARElackVAFLP 83
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgmAYITESRRD----NGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 QVlpipegvNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLA------ERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK09700 355 NF-------SIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLAlkchsvNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-221 |
1.19e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIP-EGVNVRQL 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSPHNSLWGRLSG-ADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGkAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492172462 176 VELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK10261 500 GQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-221 |
1.54e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.85 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL--ACKVAFLPQVLpipeg 91
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLrrNIAVVFQDAGL----- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 vnvrqlvaYGRSPHNSLW-GRLSGADQHSVD-----QALQRME-----LATLA-ERPLSdLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK13657 421 --------FNRSIEDNIRvGRPDATDEEMRAaaeraQAHDFIErkpdgYDTVVgERGRQ-LSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-218 |
3.32e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQSGSLSLDGKGYSQLSARELACK---VAFlPQVLPIPeG 91
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAgifLAF-QYPVEIP-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 VNVRQLVaygRSPHNSLWG-RLSGADQHS-VDQALQRMEL-ATLAERPL-SDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:COG0396 92 VSVSNFL---RTALNARRGeELSAREFLKlLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 168 TYLDI-SHQVeLLDLMRELSAEGKT--VIT----VLHDINqacryADHLAVMQGGRLV 218
Cdd:COG0396 169 SGLDIdALRI-VAEGVNKLRSPDRGilIIThyqrILDYIK-----PDFVHVLVDGRIV 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-223 |
3.96e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.13 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 30 QVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGY-SQLSArelackvaflpqvlpipegvnVRQlvAYGRSP-HNS 107
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA---------------------VRQ--SLGMCPqHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 108 LWGRLSGADQ---------HSVDQALQRMElATLAERPL--------SDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:TIGR01257 1014 LFHHLTVAEHilfyaqlkgRSWEEAQLEME-AMLEDTGLhhkrneeaQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492172462 171 DISHQVELLDLMRELSAeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-198 |
8.53e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.69 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC----KVAFLPQ--- 84
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQryh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 VLP-IPEGVNVRQLVAYGRSPHNSlwgRLSGADQhsvdqALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10535 97 LLShLTAAQNVEVPAVYAGLERKQ---RLLRAQE-----LLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190
....*....|....*....|....*....|....*
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-227 |
1.85e-15 |
|
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: 75.61 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLD-GKGYSQLSARELACK---- 78
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRgrak 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 79 --VAFLPQvlpipegvnvrqlvAYGRSPHNSLWGRLSGA------DQHSVDQALQRMELATLAE--------RPLSDLSG 142
Cdd:TIGR03269 365 ryIGILHQ--------------EYDLYPHRTVLDNLTEAiglelpDELARMKAVITLKMVGFDEekaeeildKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 143 GQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD-LMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*.
gi 492172462 222 APGDVL 227
Cdd:TIGR03269 511 DPEEIV 516
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-223 |
2.90e-15 |
|
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: 73.06 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA-----RIltpQSGSLSLDGKGYSQLSARELACK 78
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpsyEV---TSGTILFKGQDLLELEPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 79 VAFLPQVLP--IPeGVNVRQLVaygRSPHNSlwgRLSGADQHSVD---------QALQRMEL-ATLAERPLSD-LSGGQR 145
Cdd:TIGR01978 78 GLFLAFQYPeeIP-GVSNLEFL---RSALNA---RRSARGEEPLDlldfekllkEKLALLDMdEEFLNRSVNEgFSGGEK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRY--ADHLAVMQGGRLVTCGAP 223
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY-QRLLNYikPDYVHVLLDGRIVKSGDV 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-217 |
3.20e-15 |
|
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: 74.86 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHL---DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKA-FARILTPQSGSLSLDGKGYSQLS-ARELAC 77
Cdd:TIGR02633 257 ILEARNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAlFGAYPGKFEGNVFINGKPVDIRNpAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQ---------VLPIPEGVNVRQLVAYgrsphnSLWGRL-SGADQHSVDQALQRMELATLA-ERPLSDLSGGQRQ 146
Cdd:TIGR02633 337 GIAMVPEdrkrhgivpILGVGKNITLSVLKSF------CFKMRIdAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-198 |
3.51e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPI--PEGvNVR 95
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----------LEVAYFDQHRAEldPEK-TVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYGRSPHNslwgrLSGADQHsVDQALQ-------RmelatlAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK11147 402 DNLAEGKQEVM-----VNGRPRH-VLGYLQdflfhpkR------AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 492172462 169 YLDIshqvELLDLMRELSAEGK-TVITVLHD 198
Cdd:PRK11147 470 DLDV----ETLELLEELLDSYQgTVLLVSHD 496
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-197 |
3.74e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPIPEGvNVR 95
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPYLPLG-TLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYgrsPhnslWGRLsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:cd03223 82 EQLIY---P----WDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|..
gi 492172462 176 VELLDLMRELSAegkTVITVLH 197
Cdd:cd03223 128 DRLYQLLKELGI---TVISVGH 146
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-224 |
6.99e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTP---QSGSLSLDGKgysQLSARELACKVAFLPQV-LPIP-----EGVNVRQLVA 99
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDdLFIPtltvrEHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 100 YGRSPHNSlwGRlsgadQHSVDQALQRMELATLA------ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD-- 171
Cdd:TIGR00955 128 MPRRVTKK--EK-----RERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsf 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 172 ISHQVelLDLMRELSAEGKTVITVLHD-INQACRYADHLAVMQGGRLVTCGAPG 224
Cdd:TIGR00955 201 MAYSV--VQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-172 |
1.04e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL-------------------- 62
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqsrdaldpnk 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 63 -------DGKGYSQLSARElackvaflpqvlpipegVNVRqlvAY-GRspHNslwgrLSGADQhsvdqalqrmelatlaE 134
Cdd:PRK11819 404 tvweeisGGLDIIKVGNRE-----------------IPSR---AYvGR--FN-----FKGGDQ----------------Q 440
|
170 180 190
....*....|....*....|....*....|....*...
gi 492172462 135 RPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:PRK11819 441 KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-214 |
1.10e-14 |
|
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: 69.91 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysqlsarelaCKVAFLPQVLpipegvnvrqlvaygrsphnsl 108
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------ITPVYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 wgrlsgadqhsvdqalqrmelatlaerplsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE 188
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*..
gi 492172462 189 G-KTVITVLHDINQACRYADHLAVMQG 214
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-221 |
1.18e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 70.63 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 L-PQVLPIPEGVNVRQLVaygrsphnslwgrlsgadqhsvdqalqrmelatlaeRPLSD-LSGGQRQRAWLAMILAQDAA 159
Cdd:cd03217 81 LaFQYPPEIPGVKNADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH-----DINQacryADHLAVMQGGRLVTCG 221
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-176 |
1.27e-14 |
|
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: 73.41 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQsGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRSPHNSLWGRLSGADQHSV-DQALQRMELAtlaerpLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:TIGR01271 1309 RKNLDPYEQWSDEEIWKVAEEVGLKSViEQFPDKLDFV------LVDggyvLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
....*....
gi 492172462 169 YLD-ISHQV 176
Cdd:TIGR01271 1383 HLDpVTLQI 1391
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-231 |
1.99e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKVAF------------LPQ 84
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplHFGDYSYRSQRIRMIFqdpstslnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 85 VLPIPEGVNVrQLVAYGRsphnslwgrlsgadQHSVDQALQRMELatlaerpLSD--------LSGGQRQRAWLAMILAQ 156
Cdd:PRK15112 109 ILDFPLRLNT-DLEPEQR--------------EKQIIETLRQVGL-------LPDhasyyphmLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAEL 231
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
2.17e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL-SARELACKV 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVLPIPEGVNVRQLVAYGrsphnslwGRLsgADQHSVDQALQRME--LATLAERPLS---DLSGGQRQRAWLAMIL 154
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG--------GFF--AERDQFQERIKWVYelFPRLHERRIQragTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-226 |
4.36e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.91 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKST-------LLKAFARIltpqSGSLSLDGKGYSQ 69
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRI----GGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 70 LSAREL----ACKVAFLPQ------------------VLPIPEGVNVRQlvAYGRSphnslwgrLSGADQHSVDQALQRM 127
Cdd:PRK09473 86 LPEKELnklrAEQISMIFQdpmtslnpymrvgeqlmeVLMLHKGMSKAE--AFEES--------VRMLDAVKMPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 128 ELATlaerplSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYA 206
Cdd:PRK09473 156 KMYP------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGIC 229
|
250 260
....*....|....*....|
gi 492172462 207 DHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK09473 230 DKVLVMYAGRTMEYGNARDV 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-230 |
4.68e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDigygATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFL 82
Cdd:PRK11288 258 LRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 P---------QVLPIPEGVNVrqlvayGRSPHNSLWGRL--SGADQHSVDQALQRMELATL-AERPLSDLSGGQRQRAWL 150
Cdd:PRK11288 334 PedrkaegiiPVHSVADNINI------SARRHHLRAGCLinNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVtcgapGDVLTAE 230
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQ 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-216 |
5.20e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILtPQ---SGSLSLDGKGYSQLSARELACK- 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 79 VAFLPQVLPIPEGVNVRQLVAYGRSPHNSlwGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPG--GIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-185 |
5.80e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQsGSLSLDGKGYSQLSAREL-----ACKVAFLPQVLPIPEGV 92
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvrhRIQVVFQDPNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVAYGRSPHNSlwgRLSGADQHS-VDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:PRK15134 380 NVLQIIEEGLRVHQP---TLSAAQREQqVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170
....*....|....*
gi 492172462 171 DISHQVELLDLMREL 185
Cdd:PRK15134 457 DKTVQAQILALLKSL 471
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-218 |
7.48e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 28 AGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGY-------SQLSA-----RELAckvaFLPQvLPIPEGVNVr 95
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpksSQEAGigiihQELN----LIPQ-LTIAENIFL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 qlvayGRSPHNSlWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK10762 103 -----GREFVNR-FGRIDWKKMYAeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492172462 175 QVELLDLMRELSAEGKTVITVLH---DINQACryaDHLAVMQGGRLV 218
Cdd:PRK10762 177 TESLFRVIRELKSQGRGIVYISHrlkEIFEIC---DDVTVFRDGQFI 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-217 |
7.96e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQ-------VLPIPEGV 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEdrqssglYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 93 NVRQLVaYGRsphNSLWGRlSGADQHSVDQALQRMELA-TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK15439 361 NVCALT-HNR---RGFWIK-PARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-218 |
1.06e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElackVAF 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE----VPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LpqvlpipegvnvRQLVAYGRSPHNSLWGR-----------LSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQ 146
Cdd:PRK10908 77 L------------RRQIGMIFQDHHLLMDRtvydnvaipliIAGASgddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-227 |
1.32e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.05 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 20 QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---KGYSQLSARElacKVAFLPQvlpipegvNVRQ 96
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRN---QVALVSQ--------NVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 97 L-------VAYGRSPHNSLWGRLSGADQ-HSVDqALQRME--LATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK11176 429 FndtiannIAYARTEQYSREQIEEAARMaYAMD-FINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 167 TTYLDISHQVELLDLMRELSAEgKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK11176 508 TSALDTESERAIQAALDELQKN-RTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-198 |
1.40e-13 |
|
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: 66.61 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPagQVTALIGPNGCGKSTLLKAFARILTPQSgslsldgkgysqlsarelackvaflpQVLPIPEGVNVRQ 96
Cdd:cd03227 11 FVPNDVTFGEG--SLTIITGPNGSGKSTILDAIGLALGGAQ--------------------------SATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 97 LVAYgrsphnslwgrlsgadqhsvdqalQRMELATLaerpLSDLSGGQRQRAWLAMILA----QDAAIVLLDEPTTYLDI 172
Cdd:cd03227 63 IVAA------------------------VSAELIFT----RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180
....*....|....*....|....*.
gi 492172462 173 SHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-215 |
1.55e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK----VAFLPQVlPIPEGVNV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK-PWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYGrSPHNSLWGRL---SGADQHSVDqALQRMELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03290 96 EENITFG-SPFNKQRYKAvtdACSLQPDID-LLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 172 ISHQVELLD--LMRELSAEGKTVITVLHDInQACRYADHLAVMQGG 215
Cdd:cd03290 173 IHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
28-219 |
1.72e-13 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 69.60 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 28 AGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackvaflpqvlpipegvnvRQLVAYGRSPHNs 107
Cdd:TIGR01194 367 QGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDY-------------------RDLFSAIFADFH- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 108 LWGRLSGAD---QHSVDQA---LQRMELA------TLAERPLSDLSGGQRQRawLAMILA--QDAAIVLLDEPTTYLDIS 173
Cdd:TIGR01194 427 LFDDLIGPDegeHASLDNAqqyLQRLEIAdkvkieDGGFSTTTALSTGQQKR--LALICAwlEDRPILLFDEWAADQDPA 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492172462 174 -HQVELLDLMRELSAEGKTVITVLHDiNQACRYADHLAVMQGGRLVT 219
Cdd:TIGR01194 505 fKRFFYEELLPDLKRQGKTIIIISHD-DQYFELADQIIKLAAGCIVK 550
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
1.79e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHL---DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKA-FARILTPQSGSLSLDGKGYSQLSARE-LAC 77
Cdd:PRK13549 259 ILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQClFGAYPGRWEGEIFIDGKPVKIRNPQQaIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQ-------VLPIPEGVNVrQLVAYGRSphnSLWGRL-SGADQHSVDQALQRMELATL-AERPLSDLSGGQRQRA 148
Cdd:PRK13549 339 GIAMVPEdrkrdgiVPVMGVGKNI-TLAALDRF---TGGSRIdDAAELKTILESIQRLKVKTAsPELAIARLSGGNQQKA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-214 |
2.10e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLD--IGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS----AR 73
Cdd:PRK10584 5 NIVEVHHLKksVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 74 ELACKVAFLPQVLPIPEGVNVRQLVaygrsphnSLWGRLSG-ADQHSVDQALQRMELATLAER----PlSDLSGGQRQRA 148
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENV--------ELPALLRGeSSRQSRNGAKALLEQLGLGKRldhlP-AQLSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQG 214
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-205 |
2.96e-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: 69.19 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgKGYsqlsarelacKVAFLPQVLPIPEGVNVRQLVAYG 101
Cdd:TIGR03719 26 LSFFP--GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGI----------KVGYLPQEPQLDPTKTVRENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPHNSLWGRLS----------------------------GADQHSVDQalqRMELATLAER------PLSDLSGGQRQR 147
Cdd:TIGR03719 93 VAEIKDALDRFNeisakyaepdadfdklaaeqaelqeiidAADAWDLDS---QLEIAMDALRcppwdaDVTKLSGGERRR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDiSHQVELLDlmRELSAEGKTVITVLHDinqacRY 205
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPGTVVAVTHD-----RY 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-229 |
3.38e-13 |
|
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: 69.20 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQL 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSPHNSLWGRLSGADQHSVDQALQ---RMELATLAErplsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPdklDHECAEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 175 QvELLDLMRELSAEGKTVITVLHDINQACRYAdHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR00957 1457 D-NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-176 |
7.43e-13 |
|
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: 66.80 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQsGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAYGRSPHNSLWGRLSGADQHSV-DQALQRMELAtlaerpLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03289 94 RKNLDPYGKWSDEEIWKVAEEVGLKSViEQFPGQLDFV------LVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
....*....
gi 492172462 169 YLD-ISHQV 176
Cdd:cd03289 168 HLDpITYQV 176
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-197 |
7.54e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysQLSARELAC---KV 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER----QSIKKDLCTyqkQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVLPIPEGVNVRQlvaygrsphNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK13540 77 CFVGHRSGINPYLTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-222 |
8.70e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTpQSGSLSLDGKGYSQLSARELackVAFLPQVLPIPEGVNVRQLV 98
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-QAGGLVQCDKMLLRRRSRQV---IELSEQSAAQMRHVRGADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRSPHNSLWGRLSGADQHS----VDQALQRMELATLAERPLS----------------DLSGGQRQRAWLAMILAQDA 158
Cdd:PRK10261 108 MIFQEPMTSLNPVFTVGEQIAesirLHQGASREEAMVEAKRMLDqvripeaqtilsryphQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGA 222
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-218 |
1.27e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILtPQ---SGSLSLDGKGYSQLSARELACK- 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 79 VAFLPQVLPIPEGVNVRQLVAYGRS-PHNSlwGRLSGADQ-HSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEiTLPG--GRMAYNAMyLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-217 |
1.89e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTllkaFARILT----PQSGSLSLDGkgysqlsarelackvaflpqvlpipEGVNVRQLVAYgRSP 104
Cdd:PRK10522 349 GELLFLIGGNGSGKST----LAMLLTglyqPQSGEILLDG-------------------------KPVTAEQPEDY-RKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 105 HNS------LWGRLSGADQHSVDQA-----LQRMELA---TLAERPLSD--LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK10522 399 FSAvftdfhLFDQLLGPEGKPANPAlvekwLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 169 YLD-----ISHQvELLDLMRELsaeGKTVITVLHDiNQACRYADHLAVMQGGRL 217
Cdd:PRK10522 479 DQDphfrrEFYQ-VLLPLLQEM---GKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-193 |
1.89e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 20 QDLSFSPPAGQVTALIGPNGCGKSTLLkafaRILT----PQSGSLSLDGKGYSQLsaRElackvAFLPQVLPI--PEGVN 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLL----RILAglarPDAGEVLWQGEPIRRQ--RD-----EYHQDLLYLghQPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 vRQLVAYgrspHNSLW-GRLSG-ADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK13538 87 -TELTAL----ENLRFyQRLHGpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|...
gi 492172462 172 iSHQVELL-DLMRELSAEGKTVI 193
Cdd:PRK13538 162 -KQGVARLeALLAQHAEQGGMVI 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-171 |
2.42e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 7 QHLDIGYGATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQV 85
Cdd:PRK10790 344 DNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 86 lPIPEGVNVRQLVAYGRSphnslwgrlsgADQHSVDQALQRMELATLAeRPLSD------------LSGGQRQRAWLAMI 153
Cdd:PRK10790 424 -PVVLADTFLANVTLGRD-----------ISEEQVWQALETVQLAELA-RSLPDglytplgeqgnnLSVGQKQLLALARV 490
|
170
....*....|....*...
gi 492172462 154 LAQDAAIVLLDEPTTYLD 171
Cdd:PRK10790 491 LVQTPQILILDEATANID 508
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-221 |
2.76e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.67 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 27 PAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARElacKVAFLPqvlpiPEGVNVRQLVAYGR-SPH 105
Cdd:PRK11144 22 PAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAE---KGICLP-----PEKRRIGYVFQDARlFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 106 NSLWGRL----SGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDL 181
Cdd:PRK11144 91 YKVRGNLrygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492172462 182 MRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11144 171 LERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-194 |
3.48e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.09 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIPEGVnVR 95
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGT-IK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYGRSphnslwgrlsgADQH---SVDQALQRME-LATLAER---PLSD----LSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:TIGR01271 505 DNIIFGLS-----------YDEYrytSVIKACQLEEdIALFPEKdktVLGEggitLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190
....*....|....*....|....*....|..
gi 492172462 165 EPTTYLDISHQVELLD--LMRELSAEGKTVIT 194
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEscLCKLMSNKTRILVT 605
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-215 |
5.14e-12 |
|
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: 65.81 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVA 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIPEGVNVRQlvaygrspHNSLWGRLSGADQHSVDQ----ALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGRE--------HLYLYARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-215 |
6.36e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.11 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIPEGVnV 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGT-I 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQLVAYGRSphnslwgrlsgADQH---SVDQALQRME-LATLAER---PLSD----LSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03291 115 KENIIFGVS-----------YDEYrykSVVKACQLEEdITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492172462 164 DEPTTYLDISHQVELLD-LMRELSAEgKTVITVLHDINQaCRYADHLAVMQGG 215
Cdd:cd03291 184 DSPFGYLDVFTEKEIFEsCVCKLMAN-KTRILVTSKMEH-LKKADKILILHEG 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-198 |
1.37e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.14 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG----YSQLSARELAckv 79
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAnigyYAQDHAYDFE--- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 aflpqvlpipEGVNVRQLVAYGRSPhnslwgrlsGADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK15064 397 ----------NDLTLFDWMSQWRQE---------GDDEQAVRGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLDIsHQVELLDLMRELsAEGkTVITVLHD 198
Cdd:PRK15064 458 NVLVMDEPTNHMDM-ESIESLNMALEK-YEG-TLIFVSHD 494
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-197 |
1.83e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 6 AQHLDIGYGA--TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiltpqsgslsldgkgysQLSARELACKVAFlp 83
Cdd:COG2401 31 LEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------ALKGTPVAGCVDV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 84 qvlpipegvnvrqlvaygrsPHNSLWGRLSGADQ----HSVDQALQRMELATLAE-----RPLSDLSGGQRQRAWLAMIL 154
Cdd:COG2401 92 --------------------PDNQFGREASLIDAigrkGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLH 197
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-233 |
2.03e-11 |
|
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: 63.81 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIpEGVNVRQLVAYG 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWI-QNDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPHNSLWGRLSGADQHSVD-QALQRMELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:TIGR00957 723 KALNEKYYQQVLEACALLPDlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 181 --LMRELSAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLT-----AELVC 233
Cdd:TIGR00957 802 hvIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQrdgafAEFLR 860
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-231 |
2.32e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDI-GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL-ACKVA 80
Cdd:COG3845 257 VLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQ-------VLPIPEGVNVrqLVAYGRSPHNSLWGRLsgaDQHSV-DQALQRME----LATLAERPLSDLSGGQRQRA 148
Cdd:COG3845 337 YIPEdrlgrglVPDMSVAENL--ILGRYRRPPFSRGGFL---DRKAIrAFAEELIEefdvRTPGPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
...
gi 492172462 229 AEL 231
Cdd:COG3845 492 EEI 494
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-217 |
2.68e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 8 HLDIGYGATRI---------VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LAC 77
Cdd:PRK10762 248 RLDKAPGEVRLkvdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQ-------VLpipeGVNVRQ---LVAYGRspHNSLWGRLSGADQH-SVDQALQRMELATLA-ERPLSDLSGGQR 145
Cdd:PRK10762 328 GIVYISEdrkrdglVL----GMSVKEnmsLTALRY--FSRAGGSLKHADEQqAVSDFIRLFNIKTPSmEQAIGLLSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
19-208 |
3.09e-11 |
|
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: 61.08 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPagqVTALIGPNGCGKSTLLKAFARILTpqsGSLSLDGKGYSQLsaRELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:cd03240 15 RSEIEFFSP---LTLIVGQNGAGKTTIIEALKYALT---GELPPNSKGGAHD--PKLIREGEVRAQVKLAFENANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYgRSPH---NSLWgrlsgadqhsVDQAlqrmELATLAERPLSDLSGGQRQ------RAWLAMILAQDAAIVLLDEPTTY 169
Cdd:cd03240 87 IT-RSLAileNVIF----------CHQG----ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492172462 170 LDISH-QVELLDLMRE-LSAEGKTVITVLHDINQAcRYADH 208
Cdd:cd03240 152 LDEENiEESLAEIIEErKSQKNFQLIVITHDEELV-DAADH 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-205 |
3.69e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPPA--GqvtaLIGPNGCGKSTLLKAFARILTPQSGSLSLDgKGYsqlsarelacKVAFLPQVLPIPEGVNVRQLV- 98
Cdd:PRK11819 28 LSFFPGAkiG----VLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGI----------KVGYLPQEPQLDPEKTVRENVe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 ------------------AYGRSPHNS---------LWGRLSGADQHSVDQalqRMELATLAER------PLSDLSGGQR 145
Cdd:PRK11819 93 egvaevkaaldrfneiyaAYAEPDADFdalaaeqgeLQEIIDAADAWDLDS---QLEIAMDALRcppwdaKVTKLSGGER 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDiSHQVELLDlmRELSAEGKTVITVLHDinqacRY 205
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--QFLHDYPGTVVAVTHD-----RY 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-227 |
3.81e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaflPQVLPIPEGVNvrqlv 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISAGLS----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 aygrsphnslwGRLSGAD----------------QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13546 98 -----------GQLTGIEniefkmlcmgfkrkeiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK13546 167 IDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-229 |
4.04e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGAT----RIVQDLSFSPPAGQVTALIGPNGCGKS-TLLKAFARILTP---QSGSLSLDGKGYSQLSA 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 73 RE----LACKVAFLPQV------------LPIPEGVNVRQlvaygrsphnslwgrlSGADQHSVDQALQRMELATLAErP 136
Cdd:PRK11022 81 KErrnlVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQ----------------GGNKKTRRQRAIDLLNQVGIPD-P 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 137 LS-------DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS-AEGKTVITVLHDINQACRYADH 208
Cdd:PRK11022 144 ASrldvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHK 223
|
250 260
....*....|....*....|.
gi 492172462 209 LAVMQGGRLVTCGAPGDVLTA 229
Cdd:PRK11022 224 IIVMYAGQVVETGKAHDIFRA 244
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-218 |
7.91e-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: 59.56 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKGYSQLSARElackVAFLPQVLPIPEGVNV 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKNFQRS----TGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 95 RQlvaygrsphnSLwgRLSGAdqhsvdqalqrmelatlaerpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03232 97 RE----------AL--RFSAL---------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQAC-RYADHLAVMQ-GGRLV 218
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKrGGKTV 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-218 |
1.23e-10 |
|
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: 58.87 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFariltpqsgslsldgkGYSQLSARELACKVAFLPQVLpipegVNVRQLv 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------------LYASGKARLISFLPKFSRNKL-----IFIDQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 aygrsphnslwgrlsgadQHSVDQALQRMELatlaERPLSDLSGGQRQRAWLAMILAQDA--AIVLLDEPTTYLDISHQV 176
Cdd:cd03238 69 ------------------QFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492172462 177 ELLDLMRELSAEGKTVITVLHDINQACrYADHLAVM------QGGRLV 218
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVV 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-221 |
1.75e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEG-----VN 93
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLAslnprMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 94 VRQLVAygrSPHNSLWGRLSGADqhsVDQALQRME-----LATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK15079 117 IGEIIA---EPLRTYHPKLSRQE---VKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 169 YLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-221 |
2.19e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 121 DQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDIN 200
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
|
90 100
....*....|....*....|.
gi 492172462 201 QACRYADHLAVMQGGRLVTCG 221
Cdd:NF000106 206 EAEQLAHELTVIDRGRVIADG 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-218 |
2.58e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQVLPIPEGVNVRQLVAYGRSPHNS 107
Cdd:PRK10982 24 HSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDNMWLGRYPTKG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 108 LWgrlsgadqhsVDQA-LQRMELATLAE--------RPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL---DISHq 175
Cdd:PRK10982 104 MF----------VDQDkMYRDTKAIFDEldididprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNH- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492172462 176 veLLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK10982 173 --LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-197 |
2.98e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFA----------------RILTPQ----SGSLSLDGKGYSQLSARE--LACKVAFLPQVL 86
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgriqgnnftgtilannRKPTKQilkrTGFVTQDDILYPHLTVREtlVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 PIPEgvnvrqlvaygrsphnslwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PLN03211 174 TKQE--------------------KILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|.
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-197 |
3.52e-10 |
|
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: 59.76 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPIPEGvNVRQL 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLG-TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSPHNSLWGRLSGADqhsVDQALQRMELATLAERPLS---------DLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKD---LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 492172462 169 ylDISHQVEllDLMRELSAE-GKTVITVLH 197
Cdd:TIGR00954 612 --AVSVDVE--GYMYRLCREfGITLFSVSH 637
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-194 |
7.63e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSlSLDGKGysqlsarelacKVAFLPQVlPIPEGVNVRQLV 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVVIRG-----------SVAYVPQV-SWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 99 AYGRSPHNSLWGRL--SGADQHSVDQALQRmELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--ISH 174
Cdd:PLN03232 700 LFGSDFESERYWRAidVTALQHDLDLLPGR-DLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahVAH 777
|
170 180
....*....|....*....|
gi 492172462 175 QVELLDLMRELSAEGKTVIT 194
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVT 797
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-194 |
1.57e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELACKVAFL 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 83 PQVLPIPEGVNVRQLVAYgrspHNSLWGRLSgadQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13543 88 GHLPGLKADLSTLENLHF----LCGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|....
gi 492172462 163 LDEPTTYLDIShQVELLDLM--RELSAEGKTVIT 194
Cdd:PRK13543 161 LDEPYANLDLE-GITLVNRMisAHLRGGGAALVT 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-172 |
1.66e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKafarILtpqSGSLSLDgKGYSQLsARELacKVA 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----IL---NGEVLLD-DGRIIY-EQDL--IVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLP----------IPEGVN-----------VRQLVAYGRSP--------------HNSLWgRLsgadQHSVDQALQ 125
Cdd:PRK11147 70 RLQQDPPrnvegtvydfVAEGIEeqaeylkryhdISHLVETDPSEknlnelaklqeqldHHNLW-QL----ENRINEVLA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492172462 126 RMELAtlAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:PRK11147 145 QLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-200 |
2.27e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdgkgysqlsarelackvaflpqvlpipegvnvrqlvaygrsphnsl 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 wgrLSGADQHSVDQALQRMELATlaeRPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD------LM 182
Cdd:smart00382 36 ---IDGEDILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170
....*....|....*...
gi 492172462 183 RELSAEGKTVITVLHDIN 200
Cdd:smart00382 110 LLKSEKNLTVILTTNDEK 127
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-198 |
2.34e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKG-----YSQLSARELAC 77
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGiklgyFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPQVLPIPEGVNVRQLVAYgrsphnsLWGRLSGADQhsVDQALQRmelatlaerplsdLSGGQRQRAWLAMILAQD 157
Cdd:PRK10636 391 DESPLQHLARLAPQELEQKLRDY-------LGGFGFQGDK--VTEETRR-------------FSGGEKARLVLALIVWQR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELsaEGKTVItVLHD 198
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVV-VSHD 486
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-232 |
2.73e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELAC--KVAFLPQVLPIPEGVNVRQ 96
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIATrrRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 97 -LVAYGRSPHnslwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWL--AMILAQDaaIVLLDEPTTYLDI 172
Cdd:NF033858 359 nLELHARLFH------LPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLavAVIHKPE--LLILDEPTSGVDP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 173 SHQVELLDLMRELSAEGKTVITV-LHDINQACRyADHLAVMQGGRLVTCGAPgdvltAELV 232
Cdd:NF033858 431 VARDMFWRLLIELSREDGVTIFIsTHFMNEAER-CDRISLMHAGRVLASDTP-----AALV 485
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-224 |
3.00e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTP---QSGSLSLDGKGYSQLSARELA-CKvaflPQVLPIPEgVNVR---QLVAYG 101
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSIGyVQ----QQDLHLPT-STVReslRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPHNslwgrLSGADQHS-VDQALQRMELATLAER----PLSDLSGGQRQRAWLAMIL-AQDAAIVLLDEPTTYLDISHQ 175
Cdd:TIGR00956 864 RQPKS-----VSKSEKMEyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQTA 938
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 176 VELLDLMRELSAEGKTVITVLH----DINQAcryADHLAVMQ-GGRLVTCGAPG 224
Cdd:TIGR00956 939 WSICKLMRKLADHGQAILCTIHqpsaILFEE---FDRLLLLQkGGQTVYFGDLG 989
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-197 |
3.23e-09 |
|
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: 56.55 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFsPPAGQVTALIGPNGCGKSTLLKAFARILTPQSG-SLSL-DGKGYSQLSARELACKVAF-------LPQVLP 87
Cdd:COG3593 12 RSIKDLSI-ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEeDFYLGDDPDLPEIEIELTFgsllsrlLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 88 IPEGVNVRQLVAYGRSPHNSLWGRLS---------GADQHSVDQALQRMELATLA-----------ERPLSDLSGGQRQR 147
Cdd:COG3593 91 EEDKEELEEALEELNEELKEALKALNellseylkeLLDGLDLELELSLDELEDLLkslslriedgkELPLDRLGSGFQRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 148 AWLAMILA-------QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:COG3593 171 ILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-227 |
3.63e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 134 ERPLSDLSGGQRQRAWLAMILAQDAAIVL--LDEPTTYLdisHQVE---LLDLMRELSAEGKTVITVLHDiNQACRYADH 208
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDnrrLINTLKRLRDLGNTLIVVEHD-EDTIRAADY 558
|
90 100
....*....|....*....|....*
gi 492172462 209 L------AVMQGGRLVTCGAPGDVL 227
Cdd:TIGR00630 559 VidigpgAGEHGGEVVASGTPEEIL 583
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-230 |
4.86e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVnvrqlVAYG 101
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGT-----VRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSP---HN--SLWGRLSGAdqHSVDqALQRMELATLAE--RPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PLN03130 1333 LDPfneHNdaDLWESLERA--HLKD-VIRRNSLGLDAEvsEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 175 QVELLDLMRElsaEGK--TVITVLHDINQA--CryaDHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PLN03130 1410 DALIQKTIRE---EFKscTMLIIAHRLNTIidC---DRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-217 |
4.89e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG----YSQLSARELACKVAFLPQVL 86
Cdd:PLN03073 517 GYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLDLSSNPLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 87 PIPEGVNVRQLVAygrspHNSLWGrLSGadqhsvdqalqrmelaTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PLN03073 597 RCFPGVPEQKLRA-----HLGSFG-VTG----------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492172462 167 TTYLDIShQVELldLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PLN03073 655 SNHLDLD-AVEA--LIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-230 |
6.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 8 HLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLP 87
Cdd:PLN03232 1241 HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 88 IPEGVNVRQLVAYgrSPHN--SLWGRLSGAdqhSVDQALQRMELATLAE--RPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PLN03232 1321 LFSGTVRFNIDPF--SEHNdaDLWEALERA---HIKDVIDRNPFGLDAEvsEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 164 DEPTTYLDISHQVELLDLMRElSAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-185 |
7.53e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 55.00 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK------------------GYS---QLSARELACKV 79
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFrkllirngefgdsaklilYYGtsrLLLDGPLKKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 80 AFLPQVLP--------IPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQ--------------RMELATL----- 132
Cdd:COG3950 97 RLKEEYFSrldgydslLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREalnkllpdfkdiriDRDPGRLvildk 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 133 --AERPLSDLSGGQRQR-AWLAMILAQDA-------------AIVLLDEPTTYLDISHQVELLDLMREL 185
Cdd:COG3950 177 ngEELPLNQLSDGERSLlALVGDLARRLAelnpalenplegeGIVLIDEIDLHLHPKWQRRILPDLRKI 245
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-223 |
1.06e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQLVayg 101
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNV--- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 rSPhnslwgrLSGADQHSVDQALqrmELATLAERPLSDLSG--------------GQRQRAWLA-MILAQDAAIVLLDEP 166
Cdd:PTZ00243 1405 -DP-------FLEASSAEVWAAL---ELVGLRERVASESEGidsrvleggsnysvGQRQLMCMArALLKKGSGFILMDEA 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 167 TTYLD--ISHQVElLDLMRELSAEgkTVITVLHDINQACRYaDHLAVMQGGRLVTCGAP 223
Cdd:PTZ00243 1474 TANIDpaLDRQIQ-ATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSP 1528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-217 |
1.07e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 34 LIGPNGCGKSTLLKAFARILTPQSGSLSLDgkgysqlsareLACKVAFLPQVLPIPEGVNVRQLVAYGrspHNSLWGRLS 113
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNERLGKLRQDQFAFEEFTVLDTVIMG---HTELWEVKQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 114 GAD------QHSVDQALQRMEL-ATLAE--------R-----------------PLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK15064 98 ERDriyalpEMSEEDGMKVADLeVKFAEmdgytaeaRagelllgvgipeeqhygLMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 162 LLDEPTTYLDIsHQVELLDlmRELSAEGKTVITVLHD---INQACryaDHLAVMQGGRL 217
Cdd:PRK15064 178 LLDEPTNNLDI-NTIRWLE--DVLNERNSTMIIISHDrhfLNSVC---THMADLDYGEL 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
29-230 |
1.43e-08 |
|
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: 54.14 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVR-QLVAYGRSPHNS 107
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD-PILFSGSIRfNLDPECKCTDDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 108 LWGRLSGADQHSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA 187
Cdd:cd03288 126 LWEALEIAQLKNMVKSLPGGLDAVVTEGG-ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA 204
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492172462 188 EgKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:cd03288 205 D-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-223 |
1.53e-08 |
|
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: 54.16 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLL-----KAFARIL--------------------------------TPQSGSLS 61
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLhlkkeqpgnhdrieglehidkvividqspigrTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 62 ldgkgYSQL--SARELACKVA----FLPQVLPipegvnvrqlVAY-GRSPHNSLwgrlsgadQHSVDQALQRME------ 128
Cdd:cd03271 91 -----YTGVfdEIRELFCEVCkgkrYNRETLE----------VRYkGKSIADVL--------DMTVEEALEFFEnipkia 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 129 --LATLAE---------RPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKT 191
Cdd:cd03271 148 rkLQTLCDvglgyiklgQPATTLSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKK---LLEVLQRLVDKGNT 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 492172462 192 VITVLHDINQAcRYADHLAVM------QGGRLVTCGAP 223
Cdd:cd03271 225 VVVIEHNLDVI-KCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-218 |
1.64e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 20 QDLSFSPPAGQVTALIGPNGCGKSTLLKafarILT---PQ---SGSLSLDG-----KGYSQLSAR-------ELAckvaF 81
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMK----VLSgvyPHgsyEGEILFDGevcrfKDIRDSEALgiviihqELA----L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 82 LPQvLPIPEGV---NVRqlvaygrsphnSLWGRLSGADQHSvdQALQRMELATLAERP---LSDLSGGQRQRAWLAMILA 155
Cdd:NF040905 90 IPY-LSIAENIflgNER-----------AKRGVIDWNETNR--RARELLAKVGLDESPdtlVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-234 |
2.95e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackvaflpqvlpipegvnvR 95
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL-------------------Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVA--YGR------SPHNSLWGRlSGAD--QHSVDQALQRMELAT------LAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK10938 77 KLVSdeWQRnntdmlSPGEDDTGR-TTAEiiQDEVKDPARCEQLAQqfgitaLLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQ 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-221 |
3.19e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.95 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQL 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-PFLFSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRsphnslwgrlSGADQHSVDQALQrmeLATLAERPLS--------------DLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10789 409 IALGR----------PDATQQEIEHVAR---LASVHDDILRlpqgydtevgergvMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-201 |
4.08e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysqlSARELACKVAFLPQVLPIpEGVNVRQLvay 100
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 101 grsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:PRK13545 112 -------MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180
....*....|....*....|.
gi 492172462 181 LMRELSAEGKTVITVLHDINQ 201
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQ 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-230 |
5.04e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElACKVAFlpqVLPIPE-------- 90
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-AINHGF---ALVTEErrstgiya 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 --GVNVRQLVAYGRSPHNSlWGRLSGADQHSVDQ-ALQRMELATLAER-PLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK10982 340 ylDIGFNSLISNIRNYKNK-VGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVtcgapGDVLTAE 230
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA-----GIVDTKT 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-198 |
5.41e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPIPEgVNVRQLVAYGRSPHNSL 108
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQETPALP-QPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 WGRLSGADQHSVDQALQ--------------RMELATLA----------ERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:PRK10636 95 EAQLHDANERNDGHAIAtihgkldaidawtiRSRAASLLhglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190
....*....|....*....|....*....|....
gi 492172462 165 EPTTYLDIShqvELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK10636 175 EPTNHLDLD---AVIWLEKWLKSYQGTLILISHD 205
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-218 |
1.36e-07 |
|
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: 50.72 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSARelaCK--VAFLPQV-LPIPEg 91
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK---YPgeIIYVSEEdVHFPT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 VNVRQLVAYGRsphnslwgRLSGADQhsvdqalqrmelatlaerpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03233 98 LTVRETLDFAL--------RCKGNEF-------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVlhDINQACR--YA--DHLAVMQGGRLV 218
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFV--SLYQASDeiYDlfDKVLVLYEGRQI 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-221 |
1.37e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA-----RILtpqSGSLSLDGKGYSQLSARELA 76
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpayKIL---EGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 77 CKVAFLPQVLP--IPeGVNVRQL--VAYgRSPHNSLwgRLSGADQHSVDQAL-QRMELATLAERPLS-----DLSGGQRQ 146
Cdd:CHL00131 83 HLGIFLAFQYPieIP-GVSNADFlrLAY-NSKRKFQ--GLPELDPLEFLEIInEKLKLVGMDPSFLSrnvneGFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 R-AWLAMILAqDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHdinqacrYA--------DHLAVMQGGRL 217
Cdd:CHL00131 159 RnEILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-------YQrlldyikpDYVHVMQNGKI 230
|
....
gi 492172462 218 VTCG 221
Cdd:CHL00131 231 IKTG 234
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
134-221 |
1.75e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.72 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 134 ERPLSDLSGGQRQRAWLAMILAQDAAIVL--LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRYADHL-- 209
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVid 210
|
90
....*....|....*.
gi 492172462 210 ----AVMQGGRLVTCG 221
Cdd:cd03270 211 igpgAGVHGGEIVAQG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-212 |
2.15e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL-DGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQ 96
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 97 LVAY------------------------GRSPHNSLWGRLSGaDQHSVDQALQRMEL----------------------- 129
Cdd:PTZ00265 479 NIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAG-DLNDMSNTTDSNELiemrknyqtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 130 ------------ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA-EGKTVITVL 196
Cdd:PTZ00265 558 ihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIA 637
|
250
....*....|....*.
gi 492172462 197 HDINqACRYADHLAVM 212
Cdd:PTZ00265 638 HRLS-TIRYANTIFVL 652
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-225 |
3.28e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLsldgkgysqLSARElackVAFLPQVLPIpegvnvrqL 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS----IAYVPQQAWI--------M 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 98 VAYGRSphNSLW------GRLSGA---DQHSVDQALQRMELAT-LAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PTZ00243 734 NATVRG--NILFfdeedaARLADAvrvSQLEADLAQLGGGLETeIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 168 TYLDiSHQVELldLMREL---SAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGD 225
Cdd:PTZ00243 811 SALD-AHVGER--VVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
119-226 |
4.01e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.80 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 119 SVDQALQRME--------LATLAE---------RPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHq 175
Cdd:COG0178 789 TVEEALEFFEnipkiarkLQTLQDvglgyiklgQPATTLSGGEAQRVKLASELSKRStgkTLYILDEPTTGLhfhDIRK- 867
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 176 veLLDLMRELSAEGKTVITVLHD---InqacRYADHLAVM------QGGRLVTCGAPGDV 226
Cdd:COG0178 868 --LLEVLHRLVDKGNTVVVIEHNldvI----KTADWIIDLgpeggdGGGEIVAEGTPEEV 921
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
19-197 |
5.43e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 49.38 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 19 VQDLSFSPPagqVTALIGPNGCGKSTLLKAFARiltpqsgSLSLDGKGYSQL-------SARELAckvaflpQVLpipeg 91
Cdd:COG3910 30 LEGLEFHPP---VTFFVGENGSGKSTLLEAIAV-------AAGFNPEGGSKNfrfstreSESALG-------EYL----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 92 vnvrQLVaygRSPHNSLWGR-LSGADQHSVDQALQRMELATLA------ERPLSDLSGGQrqrAWLAMILA--QDAAIVL 162
Cdd:COG3910 88 ----RLS---RGLPKPRDGFfLRAESFFNVATYLDELAAEGPGildsygGRSLHEQSHGE---SFLALFENrfRGNGLYL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:COG3910 158 LDEPEAALSPSRQLALLALIHDLVREGSQFIIATH 192
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-226 |
6.09e-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: 50.40 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 120 VDQALQRMELAtlaeRPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVI 193
Cdd:TIGR00630 814 CDVGLGYIRLG----QPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKK---LLEVLQRLVDKGNTVV 886
|
90 100 110
....*....|....*....|....*....|....*....
gi 492172462 194 TVLHDINqACRYADHLAVM------QGGRLVTCGAPGDV 226
Cdd:TIGR00630 887 VIEHNLD-VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-171 |
8.25e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 11 IGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKafarILT---PQ--SGSLSLDGK---------------GY--S 68
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITgdhPQgySNDLTLFGRrrgsgetiwdikkhiGYvsS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 69 QLsarELACKVAflpqvlpipegVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQR 147
Cdd:PRK10938 344 SL---HLDYRVS-----------TSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRL 409
|
170 180
....*....|....*....|....
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLD 433
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-221 |
1.07e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKGYSQLSARELACKVA 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLP--IPegvnvrqlvayGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDL---------------SGG 143
Cdd:PRK09580 81 FMAFQYPveIP-----------GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 144 QRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHdINQACRY--ADHLAVMQGGRLVTCG 221
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-229 |
2.28e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 1 MSILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARIlTPQSGSLSLDGKGYS-----QLS 71
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDdidllRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 72 ARE----LACKVAFL---PQVLPIPEGVNVRQLV-AYGRSPHNSLWGRLSGADQHSVDQALQRMEL----ATLAERPLsD 139
Cdd:PRK15093 80 PRErrklVGHNVSMIfqePQSCLDPSERVGRQLMqNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIkdhkDAMRSFPY-E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVL-HDINQACRYADHLAVMQGGRLV 218
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLIsHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|.
gi 492172462 219 TCGAPGDVLTA 229
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-224 |
3.51e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 23 SFSPpaGQVTALIGPNGCGKSTLL-------------------------KAFARIltpqSGSLSLDGKGYSQLSARELAC 77
Cdd:PLN03140 902 AFRP--GVLTALMGVSGAGKTTLMdvlagrktggyiegdirisgfpkkqETFARI----SGYCEQNDIHSPQVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 78 KVAFLPqvlpIPEGVNVRQLVAYgrsphnslwgrlsgadqhsVDQALQRMELATLAER-----PLSDLSGGQRQRAWLAM 152
Cdd:PLN03140 976 YSAFLR----LPKEVSKEEKMMF-------------------VDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAV 1032
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH----DINQAcryADHLAVMQ-GGRLVTCGAPG 224
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKrGGQVIYSGPLG 1106
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-201 |
4.34e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQS-GSLSLDGKgysqlsarelackVAFLPQVLPIPEGvNVRQLVA 99
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQVSWIFNA-TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 100 YGrSPHNSlwGRLSGA-DQHSVDQALQRM---ELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--IS 173
Cdd:PLN03130 701 FG-SPFDP--ERYERAiDVTALQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDahVG 776
|
170 180 190
....*....|....*....|....*....|.
gi 492172462 174 HQVELLDLMRELSaeGKTVITV---LHDINQ 201
Cdd:PLN03130 777 RQVFDKCIKDELR--GKTRVLVtnqLHFLSQ 805
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-227 |
5.15e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 134 ERPLSDLSGGQRQRAWLAMILAQDAAIV--LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRYADHL-- 209
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIid 549
|
90 100
....*....|....*....|..
gi 492172462 210 ----AVMQGGRLVTCGAPGDVL 227
Cdd:PRK00635 550 igpgAGIFGGEVLFNGSPREFL 571
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-198 |
5.54e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 133 AERPLSDLSGGQRQ------RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK03918 782 KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
20-68 |
7.12e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 45.56 E-value: 7.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 492172462 20 QDLSFSPPagqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYS 68
Cdd:pfam13476 12 QTIDFSKG---LTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGF 57
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
131-230 |
7.69e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 131 TLAeRPLSDLSGGQRQRAWLAmilAQdaaI------VL--LDEPTTYLdisHQ------VELLDLMRELsaeGKTVITVL 196
Cdd:PRK00349 482 TLS-RSAGTLSGGEAQRIRLA---TQ---IgsgltgVLyvLDEPSIGL---HQrdndrlIETLKHLRDL---GNTLIVVE 548
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 492172462 197 HDiNQACRYADHL------AVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK00349 549 HD-EDTIRAADYIvdigpgAGVHGGEVVASGTPEEIMKNP 587
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
81-217 |
8.38e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 81 FLPQVLPIP-EGVNVRQLVAYGRSPHNSLWgrLSGADQHSVDQALQRMELATLA-ERPLSDLSGGQRQRAWLAMIL---A 155
Cdd:PRK00635 751 FLPQVLEVRyKGKNIADILEMTAYEAEKFF--LDEPSIHEKIHALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELlapS 828
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 156 QDAAIVLLDEPTTYLDiSHQVE-LLDLMRELSAEGKTVITVLHDINqACRYADHLAVM--QGGRL 217
Cdd:PRK00635 829 KKPTLYVLDEPTTGLH-THDIKaLIYVLQSLTHQGHTVVIIEHNMH-VVKVADYVLELgpEGGNL 891
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-230 |
9.76e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 137 LSDLSGGQRQRAWLAMIL---AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDInQACRYADHLAVM- 212
Cdd:PRK00635 1697 LSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLIEMg 1775
|
90 100
....*....|....*....|...
gi 492172462 213 -----QGGRLVTCGAPGDVLTAE 230
Cdd:PRK00635 1776 pgsgkTGGKILFSGPPKDISASK 1798
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-230 |
2.47e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 131 TLAeRPLSDLSGGQRQRAWLAmilaqdAAI------VL--LDEPTTYLdisHQ---VELLDLMRELSAEGKTVITVLHDi 199
Cdd:COG0178 478 TLD-RSAGTLSGGEAQRIRLA------TQIgsglvgVLyvLDEPSIGL---HQrdnDRLIETLKRLRDLGNTVIVVEHD- 546
|
90 100 110
....*....|....*....|....*....|....*..
gi 492172462 200 NQACRYADHL------AVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG0178 547 EDTIRAADYIidigpgAGEHGGEVVAQGTPEEILKNP 583
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
119-171 |
3.36e-05 |
|
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: 44.79 E-value: 3.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 119 SVDQALQRMELATLAERPL---SDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:TIGR03269 145 AVGRAVDLIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
12-198 |
3.60e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.80 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 12 GYGATRIVQDLSFSPPAGQVTALI-GPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipe 90
Cdd:cd03279 10 NFGPFREEQVIDFTGLDNNGLFLIcGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 91 gvnvrqlvaygRSPHNSLWGRLSGADQHSVDQA--LQRMELATLAERPLSDLSGGQRQRAWLAM------ILAQDAAIVL 162
Cdd:cd03279 84 -----------LGGKKYRVERSRGLDYDQFTRIvlLPQGEFDRFLARPVSTLSGGETFLASLSLalalseVLQNRGGARL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492172462 163 ----LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03279 153 ealfIDEGFGTLDPEALEAVATALELIRTENRMVGVISHV 192
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-57 |
4.24e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 40.28 E-value: 4.24e-05
10 20 30
....*....|....*....|....*....|....*...
gi 492172462 20 QDLSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQS 57
Cdd:pfam13555 15 HTIPIDP--RGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-193 |
7.79e-05 |
|
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: 43.15 E-value: 7.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 134 ERPLSDLSGGQRQraWLAMILA-----QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:pfam13304 231 ELPAFELSDGTKR--LLALLAAllsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLI 293
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-65 |
9.52e-05 |
|
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: 42.76 E-value: 9.52e-05
10 20 30
....*....|....*....|....*....|....*
gi 492172462 31 VTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK 65
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDE 35
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
20-199 |
1.22e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 20 QDLSFSPPagqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL----PQVLPIPEGvNVR 95
Cdd:COG0419 17 ETIDFDDG---LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEhggkRYRIERRQG-EFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 96 QLVAYGRSPHNSLWGRLSGAD------------QHSVDQALQRMELATLAER----------PLSDLSGGQRQRAWLAMI 153
Cdd:COG0419 93 EFLEAKPSERKEALKRLLGLEiyeelkerlkelEEALESALEELAELQKLKQeilaqlsgldPIETLSGGERLRLALADL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492172462 154 LAqdaaiVLLDepTTYLDISHQVELLDLMRELSaegktVITvlHDI 199
Cdd:COG0419 173 LS-----LILD--FGSLDEERLERLLDALEELA-----IIT--HVI 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-199 |
1.88e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG-KTVITVLHDI 199
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRI 1419
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
29-50 |
2.05e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.23 E-value: 2.05e-04
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
140-226 |
2.25e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 LSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVITVLH--DInqaCRYADHLAV 211
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRK---LLEVLHRLVDKGNTVVVIEHnlDV---IKTADWIID 904
|
90 100
....*....|....*....|.
gi 492172462 212 M------QGGRLVTCGAPGDV 226
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPEEV 925
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
140-193 |
4.78e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 4.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 492172462 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-209 |
5.37e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 LSGGQRQ------RAWLAMILAQ----DAAI--VLLDEPTTYLD---ISHQVELLDLMRELSAEgkTVITVLHDiNQACR 204
Cdd:PRK02224 782 LSGGERAlfnlslRCAIYRLLAEgiegDAPLppLILDEPTVFLDsghVSQLVDLVESMRRLGVE--QIVVVSHD-DELVG 858
|
....*
gi 492172462 205 YADHL 209
Cdd:PRK02224 859 AADDL 863
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
20-50 |
6.32e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 6.32e-04
10 20 30
....*....|....*....|....*....|....
gi 492172462 20 QDLSFSPPA---GQVTALIGPNGCGKSTLLKAFA 50
Cdd:COG1106 17 LTLSMVASGlrlLRVNLIYGANASGKSNLLEALY 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-55 |
1.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|
gi 492172462 26 PPAGQVTALIGPNGCGKSTLLKAFARILTP 55
Cdd:COG4913 21 DFDGRGTLLTGDNGSGKSTLLDAIQTLLVP 50
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-171 |
1.69e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSldgkgYSQLSARELA---CkvAFLPQVLPIPEGVN 93
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAkpyC--TYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 94 VRQLVAYGRSPHNSLwgrlsgadqHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK13541 87 VFENLKFWSEIYNSA---------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
30-49 |
4.32e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 37.96 E-value: 4.32e-03
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
137-174 |
6.62e-03 |
|
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: 36.89 E-value: 6.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 492172462 137 LSDLSGGQRQRAWLAMILA----QDAAIVLLDEPTTYLDISH 174
Cdd:cd03273 164 LTELSGGQRSLVALSLILAlllfKPAPMYILDEVDAALDLSH 205
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-197 |
6.90e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.53 E-value: 6.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIsHQVelLDLMRELSAEGKTVITVLH 197
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAV--LWLETYLLKWPKTFIVVSH 399
|
|
|